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2 cellobiose
cellotetraose + H2O
2',4'-dinitrophenyl-beta-D-cellobiose + H2O
?
-
-
-
-
?
2,3-di-O-methylated cellulase + H2O
?
-
2,3-di-O-methylated cellulase, having a trace amount of unsubstituted glucose units is hydrolyzed. Only the linkages between glucose units and 2,3-di-O-methylated units are cleaved. No hydrolysis of 2,3-di-O-methylcellulose, having every structural unit of them regioselectively substituted
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
2,4-dinitrophenyl beta-cellotrioside + H2O
2,4-dinitrophenyl beta-cellobioside + D-glucose
cleavage occurs between the second and third sugar residues with no release of chromophore, thus no colour change
-
-
?
2,4-dinitrophenyl beta-D-cellobioside + H2O
?
2-hydroxyethyl cellulose + H2O
?
4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside + H2O
4'',6''-O-benzylidene beta-cellobioside + 2-chloro-4-nitrophenyl beta-D-glucoside
4-methylumbelliferyl beta-cellotrioside + H2O
?
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
?
-
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
4-methylumbelliferyl cellobioside + H2O
4-methylumbelliferone + cellobiose
-
-
-
?
4-methylumbelliferyl cellobioside + H2O
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside + H2O
4,6-O-(3-oxobutylidene)-beta-D-cellotriose + 4-nitrophenyl-beta-D-cellobioside
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
0.16% of the activity with carboxymethyl cellulose
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
?
7.7% of the activity with carboxymethyl cellulose
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
33.2% of the activtiy with carboxymethyl cellulose
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
33.2% of the activity with carboxymethyl cellulose
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
4-nitrophenyl cellobioside + H2O
?
-
-
-
?
4-nitrophenyl cellopentaoside + H2O
4-nitrophenol + cellopentaose
-
-
-
?
4-nitrophenyl cellotetraoside + H2O
4-nitrophenol + cellotetraose
-
-
-
?
4-nitrophenyl cellotrioside + H2O
4-nitrophenol + cellotriose
-
-
-
?
4-nitrophenyl D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl D-cellobioside + H2O
4-nitrophenol + D-cellobiose
-
-
-
?
6-chloro-4-methylumbelliferyl beta-cellobioside + H2O
6-chloro-4-methylumbelliferone + cellobiose
-
-
-
?
acid swollen cellulose + H2O
cellobiose + cellotriose
endoglucanase with exohydrolytic activity
-
-
?
acid-swollen cellulose + H2O
?
alpha-cellulose + H2O
?
-
activity of the catalytic module EG1-CM is 58% of the activity with endoglucanase 1
-
-
?
alpha-chitin + H2O
?
-
due to the binding, it seems chitin would be an inhibitor of Cel6B, Cel9A and Cel48A, but not of Cel6A and Cel5A
-
-
?
amorphic Solca Floc cellulose + H2O
?
amorphous cellulose + H2O
?
-
-
-
?
avicel + H2O
cellobiose + ?
avicel + H2O
cellobiose + cellotriose
avicel + H2O
cellobiose + glucose
-
the main product is cellobiose together with a small amount of glucose, endoglucanase 35
-
-
?
avicel + H2O
D-glucose + ?
Avicel PH-101 + H2O
?
low activity
-
-
?
azurine-labelled hydroxyethylcellulose + H2O
?
bacterial cellulose + H2O
?
bacterial microcrystalline cellulose + H2O
?
bacterial microcrystalline cellulose + H2O
cellotetraose
-
weak activity
83% cellotetraose + 11% cellotriose + 4% cellobiose
-
?
bacterial micropcrystalline cellulose + H2O
?
-
-
-
-
?
bagasse + H2O
?
-
steam-exploded bagasse
-
-
?
ball-milled cellulose + H2O
?
-
-
-
-
?
barley 1,3-1,4-beta glucan + H2O
?
-
-
-
-
?
barley beta-1,4-D-glucan + H2O
?
Thermochaetoides thermophila
best endoglucanase substrate
-
-
?
barley beta-D-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
barley beta-glucan + H2O
cellobiose + cellotriose + D-glucose
best substrate, high activity, product analysis
-
-
?
barley beta-glucan + H2O
D-glucose + ?
beta-1,4-D-glucan + H2O
?
beta-1,4-D-xylan + H2O
?
Thermochaetoides thermophila
bifunctional endoglucanase/xylanase enzyme
-
-
?
beta-D-glucan + H2O
?
Thermochaetoides thermophila
-
-
-
?
beta-glucan + H2O
cellotriose + ?
-
-
-
?
carboxymethyl cellulose + H2O
?
carboxymethyl cellulose + H2O
cellobiose + ?
carboxymethyl cellulose + H2O
cellobiose + cellooligosaccharides
-
-
-
-
?
carboxymethyl cellulose + H2O
cellobiose + cellotriose
-
substrate concentration 1%, low activity
-
-
?
carboxymethyl cellulose + H2O
cellobiose + cellotriose + ?
carboxymethyl cellulose + H2O
cellotriose + cellobiose + D-glucose
-
enzyme hydrolyzes internal beta-1,4 glycosidic bonds within lichenan as well as carboxymethyl cellulose to release oligosaccharides and glucose
major products
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
carboxymethyl cellulose + H2O
D-glucose + cellobiose + cellooligosaccharide
carboxymethyl cellulose + H2O
glucose + cellobiose + short oligomers
carboxymethyl-cellulose + H2O
?
carboxymethylcellulose + H2O
?
carboxymethylcellulose + H2O
carboxymethyl glucose + cellobiose + cellotriose
carboxymethylcellulose + H2O
cellobiose + ?
carboxymethylcellulose + H2O
cellobiose + cello-oligomer
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellooligomers
endo-beta-1,4-glucanase activity. The enzyme shows cellulase and xylanase activity
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellotriose + cellotetraose
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellotriose + cellotetraose + cellopentaose
carboxymethylcellulose + H2O
D-glucose + ?
carboxymethylcellulose + H2O
short glucose oligomers + cellobiose + glucose
carboxymethylpachyman + H2O
?
-
cellulase I
-
-
?
carob bean gum + H2O
?
-
-
-
?
cello-oligosaccharide + H2O
?
-
insoluble cello-oligosaccharide average degree of polymerization 34 and soluble cello-oligosaccharides longer than cellotriose
-
-
?
cellobiose + H2O
2 D-glucose
cellobioside + H2O
?
-
about 2% of the activity with barley beta-glucan
-
-
?
cellohexaitol + H2O
?
-
-
-
-
?
cellohexaose + 5 H2O
6 D-glucose
-
-
-
?
cellohexaose + H2O
2 cellotriose
cellohexaose + H2O
cellobiose + cellotriose
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose + cellulose + cellopentaose
-
cellobiose is the main product
-
-
?
cellohexaose + H2O
cellotetraose + cellobiose
-
-
-
?
cellohexaose + H2O
cellotriose + cellobiose
-
-
-
?
cellohexaose + H2O
cellotriose + cellobiose + D-glucose
-
-
-
-
?
cellohexaose + H2O
cellotriose + cellotetraose + cellobiose
cellohexaose + H2O
D-glucose + ?
-
-
-
-
?
cellooligosaccharide + H2O
?
cellooligosaccharides + H2O
?
random cleavage, slow reaction rates for cellooligosaccharides smaller than G5
-
-
?
cellopentaose
cellohexaose + celloheptaose
-
transfer reaction
-
?
cellopentaose + 4 H2O
5 D-glucose
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
cellopentaose + H2O
cellobiose + cellotriose + cellotetraose + cellulose
-
cellobiose is the main product
-
-
?
cellopentaose + H2O
cellobiose + glucose
-
-
-
-
?
cellopentaose + H2O
cellotetraose + glucose
-
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
cellopentaose + H2O
cellotriose + cellobiose + D-glucose
-
-
-
-
?
cellopentaose + H2O
D-glucose + ?
-
-
-
-
?
cellopentaosyl sorbitol + H2O
?
-
cellulase A, B, and C
-
-
?
cellotetraose
cellopentaose + cellohexaose
cellotetraose + 3 H2O
4 D-glucose
-
-
-
?
cellotetraose + H2O
2 cellobiose
cellotetraose + H2O
cellotriose + cellobiose + D-glucose
-
-
-
-
?
cellotetraose + H2O
D-glucose + cellobiose + cellotriose
-
-
-
-
?
cellotetraosyl sorbitol + H2O
?
-
cellulase A, B, and C
-
-
?
cellotriose
cellopentaose + cellotetraose
cellotriose + 2 H2O
3 D-glucose
-
-
-
?
cellotriose + H2O
D-glucose + cellobiose
cellotrioside + H2O
?
-
7.4% of the activity with barley beta-glucan
-
-
?
cellulose + H2O
cellobiose + ?
cellulose + H2O
cellobiose + cellotriose + cellotetraose + cellopentaose
Thermochaetoides thermophila
-
-
-
-
?
cellulose + H2O
cellobiose + glucose
-
-
-
-
?
cellulose + H2O
cellooligosaccharide
cellulose + H2O
D-glucose + ?
cellulose from Smallanthus sonchifolius
D-glucose + ?
-
-
-
-
?
cellulose from yam
D-glucose + ?
-
-
-
-
?
chitotetraose + H2O
?
-
-
-
-
?
chitotriose + H2O
?
-
-
-
-
?
CM cellulose + H2O
?
-
-
-
?
corn stover + H2O
?
-
-
-
-
?
cotton straw + H2O
?
-
-
-
-
?
crystalline cellulase + H2O
?
-
-
-
?
crystalline cellulose
?
-
-
-
?
crystalline cellulose + H2O
?
curdlan + H2O
?
activity is 26% compared to activity with carboxymethyl-cellulose
-
-
?
debranched arabinan
?
activity is 25% compared to activity with carboxymethyl-cellulose
-
-
?
dextran + H2O
?
-
-
-
-
?
filter paper + H2O
cellobiose + ?
-
-
-
-
?
filter paper + H2O
cellotriose + cellobiose + D-glucose
-
poor substrate
major products
-
?
hydroxyethyl cellulose + H2O
?
hydroxyethylcellulose + H2O
?
insoluble cellulose + H2O
?
insoluble H3PO4 acid-swollen cellulose + H2O
?
-
-
-
-
?
konac glucomannan + H2O
?
konjac glucomannan + H2O
?
-
-
-
?
konjac glucomannan + H2O
cellobiose + cellotriose
-
substrate concentration 1%
-
-
?
laminarin + H2O
6 D-glucose
-
-
-
?
lichenan + H2O
cellotriose + cellobiose + D-glucose
-
enzyme hydrolyzes internal beta-1,4 glycosidic bonds within lichenan as well as carboxymethyl cellulose to release oligosaccharides and glucose
major products
-
?
locust bean gum + H2O
?
-
-
-
?
methyl cellulose + H2O
D-glucose
-
-
-
-
?
microcrystaliine cellulose + H2O
cellobiose + ?
Thermochaetoides thermophila
-
-
-
-
?
microcrystalline cellulose + H2O
?
milled aspen wood + H2O
?
-
-
-
-
?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
-
the enzyme liberates disaccharides from the reducing end
-
-
?
N,N',N''-triacetyl-chitotriose + H2O
N,N'-diacetyl-chitobiose + N-acetyl-D-glucosamine
-
the enzyme liberates disaccharides from the reducing end
-
-
?
N-acetyllactosamine + butanol
butyl beta-N-acetyllactosaminide + H2O
-
-
-
-
?
N-acetyllactosamine + ethanol
ethyl beta-N-acetyllactosaminide + H2O
-
-
-
-
?
N-acetyllactosamine + glycerol
glyceryl beta-N-acetyllactosaminide
-
-
-
-
?
N-acetyllactosamine + propanol
propyl beta-N-acetyllactosaminide + H2O
-
-
-
-
?
N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
?
N-[2-N-[(S-(4-deoxy-4-dimethylaminophenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
?
-
-
-
?
N-[2-N-[(S-(4-deoxy-4-dimethylaminophenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
? + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
-
-
?
noncrystalline cellulose + H2O
?
-
as natural substrate for CEL7
-
-
?
o-nitrophenyl beta-cellobioside + H2O
?
p-nitrophenyl beta-D-cellobioside + H2O
glucose + cellobiose + ?
p-nitrophenyl cellobiose + H2O
?
-
-
-
?
p-nitrophenyl cellobiose + H2O
p-nitrophenol + cellobiose
p-nitrophenyl-beta-D-cellobioside + H2O
?
p-nitrophenyl-beta-D-cellopentaoside + H2O
?
-
-
-
?
p-nitrophenyl-beta-D-cellotetraoside + H2O
?
-
-
-
?
p-nitrophenyl-cellobiose + H2O
?
-
-
-
?
pachyman + H2O
?
activity is 22% compared to activity with carboxymethyl-cellulose
-
-
?
pectin + H2O
galacturonic acid oligosaccharides
Thermochaetoides thermophila
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
phosphoric acid swollen cellulose + H2O
cellobiose + cellotriose
-
substrate concentration 1%, best substrate and high activity
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
phosphoric acid-swollen avicel + H2O
cellobiose + ?
Thermochaetoides thermophila
-
-
-
-
?
phosphoric acid-swollen cellulose + H2O
?
phosphoric acid-treated wheat straw + H2O
?
pretreated sorghum stover + H2O
?
pullulan + H2O
?
-
-
-
-
?
raffinose + H2O
?
-
-
-
?
sea lettuce + H2O
cellotriose + cellobiose + D-glucose
-
-
major products
-
?
sodium carboxymethyl cellulose + H2O
?
soluble cellodextrin + H2O
?
soluble cellulose + H2O
?
-
endo mode of action. At the beginning only high molecular mass products are released suggesting an endowise action of the enzyme. The major product has a degree of polymerization of three, minor quantities of smaller and larger oligosaccharides are also produced. Not active against insoluble cellulose
-
-
?
soluble starch + H2O
?
Thermochaetoides thermophila
-
-
-
?
sugarcane bagasse + H2O
?
sulfite-pulped spruce + H2O
cellobiose + cellotriose
-
substrate concentration 1%
-
-
?
tamarind xyloglucan + H2O
?
Whatman filter paper + H2O
?
xylan + H2O
D-xylose + ?
at 90°C, pH 4 by an enzyme mix consisting of SSO1354 and additional glycosyl hydrolases
-
-
?
yeast glucan + H2O
?
-
best substrate of isoform cellulase I, no substrate of isoforms cellulase II and III
-
-
?
6-O-methylcellulose + H2O
additional information
-
2 cellobiose
cellotetraose + H2O
-
transfer reaction
-
?
2 cellobiose
cellotetraose + H2O
-
transfer reaction
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
-
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
-
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
-
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
-
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
-
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
-
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
?
-
-
-
?
2,4-dinitrophenyl beta-D-cellobioside + H2O
?
-
-
-
?
2,4-dinitrophenyl beta-D-cellobioside + H2O
?
-
-
-
?
2-hydroxyethyl cellulose + H2O
?
-
-
-
?
2-hydroxyethyl cellulose + H2O
?
-
-
-
?
4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside + H2O
4'',6''-O-benzylidene beta-cellobioside + 2-chloro-4-nitrophenyl beta-D-glucoside
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture
-
-
?
4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside + H2O
4'',6''-O-benzylidene beta-cellobioside + 2-chloro-4-nitrophenyl beta-D-glucoside
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture
-
-
?
4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside + H2O
4'',6''-O-benzylidene beta-cellobioside + 2-chloro-4-nitrophenyl beta-D-glucoside
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture
-
-
?
4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside + H2O
4'',6''-O-benzylidene beta-cellobioside + 2-chloro-4-nitrophenyl beta-D-glucoside
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
-
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
-
-
-
-
?
4-methylumbelliferyl cellobioside + H2O
?
Bacillus cellulyticus K-12
-
-
-
-
?
4-methylumbelliferyl cellobioside + H2O
?
-
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
very low activity
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
-
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside + H2O
4,6-O-(3-oxobutylidene)-beta-D-cellotriose + 4-nitrophenyl-beta-D-cellobioside
-
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside + H2O
4,6-O-(3-oxobutylidene)-beta-D-cellotriose + 4-nitrophenyl-beta-D-cellobioside
-
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside + H2O
4,6-O-(3-oxobutylidene)-beta-D-cellotriose + 4-nitrophenyl-beta-D-cellobioside
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
14% of the activity with carboxymethyl cellulose
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
14% of the activity with carboxymethyl cellulose
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
low activity
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
acid-swollen cellulose + H2O
?
-
-
-
-
?
acid-swollen cellulose + H2O
?
-
-
-
-
?
acid-swollen cellulose + H2O
?
-
-
-
?
acid-swollen cellulose + H2O
?
cleaved cellulose randomly
-
-
?
acid-swollen cellulose + H2O
?
-
-
-
?
acid-swollen cellulose + H2O
?
-
-
-
?
acid-swollen cellulose + H2O
?
activity of truncated enzyme form
-
-
?
acid-swollen cellulose + H2O
?
activity of truncated enzyme form
-
-
?
acid-swollen cellulose + H2O
?
-
-
-
?
amorphic Solca Floc cellulose + H2O
?
-
-
-
?
amorphic Solca Floc cellulose + H2O
?
-
-
-
?
arabinan + H2O
?
-
-
-
?
arabinan + H2O
?
hydrolysed at 53% compared to the hydrolysis of carboxymethylcellulose
-
-
?
avicel + H2O
?
-
weak activity
-
-
?
avicel + H2O
?
-
no hydrolysis
-
-
?
avicel + H2O
?
-
endoglucanase I show very low activity
-
-
?
avicel + H2O
?
-
weak activity
-
-
?
avicel + H2O
?
-
8.1% of the activity with carboxymethyl cellulose
-
?
avicel + H2O
?
Actinomyces sp. 40 Korean Native Goat 40
-
8.1% of the activity with carboxymethyl cellulose
-
?
avicel + H2O
?
-
low activity
-
-
?
avicel + H2O
?
-
14% of the activity with carboxymethylcellulose
-
-
?
avicel + H2O
?
-
14% of the activity with carboxymethylcellulose
-
-
?
avicel + H2O
?
Bacillus cellulyticus K-12
-
-
cellobiose + cellotetraose
?
avicel + H2O
?
-
microcrystalline cellulose, shows poor growth and enzyme production, relative activity 5.2%
-
-
?
avicel + H2O
?
-
microcrystalline cellulose, shows poor growth and enzyme production, relative activity 5.2%
-
-
?
avicel + H2O
?
21.8% of the activity with carboxymethyl cellulose
-
-
?
avicel + H2O
?
21.8% of the activtiy with carboxymethyl cellulose
-
-
?
avicel + H2O
?
-
chimeric xylanase/endoglucanase
-
-
?
avicel + H2O
?
-
endoglucanase 47
-
-
?
avicel + H2O
?
-
cellulase I
-
-
?
avicel + H2O
?
-
12% of the activity with carboxymethyl cellulose
-
-
?
avicel + H2O
?
-
-
glucose + cellobiose + cellotriose + cellotetraose
?
avicel + H2O
?
-
-
main product is cellobiose
?
avicel + H2O
?
14% of the activity with carboxymethyl-cellulose
-
-
?
avicel + H2O
?
17.7% of the activity with carboxymethyl-cellulose
-
-
?
avicel + H2O
?
-
no hydrolysis
-
-
?
avicel + H2O
?
-
weak activity
-
-
?
avicel + H2O
?
weak activity
-
-
?
avicel + H2O
?
-
33% of the activity with carboxymethyl cellulose
-
-
?
avicel + H2O
?
-
33% of the activity with carboxymethyl cellulose
-
-
?
avicel + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
avicel + H2O
?
-
good substrate of isoforms cellulase II and III
-
-
?
avicel + H2O
?
Thermochaetoides thermophila
-
-
-
-
?
avicel + H2O
?
Thermochaetoides thermophila CT2
-
-
-
-
?
avicel + H2O
?
-
microcrystalline cellulose (Avicel) is subjected to 3 different pretreatments (acid, alkaline, and organic solvent) before exposure to amixture of cellulases
-
-
?
avicel + H2O
?
-
activity of the catalytic module EG1-CM is43% of the activity with endoglucanase 1
-
-
?
avicel + H2O
?
55% of the activity with carboxymethyl cellulose
-
-
?
avicel + H2O
cellobiose + ?
-
-
-
?
avicel + H2O
cellobiose + ?
the main product is cellobiose
-
-
?
avicel + H2O
cellobiose + ?
the main product is cellobiose
-
-
?
avicel + H2O
cellobiose + ?
-
-
-
?
avicel + H2O
cellobiose + cellotriose
-
substrate concentration 1%, low activity
-
-
?
avicel + H2O
cellobiose + cellotriose
cellooligosaccharides production from Avicel is detected only when 0.00185 mkat of Xf818his are employed, and not when 16.67 nkat are used. Endoglucanase with exohydrolytic activity
-
-
?
avicel + H2O
D-glucose + ?
-
-
-
-
?
avicel + H2O
D-glucose + ?
-
-
-
-
?
avicel + H2O
D-glucose + ?
-
-
-
-
?
azurine-labelled hydroxyethylcellulose + H2O
?
-
-
-
-
?
azurine-labelled hydroxyethylcellulose + H2O
?
-
-
-
-
?
azurine-labelled hydroxyethylcellulose + H2O
?
-
-
-
-
?
bacterial cellulose + H2O
?
-
-
-
?
bacterial cellulose + H2O
?
-
-
-
?
bacterial cellulose + H2O
?
-
-
-
?
bacterial cellulose + H2O
?
-
-
-
?
bacterial cellulose + H2O
?
-
-
-
?
bacterial cellulose + H2O
?
-
-
-
?
bacterial cellulose + H2O
?
-
-
-
?
bacterial cellulose + H2O
?
-
-
-
?
bacterial microcrystalline cellulose + H2O
?
weak activity
-
-
?
bacterial microcrystalline cellulose + H2O
?
-
-
-
?
bacterial microcrystalline cellulose + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
-
?
barley beta-glucan + H2O
?
92% of the activity on carboxymethyl cellulose
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
soluble substrate
-
-
?
barley beta-glucan + H2O
?
-
soluble substrate
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
as AZCL beta-glucan
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
MG570051
311% of the activity with carboxymethylcellulose
-
-
?
barley beta-glucan + H2O
?
-
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
the highest specific activity toward polysaccharides occurs with mixed-linkage (1->3),(1->4)-beta-D-glucans such as barley beta-glucan and lichenan
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
best substrate
-
-
?
barley beta-glucan + H2O
?
best substrate
-
-
?
barley beta-glucan + H2O
?
best substrate
-
-
?
barley beta-glucan + H2O
?
136% of the activity with carboxymethyl cellulose
-
-
?
barley beta-glucan + H2O
?
-
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
moderate activity
-
-
?
barley beta-glucan + H2O
D-glucose + ?
high activity
-
-
?
barley beta-glucan + H2O
D-glucose + ?
high activity
-
-
?
barley beta-glucan + H2O
D-glucose + ?
high activity
-
-
?
barley glucan + H2O
?
-
-
-
-
?
barley glucan + H2O
?
-
-
-
-
?
barley glucan + H2O
?
120% of the activity with carboxymethyl-cellulose
-
-
?
barley glucan + H2O
?
143% of the activity with carboxymethyl-cellulose
-
-
?
barley glucan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
barley glucan + H2O
?
the enzyme hydrolyzes mixed linked beta-(1-3)(1-4) substrates such as barley glucan and lichenan more strongly than carboxymethylcellulose
-
-
?
beechwood xylan + H2O
?
hydrolysed at 84% compared to the hydrolysis of carboxymethylcellulose
-
-
?
beechwood xylan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
beechwood xylan + H2O
?
10% of the activity with carboxymethyl cellulose
-
-
?
beta-1,4-D-glucan + H2O
?
Thermochaetoides thermophila
-
-
-
?
beta-1,4-D-glucan + H2O
?
Thermochaetoides thermophila
bifunctional endoglucanase/xylanase enzyme
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
24.6% of the activity with carboxymethylcellulose
-
-
?
beta-glucan + H2O
?
-
24.6% of the activity with carboxymethylcellulose
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
and lichenan, preferred substrates
-
-
?
beta-glucan + H2O
?
-
and lichenan, preferred substrates
-
-
?
beta-glucan + H2O
?
from Hordeum vulgare
-
-
?
beta-glucan + H2O
?
-
endoglucanase EG25
-
-
?
beta-glucan + H2O
?
-
endoglucanase EG28
-
-
?
beta-glucan + H2O
?
-
endoglucanase EG44
-
-
?
beta-glucan + H2O
?
-
endoglucanase EG47
-
-
?
beta-glucan + H2O
?
-
endoglucanase EG51
-
-
?
beta-glucan + H2O
?
-
endoglucanase EG60
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
degree of hydrolysis reaches 10%, products are oligosaccharides with degree of polymerization 2-10
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
400% of the activity with carboxymethyl cellulose
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
2% of the activity with carboxymethyl cellulose
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
hydrolysed at 73% compared to the hydrolysis of carboxymethylcellulose
-
-
?
birchwood xylan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
birchwood xylan + H2O
?
-
88% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
birchwood xylan + H2O
?
-
88% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
birchwood xylan + H2O
?
44% of the activity with carboxymethylcellulose
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
Actinomyces sp. 40 Korean Native Goat 40
-
-
-
?
carboxymethyl cellulose + H2O
?
-
production of a mixture of cellobiose, cellotriose, cellotetraose and cellopentaose
-
?
carboxymethyl cellulose + H2O
?
-
2% solution
-
-
?
carboxymethyl cellulose + H2O
?
-
2% solution
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
endo-beta-1,4-glucanase EG27 shows high preference for
-
-
?
carboxymethyl cellulose + H2O
?
-
endo-beta-1,4-glucanase EG45 shows high preference for
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
18.6% of the activity with barley beta-glucan
-
-
?
carboxymethyl cellulose + H2O
?
18.6% of the activity with barley beta-glucan
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
products are mainly cello-oligosaccharides along with small amounts of glucose and cellobiose
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
processive endoglucanase activity
-
-
?
carboxymethyl cellulose + H2O
?
processive endoglucanase activity
-
-
?
carboxymethyl cellulose + H2O
?
-
endoglucanase EG25
-
-
?
carboxymethyl cellulose + H2O
?
-
endoglucanase EG28
-
-
?
carboxymethyl cellulose + H2O
?
-
endoglucanase EG44
-
-
?
carboxymethyl cellulose + H2O
?
-
endoglucanase EG47
-
-
?
carboxymethyl cellulose + H2O
?
-
endoglucanase EG51
-
-
?
carboxymethyl cellulose + H2O
?
-
endoglucanase EG60
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
Ctenolepisma longicaudatum
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
Cel9A is a nonprocessive enzyme with endo-cellulase activities
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
high activity
-
-
?
carboxymethyl cellulose + H2O
?
-
endoglucanase 35
-
-
?
carboxymethyl cellulose + H2O
?
-
endoglucanase 47
-
-
?
carboxymethyl cellulose + H2O
?
high activity
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
best substrate
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
13.6% of the activity with barley beta-glucan
-
-
?
carboxymethyl cellulose + H2O
?
13.6% of the activity with barley beta-glucan
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
no glucose, cellobiose and short chain celloolifgosaccharides are formed
-
?
carboxymethyl cellulose + H2O
?
-
-
no glucose, cellobiose and short chain celloolifgosaccharides are formed
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
medium and low viscosity
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
68% of the activity with barley beta-glucan
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
best substrate
-
-
?
carboxymethyl cellulose + H2O
?
activity of truncated enzyme form
-
-
?
carboxymethyl cellulose + H2O
?
activity of truncated enzyme form
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
release of reducing sugar, degradation
-
-
?
carboxymethyl cellulose + H2O
?
release of reducing sugar, degradation
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
AZO-carboxymethyl cellulose
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
22% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
carboxymethyl cellulose + H2O
?
-
best substrate of isoform cellulase III, no substrate of cellulase II
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
22% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila
-
-
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila
-
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila
-
best substrate tested
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila
1% w/v CMC-Na
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila
bifunctional endoglucanase/xylanase enzyme
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila CBS 144.50
-
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila CT2
-
best substrate tested
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila DSM 1495
-
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila IMI 039719
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
best substrate
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
soluble, lower activity
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
moderate activity
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
endoglucanase with exohydrolytic activity
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
cellobiose + ?
-
-
-
?
carboxymethyl cellulose + H2O
cellobiose + ?
-
-
-
?
carboxymethyl cellulose + H2O
cellobiose + cellotriose + ?
-
products are 18% cellotriose, 72% cellobiose and 10% glucose
-
?
carboxymethyl cellulose + H2O
cellobiose + cellotriose + ?
-
-
-
?
carboxymethyl cellulose + H2O
cellobiose + cellotriose + ?
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
-
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
-
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
high activity
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
high activity
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
high activity
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
-
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
-
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
-
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
-
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
-
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
-
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
-
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + ?
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + cellobiose + cellooligosaccharide
-
-
-
-
?
carboxymethyl cellulose + H2O
D-glucose + cellobiose + cellooligosaccharide
-
-
-
-
?
carboxymethyl cellulose + H2O
glucose + cellobiose + short oligomers
-
-
-
-
?
carboxymethyl cellulose + H2O
glucose + cellobiose + short oligomers
-
-
-
-
?
carboxymethyl-cellulose + H2O
?
-
-
-
?
carboxymethyl-cellulose + H2O
?
-
-
-
?
carboxymethyl-cellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
the smallest product is a disaccharide
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
best substrate
-
-
?
carboxymethylcellulose + H2O
?
-
best substrate
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
soluble substrate
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
soluble substrate
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
Bellamya chinensis laeta UM-2014
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
activity with carbomethylcellulose with approxomately 4 carboxymethyl groups per 10 anhydro-glucose units is about 3.5 times better than that with carbomethylcellulose with approximately 8 carboxymethyl groups
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
high specific activity towards carboxymethylcellulose
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
MG570051
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
medium-viscosity substrate
-
-
?
carboxymethylcellulose + H2O
?
Thermochaetoides thermophila
-
-
-
-
?
carboxymethylcellulose + H2O
?
Thermochaetoides thermophila
-
-
-
?
carboxymethylcellulose + H2O
?
Thermochaetoides thermophila CT2
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
the enzyme hydrolyzes mixed linked beta-(1-3)(1-4) substrates such as barley glucan and lichenan more strongly than carboxymethylcellulose
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
carboxymethyl glucose + cellobiose + cellotriose
-
-
-
-
?
carboxymethylcellulose + H2O
carboxymethyl glucose + cellobiose + cellotriose
-
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellotriose + cellotetraose + cellopentaose
-
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellotriose + cellotetraose + cellopentaose
-
-
-
-
?
carboxymethylcellulose + H2O
D-glucose + ?
-
-
-
-
?
carboxymethylcellulose + H2O
D-glucose + ?
-
-
-
-
?
carboxymethylcellulose + H2O
short glucose oligomers + cellobiose + glucose
-
-
-
-
?
carboxymethylcellulose + H2O
short glucose oligomers + cellobiose + glucose
-
-
-
-
?
cellobiose + H2O
2 D-glucose
-
26% of the activity with carboxymethyl cellulose
-
?
cellobiose + H2O
2 D-glucose
Actinomyces sp. 40 Korean Native Goat 40
-
26% of the activity with carboxymethyl cellulose
-
?
cellobiose + H2O
2 D-glucose
-
-
-
-
?
cellobiose + H2O
2 D-glucose
-
-
-
-
?
cellobiose + H2O
2 D-glucose
-
-
-
?
cellobiose + H2O
?
-
9.8% of the activity with carboxymethyl cellulose
-
?
cellobiose + H2O
?
-
9.8% of the activity with carboxymethyl cellulose
-
?
cellobiose + H2O
?
-
8.6% of the activity with carboxymethylcellulose
-
-
?
cellobiose + H2O
?
-
-
-
?
cellobiose + H2O
?
-
-
-
?
cellobiose + H2O
?
-
25% of the activity with carboxymethyl cellulose
-
-
?
cellobiose + H2O
?
-
-
-
-
?
cellodextrin + H2O
?
-
-
-
-
?
cellodextrin + H2O
?
-
cellulase A, B, and C
-
-
?
celloheptaose + H2O
?
-
-
-
-
?
celloheptaose + H2O
?
-
-
-
-
?
cellohexaose + H2O
2 cellotriose
-
-
+ small amounts of cellobiose and cellotriose
-
?
cellohexaose + H2O
2 cellotriose
-
-
+ small amounts of cellobiose and cellotriose
-
?
cellohexaose + H2O
?
-
-
-
-
?
cellohexaose + H2O
?
-
-
-
?
cellohexaose + H2O
?
-
-
-
?
cellohexaose + H2O
?
-
-
-
-
?
cellohexaose + H2O
?
Thermochaetoides thermophila
-
the enzyme hydrolyzes cellotetraose, cellopentaose, and cellohexaose at comparable rates
-
-
?
cellohexaose + H2O
cellobiose + cellotriose
-
-
-
?
cellohexaose + H2O
cellobiose + cellotriose
-
-
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
-
-
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
Bellamya chinensis laeta UM-2014
-
-
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
-
-
-
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
-
-
-
-
?
cellohexaose + H2O
cellotriose + cellotetraose + cellobiose
major product is cellotriose, minor products are cellobiose and cellotetraose
-
-
?
cellohexaose + H2O
cellotriose + cellotetraose + cellobiose
major product is cellotriose, minor products are cellobiose and cellotetraose
-
-
?
cellooligosaccharide + H2O
?
-
-
-
-
?
cellooligosaccharide + H2O
?
-
insolvent cellooligosaccharide 33
-
-
?
cellooligosaccharide + H2O
?
-
-
-
-
?
cellopentaose + H2O
?
-
-
-
-
?
cellopentaose + H2O
?
-
-
-
?
cellopentaose + H2O
?
minimal length substrate
-
-
?
cellopentaose + H2O
?
minimal length substrate
-
-
?
cellopentaose + H2O
?
-
-
-
?
cellopentaose + H2O
?
-
-
-
-
?
cellopentaose + H2O
?
Thermochaetoides thermophila
-
the enzyme hydrolyzes cellotetraose, cellopentaose, and cellohexaose at comparable rates
-
-
?
cellopentaose + H2O
?
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellotetraose
cellopentaose + cellohexaose
-
transfer reaction
-
?
cellotetraose
cellopentaose + cellohexaose
-
transfer reaction
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
enzyme form EGB and EGC
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
+ glucose + cellotriose
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
glucose, 15%, cellobiose, 64%, cellotriose, 14% and cellotetraose, 3.3%
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
Bacillus sp. (in: Bacteria) No. 1139
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
Bacillus sp. (in: Bacteria) No. 1139
-
-
glucose, 15%, cellobiose, 64%, cellotriose, 14% and cellotetraose, 3.3%
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
+ glucose + cellotriose
?
cellotetraose + H2O
2 cellobiose
-
-
+ glucose + cellotriose
?
cellotetraose + H2O
2 cellobiose
-
-
+ glucose + cellotriose
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
cellulase A, B, and C
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
predominant product
?
cellotetraose + H2O
2 cellobiose
-
-
predominant product
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
minimal substrate length, cellotriose and cellobiose are not hydrolyzed
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
minimal substrate length, cellotriose and cellobiose are not hydrolyzed
-
-
?
cellotetraose + H2O
2 cellobiose
-
effectively hydrolyzed by endoglucanase E1, limited hydrolysis by endoglucanase E2
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
?
-
-
-
?
cellotetraose + H2O
?
-
-
-
?
cellotetraose + H2O
?
-
-
-
-
?
cellotetraose + H2O
?
Thermochaetoides thermophila
-
the enzyme hydrolyzes cellotetraose, cellopentaose, and cellohexaose at comparable rates
-
-
?
cellotetraose + H2O
?
-
-
-
?
cellotriose
cellopentaose + cellotetraose
-
transfer reaction
-
?
cellotriose
cellopentaose + cellotetraose
-
transfer reaction
-
?
cellotriose + H2O
?
-
-
-
?
cellotriose + H2O
?
-
-
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
no hydrolysis
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
enzyme form EGC
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
-
+ glucose
?
cellotriose + H2O
D-glucose + cellobiose
-
-
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
-
a mixture of glucose, 5.5%, cellobiose, 55%, cellotriose, 34%, and traces of cellotetraose
?
cellotriose + H2O
D-glucose + cellobiose
-
-
-
-
?
cellotriose + H2O
D-glucose + cellobiose
Bacillus sp. (in: Bacteria) No. 1139
-
-
-
-
?
cellotriose + H2O
D-glucose + cellobiose
Bacillus sp. (in: Bacteria) No. 1139
-
-
a mixture of glucose, 5.5%, cellobiose, 55%, cellotriose, 34%, and traces of cellotetraose
?
cellotriose + H2O
D-glucose + cellobiose
-
-
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
-
+ glucose
?
cellotriose + H2O
D-glucose + cellobiose
-
no reaction
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
no reaction
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
-
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
cellulase C
-
?
cellotriose + H2O
D-glucose + cellobiose
-
hydrolyzed by endo-beta-1,4-glucanase component YEG2, no hydrolysis with endo-beta-1,4-glucanase component YEG1
+ glucose
?
cellotriose + H2O
D-glucose + cellobiose
-
-
predominant product
?
cellotriose + H2O
D-glucose + cellobiose
-
-
predominant product
?
cellotriose + H2O
D-glucose + cellobiose
-
no activity
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
no reaction
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
negligibly hydrolyzed
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
effectively hydrolyzed by endoglucanase E1, limited hydrolysis by endoglucanase E2
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
hydrolyzed by endoglucanase E1, no activity with endoglucanase E2
+ glucose, endoglucanase E1
?
cellotriose + H2O
D-glucose + cellobiose
-
-
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
slightly degraded
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
endoglucanase I shows very low activity with acid-swollen cellulose
-
-
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
Walseth cellulose shows 1.1% of the activity with carboxymethylcellulose
-
-
?
cellulose + H2O
?
-
little ability to hydrolyze ordered cellulose
-
-
?
cellulose + H2O
?
-
enzyme form EGA and EGD
-
-
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
pretreatment of cellulose with ionic liquids such as 1-butyl-3-methylimidazolium chloride, 1-methylimidazolium chloride, and tris-(2-hydroxyethyl)-methylammonium methylsulfate results in more rapid conversion to glucose than hydrolysis with cellulose that is not pretreated
-
-
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
Walseth cellulose
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
amorphous cellulose (relative activity 15.2%), filter paper (shows poor growth and enzyme production, relative activity 3.1%), cotton wool (relative activity 4.3%)
-
-
?
cellulose + H2O
?
-
amorphous cellulose (relative activity 15.2%), filter paper (shows poor growth and enzyme production, relative activity 3.1%), cotton wool (relative activity 4.3%)
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
?
cellulose + H2O
?
-
acid-swollen
major end product are cellobiose and cellotriose, endoglucanase Z
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
swollen cellulose
a mixture of cellooligosaccharides
?
cellulose + H2O
?
-
swollen cellulose
a mixture of cellooligosaccharides
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
maximal activity soluble cellulosic substrate (CMC-Na salt), indicating that the crude enzyme has endoglucanase activity
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
maximal activity soluble cellulosic substrate (CMC-Na salt), indicating that the crude enzyme has endoglucanase activity
-
-
?
cellulose + H2O
?
-
Walseth cellulose
products from Walseth cellulose: glucose + cellobiose + cellotriose + cellotetraose
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
?
cellulose + H2O
?
crystalline and amorphous cellulose
-
-
?
cellulose + H2O
?
-
-
-
?
cellulose + H2O
?
-
Avicel or coastal Bermuda grass
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
amorphous cellulose and ball-milled cellulose
-
-
?
cellulose + H2O
?
activity is evaluated on 13 insoluble celluloses characterized for crystallinity and crystal width (by X-ray diffraction), wet porosity (by thermoporometry), and particle size (by light scattering). Looser crystalline packing increases the lengths of released cello-oligomers as well as the maximum endoglucanase specific activity (kcat)
-
-
?
cellulose + H2O
?
-
-
-
?
cellulose + H2O
?
-
-
-
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
-
crystalline cellulose is hydrolyzed to glucose and cellobiose
?
cellulose + H2O
?
-
filter paper, 18% activity compared to carboxymethyl cellulose
-
-
?
cellulose + H2O
?
-
acid-swollen
-
?
cellulose + H2O
?
-
acid-swollen
large amounts of cellotriose and a small amount of cellotetraose
?
cellulose + H2O
?
-
acid-swollen
-
?
cellulose + H2O
?
-
-
-
?
cellulose + H2O
?
-
no hydrolysis of native cellulose
-
-
?
cellulose + H2O
?
Sporotrichum pulverulentum
-
-
-
-
?
cellulose + H2O
?
Sporotrichum pulverulentum
-
acid-swollen
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
Walseth cellulose
-
-
?
cellulose + H2O
?
-
Walseth cellulose
mainly glucose, cellobiose and traces of cellotriose
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
hydrolysis of Solka floc, Avicel, CMC, waste paper, and waste wood refiner
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
partial degradation of native cellulose
-
-
?
cellulose + H2O
?
-
endoglucanase E1 exhibits higher activity
-
?
cellulose + H2O
?
-
acid-swollen
-
?
cellulose + H2O
?
-
amorphous cellulose
endoglucanase E1 produces mainly cellobiose and a trace of glucose, endoglucanase E2 produces mainly cellotriose and higher oligomers with some cellobiose and a trace of glucose
?
cellulose + H2O
?
-
the catalytic domains of Cel6A, Cel6B, Cel48A, Cel5A, and Cel9A only show very weak binding to bacterial cellulose
-
-
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
amorphous cellulose
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
?
cellulose + H2O
?
-
no degradation of crystalline cellulose
-
-
?
cellulose + H2O
?
-
the family 1 carbohydrate-binding module, CBM, mediates the interaction between enzyme and crystalline cellulose surface via residues Y5, Q7, N29, and Y32, thus CBM is responsible for anchoring the enzyme at discrete points along a cellulose chain to aid in both recognizing cellulose chain ends for initial attachment to cellulose as well as aid in enzymatic catalysis by diffusing between stable wells on a length scale commensurate with the catalytic, processive cycle of Cel7A during cellulose hydrolysis, molecular-level mechanisms of recognition and interaction, overview
-
-
?
cellulose + H2O
?
-
no degradation of crystalline cellulose
-
-
?
cellulose + H2O
?
-
acid-swollen
-
-
?
cellulose + H2O
?
-
amorphous cellulose
-
-
?
cellulose + H2O
cellobiose + ?
the substrate position is fixed by the alignment of one cellobiose unit between the two aromatic amino acid residues at subsites +1 and +2. During the enzyme reaction, the glucose structure of cellulose substrates is distorted at subsite -1, and the beta-1,4-glucoside bond between glucose moieties is twisted between subsites -1 and +1. Subsite -2 specifically recognizes the glucose residue, but recognition by subsites +1 and +2 is loose during the enzyme reaction. Analysis of the enzyme-substrate structure suggests that an incoming water molecule, essential for hydrolysis during the retention process, might be introduced to the cleavage position after the cellobiose product at subsites +1 and +2 is released from the active site
-
-
?
cellulose + H2O
cellobiose + ?
the substrate position is fixed by the alignment of one cellobiose unit between the two aromatic amino acid residues at subsites +1 and +2. During the enzyme reaction, the glucose structure of cellulose substrates is distorted at subsite -1, and the beta-1,4-glucoside bond between glucose moieties is twisted between subsites -1 and +1. Subsite -2 specifically recognizes the glucose residue, but recognition by subsites +1 and +2 is loose during the enzyme reaction. Analysis of the enzyme-substrate structure suggests that an incoming water molecule, essential for hydrolysis during the retention process, might be introduced to the cleavage position after the cellobiose product at subsites +1 and +2 is released from the active site
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
?
cellulose + H2O
cellobiose + ?
the secreted protein enables Sulfolobus solfataricus to use cellulose as an external carbon source
-
-
?
cellulose + H2O
cellobiose + ?
the secreted protein enables Sulfolobus solfataricus to use cellulose as an external carbon source
-
-
?
cellulose + H2O
cellooligosaccharide
-
the enzyme plays an important role in maintaining the carbon balance in nature
-
-
?
cellulose + H2O
cellooligosaccharide
-
in bean the 9.5 cellulase appears to function in the shedding of various organs such as fruits, flowers, and leaves. The acid cellulases function in loosening the cellulose fibrils of the cell wall to allow expansion and growth
-
-
?
cellulose + H2O
cellooligosaccharide
-
-
-
?
cellulose + H2O
cellooligosaccharide
-
inducible enzyme
-
-
?
cellulose + H2O
cellooligosaccharide
Sporotrichum pulverulentum
-
enzyme is involved in degradation of cellulose
-
-
?
cellulose + H2O
cellooligosaccharide
-
induced by carboxymethylcellulose, non-constitutive synthesis
-
-
?
cellulose + H2O
cellooligosaccharide
-
enzyme plays an important role in the carbon cycle
-
-
?
cellulose + H2O
cellooligosaccharide
-
enzyme plays an important role in the carbon cycle
-
-
?
cellulose + H2O
D-glucose + ?
-
enzyme is able to degrade crystalline cellulose to glucose
-
?
cellulose + H2O
D-glucose + ?
enzyme FnCel5A catalyzes the hydrolysis of cellulose to glucose
-
-
?
cellulose + H2O
D-glucose + ?
enzyme FnCel5A catalyzes the hydrolysis of cellulose to glucose
-
-
?
cellulose + H2O
D-glucose + ?
enzyme FnCel5A catalyzes the hydrolysis of cellulose to glucose
-
-
?
cellulose + H2O
D-glucose + ?
-
-
-
?
cellulose + H2O
D-glucose + ?
at 90°C, pH 4 by an enzyme mix consisting of SSO1354 and additional glycosyl hydrolases
-
-
?
cellulose + H2O
D-glucose + ?
-
-
-
-
?
cotton + H2O
?
-
-
-
-
?
crystalline cellulose + H2O
?
-
-
-
?
crystalline cellulose + H2O
?
-
as natural substrate for CEL9C1
-
-
?
filter paper + H2O
?
-
18% of the activity with carboxymethyl cellulose
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
qualitative filter paper-grade 1
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
-
8.4% of the activity with carboxymethyl cellulose
-
-
?
filter paper + H2O
?
-
8.4% of the activity with carboxymethyl cellulose
-
-
?
filter paper + H2O
?
7.6% of the activity with carboxymethyl cellulose
-
-
?
filter paper + H2O
?
7.6% of the activtiy with carboxymethyl cellulose
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
-
-
-
?
filter paper + H2O
?
-
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
4% of the activity with carboxymethyl-cellulose. CBH6A and EgGH45, synergic effect, showing the highest efficiency in the ratio at 80:20
-
-
?
filter paper + H2O
?
8% of the activity with carboxymethyl-cellulose. CBH6A and EgGH45, synergic effect, showing the highest efficiency in the ratio at 80:20
-
-
?
filter paper + H2O
?
Sporotrichum pulverulentum
-
-
-
-
?
filter paper + H2O
?
-
best substrate of isoforms cellulase II and III
-
-
?
filter paper + H2O
?
Thermochaetoides thermophila
-
-
-
-
?
filter paper + H2O
?
Thermochaetoides thermophila CT2
-
-
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
-
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
-
-
-
?
glucan + H2O
?
-
barley beta-glucan
-
-
?
glucan + H2O
?
-
catalytic domain of endoglucanase G
-
-
?
glucan + H2O
?
-
barley beta-glucan
-
-
?
glucan + H2O
?
-
catalytic domain of endoglucanase G
-
-
?
glucan + H2O
?
-
barley beta-glucan
-
-
?
glucan + H2O
?
-
barley beta-glucan
-
-
?
glucan + H2O
?
-
yeast glucan
-
-
?
glucomannan + H2O
?
-
-
-
?
glucomannan + H2O
?
-
-
-
?
glucomannan + H2O
?
-
-
-
?
glucomannan + H2O
?
-
-
-
?
glucomannan + H2O
?
-
-
-
?
hydroxyethyl cellulose + H2O
?
-
-
-
-
?
hydroxyethyl cellulose + H2O
?
-
-
-
-
?
hydroxyethyl cellulose + H2O
?
-
-
-
-
?
hydroxyethyl cellulose + H2O
?
-
-
-
?
hydroxyethylcellulose + H2O
?
-
-
-
-
?
hydroxyethylcellulose + H2O
?
-
-
-
?
hydroxyethylcellulose + H2O
?
-
-
-
?
hydroxyethylcellulose + H2O
?
-
-
-
?
hydroxyethylcellulose + H2O
?
-
-
-
-
?
hydroxyethylcellulose + H2O
?
-
-
-
-
?
hydroxyethylcellulose + H2O
?
-
-
-
-
?
hydroxyethylcellulose + H2O
?
-
-
-
?
insoluble cellulose + H2O
?
-
e.g. Avicel, Solka-floc, Sigmacell 50
no glucose, cellobiose and short chain celloolifgosaccharides are formed
-
?
insoluble cellulose + H2O
?
-
e.g. Avicel, Solka-floc, Sigmacell 50
no glucose, cellobiose and short chain celloolifgosaccharides are formed
-
?
konac glucomannan + H2O
?
-
-
-
?
konac glucomannan + H2O
?
-
-
-
?
konjac mannan + H2O
?
-
-
-
?
konjac mannan + H2O
?
-
-
-
?
laminarin + H2O
?
9.1% of the activity with barley beta-glucan
-
-
?
laminarin + H2O
?
9.1% of the activity with barley beta-glucan
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
5% of the activity with carboxymethyl cellulose
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
cellulase I
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
low activity
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
6% of the activity with carboxymethylcellulose
-
-
?
lichenan + H2O
?
-
enzyme form EGD
-
-
?
lichenan + H2O
?
-
the smallest product is a disaccharide
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
94% of the activity on carboxymethyl cellulose
-
-
?
lichenan + H2O
?
53.2% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
53.2% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
-
and beta-glucan, preferred substrates
-
-
?
lichenan + H2O
?
-
and beta-glucan, preferred substrates
-
-
?
lichenan + H2O
?
-
endoglucanase A
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
30% of the activity with barley beta-glucan, catalytic domain of endoglucanase G
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
30% of the activity with barley beta-glucan, catalytic domain of endoglucanase G
-
-
?
lichenan + H2O
?
-
77% of the activity with carboxymethyl cellulose
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
60.5% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
60.5% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
9% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
MG570051
157% of the activity with carboxymethylcellulose
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
the highest specific activity toward polysaccharides occurs with mixed-linkage (1->3),(1->4)-beta-D-glucans such as barley beta-D-glucan and lichenan
-
-
?
lichenan + H2O
?
weak activity
-
-
?
lichenan + H2O
?
activity of truncated enzyme form
-
-
?
lichenan + H2O
?
activity of truncated enzyme form
-
-
?
lichenan + H2O
?
best substrate
-
-
?
lichenan + H2O
?
best substrate
-
-
?
lichenan + H2O
?
best substrate
-
-
?
lichenan + H2O
?
activity is 120% compared to activity with carboxymethyl-cellulose
-
-
?
lichenan + H2O
?
130% of the activity with carboxymethyl cellulose
-
-
?
lichenan + H2O
?
130% of the activity with carboxymethyl cellulose
-
-
?
lichenan + H2O
?
-
380% of the activity with carboxymethyl cellulose
-
-
?
lichenan + H2O
?
-
380% of the activity with carboxymethyl cellulose
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
cellulase I, II and III
-
-
?
lichenan + H2O
?
Thermochaetoides thermophila
-
-
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
the enzyme hydrolyzes mixed linked beta-(1-3)(1-4) substrates such as barley glucan and lichenan more strongly than carboxymethylcellulose
-
-
?
lichenan + H2O
?
high activity
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenin + H2O
?
-
-
-
-
?
lichenin + H2O
?
best substrate
-
-
?
lignocellulose + H2O
?
-
solubilizes lignocellulose
-
-
?
lignocellulose + H2O
?
-
-
-
-
?
methylcellulose + H2O
?
-
-
-
-
?
methylcellulose + H2O
?
-
-
-
-
?
microcrystalline cellulose + H2O
?
-
endoglucanase 35
-
-
?
microcrystalline cellulose + H2O
?
-
endoglucanase 47
-
-
?
N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
?
-
-
-
?
N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
?
-
-
-
?
N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate + H2O
?
-
-
-
?
o-nitrophenyl beta-cellobioside + H2O
?
-
-
-
-
?
o-nitrophenyl beta-cellobioside + H2O
?
-
-
-
-
?
o-nitrophenyl beta-cellobioside + H2O
?
-
-
-
-
?
o-nitrophenyl beta-cellobioside + H2O
?
-
-
-
-
?
o-nitrophenyl beta-cellobioside + H2O
?
-
-
-
-
?
o-nitrophenyl beta-cellobioside + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
activity is 25% compared to activity with carboxymethyl-cellulose
-
-
?
oat spelt xylan + H2O
?
hydrolysed at 76% compared to the hydrolysis of carboxymethylcellulose
-
-
?
oat spelt xylan + H2O
?
-
92% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
oat spelt xylan + H2O
?
-
92% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
59% of the activity with carboxymethylcellulose
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
glucose + cellobiose + ?
Bacillus cellulyticus K-12
-
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
glucose + cellobiose + ?
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
glucose + cellobiose + ?
-
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
glucose + cellobiose + ?
-
cellulase III preferentially attacks the aglycone linkage
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
glucose + cellobiose + ?
-
cellulase II-A preferentially attacks the holoside linkage of p-nitrophenyl beta-D-cellobioside, cellulase II-B attacks mainly the aglycone linkage. Synthesis of cellotriose from p-nitrophenyl beta-D-cellobioside by transfer of a glucosyl residue, possibly to cellobiose produced in the reaction mixture
-
-
?
p-nitrophenyl cellobiose + H2O
p-nitrophenol + cellobiose
-
-
-
?
p-nitrophenyl cellobiose + H2O
p-nitrophenol + cellobiose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG25
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG28
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG44
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG47
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG51
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
endoglucanase EG60
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
?
-
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
Thermochaetoides thermophila
-
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
Thermochaetoides thermophila CT2
-
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
fluorimetric determination in cellulase activity assay using calcofluor white
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid swollen cellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose
best substrate
-
-
?
phosphoric acid-swollen cellulose + H2O
?
-
-
-
?
phosphoric acid-swollen cellulose + H2O
?
-
-
-
-
?
phosphoric acid-swollen cellulose + H2O
?
-
-
-
?
phosphoric acid-swollen cellulose + H2O
?
-
weak
-
-
?
phosphoric acid-swollen cellulose + H2O
?
-
-
-
-
?
phosphoric acid-swollen cellulose + H2O
?
-
-
-
?
phosphoric acid-swollen cellulose + H2O
?
-
-
-
?
phosphoric acid-swollen cellulose + H2O
?
Thermochaetoides thermophila
-
low activity
-
-
?
phosphoric acid-swollen cellulose + H2O
?
Thermochaetoides thermophila CT2
-
low activity
-
-
?
phosphoric acid-swollen cellulose + H2O
?
-
-
-
?
phosphoric acid-swollen cellulose + H2O
?
-
-
-
-
?
phosphoric acid-treated wheat straw + H2O
?
-
74% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
phosphoric acid-treated wheat straw + H2O
?
-
74% saccharification within 36 h, preparation containing cellulase and xylanase
-
?
pretreated sorghum stover + H2O
?
-
-
-
-
?
pretreated sorghum stover + H2O
?
-
-
-
-
?
rice husk + H2O
?
-
-
-
-
?
rice husk + H2O
?
-
-
-
-
?
rice straw + H2O
?
-
-
-
-
?
rice straw + H2O
?
-
-
-
-
?
salicin + H2O
?
-
low activity
-
-
?
salicin + H2O
?
-
low activity
-
-
?
Sigmacell 101 + H2O
?
-
low activity, endo-beta-1,4-glucanase EG27
-
-
?
Sigmacell 101 + H2O
?
-
low activity, endo-beta-1,4-glucanase EG45
-
-
?
sodium carboxymethyl cellulose + H2O
?
-
-
-
-
?
sodium carboxymethyl cellulose + H2O
?
-
-
-
-
?
soluble cellodextrin + H2O
?
-
-
no glucose, cellobiose and short chain cellooligosaccharides are formed
-
?
soluble cellodextrin + H2O
?
-
-
no glucose, cellobiose and short chain cellooligosaccharides are formed
-
?
soybean husk + H2O
?
-
-
-
-
?
soybean husk + H2O
?
-
-
-
-
?
sugarcane bagasse + H2O
?
-
-
-
-
?
sugarcane bagasse + H2O
?
-
-
-
-
?
sugarcane bagasse + H2O
?
-
-
-
-
?
tamarind xyloglucan + H2O
?
-
-
-
?
tamarind xyloglucan + H2O
?
-
-
-
?
tamarind xyloglucan + H2O
?
-
-
-
?
tamarind xyloglucan + H2O
?
-
-
-
?
tamarind xyloglucan + H2O
?
-
-
-
?
tamarind xyloglucan + H2O
?
-
-
-
?
tamarind xyloglucan + H2O
?
-
-
-
?
Whatman filter paper + H2O
?
-
-
-
-
?
Whatman filter paper + H2O
?
-
-
-
-
?
wheat straw + H2O
?
-
-
-
-
?
wheat straw + H2O
?
-
-
-
-
?
wheat straw + H2O
?
-
-
-
-
?
wheat straw + H2O
?
-
-
-
-
?
xylan + H2O
?
-
the smallest product is a disaccharide
-
-
?
xylan + H2O
?
-
6.1% of the activity with carboxymethyl cellulose
-
?
xylan + H2O
?
Actinomyces sp. 40 Korean Native Goat 40
-
6.1% of the activity with carboxymethyl cellulose
-
?
xylan + H2O
?
beechwood xylan, 34% , and birchwood xylan, 31% of the activity on carboxymethyl cellulose, respectively
-
-
?
xylan + H2O
?
-
low acrtivity, endo-beta-1,4-glucanase EG27
-
-
?
xylan + H2O
?
-
low acrtivity, endo-beta-1,4-glucanase EG45
-
-
?
xylan + H2O
?
-
20% of the activity with carboxymethyl cellulose
-
?
xylan + H2O
?
-
20% of the activity with carboxymethyl cellulose
-
?
xylan + H2O
?
-
22.5% of the activity with carboxymethylcellulose
-
-
?
xylan + H2O
?
-
22.5% of the activity with carboxymethylcellulose
-
-
?
xylan + H2O
?
-
20.3% of the activity with carboxymethyl cellulose
-
-
?
xylan + H2O
?
-
20.3% of the activity with carboxymethyl cellulose
-
-
?
xylan + H2O
?
3.3% of the activity with carboxymethyl cellulose
-
-
?
xylan + H2O
?
-
about 2% of the activity with barley beta-glucan
-
-
?
xylan + H2O
?
weak activity
-
-
?
xylan + H2O
?
activity of truncated enzyme form
-
-
?
xylan + H2O
?
activity of truncated enzyme form
-
-
?
xyloglucan + H2O
?
-
71% of the activity with carboxymethyl cellulose
-
?
xyloglucan + H2O
?
-
71% of the activity with carboxymethyl cellulose
-
?
xyloglucan + H2O
?
isolated from tamarind
-
-
?
xyloglucan + H2O
?
isolated from tamarind
-
-
?
xyloglucan + H2O
?
-
-
-
?
xyloglucan + H2O
?
-
-
-
-
?
xyloglucan + H2O
?
-
as natural substrate in CEL7
-
-
?
xyloglucan + H2O
?
a beta-1,4-1,6-glucan, 40% activity compared to barley beta-glucan
-
-
?
6-O-methylcellulose + H2O
additional information
-
-
6-O-methylcellulose having every structural unit of them regioselectively substituted
glycosidic bond between two adjacent substituted units can be cleaved to give oligomers with a degree of polymerization of ca. 8
?
carboxymethyl cellulose + H2O
additional information
-
-
-
short glucose oligomers, cellobiose and a very small amount of glucose
-
?
carboxymethyl cellulose + H2O
additional information
-
-
-
short glucose oligomers, cellobiose and a very small amount of glucose
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
endoglucanase 1b: cellotriose, 45%, cellotetraose, 31%, cellobiose, 17%, and cellopentaose, 8%. Endoglucanase 2: cellotriose, 50%, and cellotetraose, 30%
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
Bacillus cellulyticus K-12
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
Bacillus sp. (in: Bacteria) No. 1139
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
Bacillus sp. (in: Bacteria) No. 1139
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
glucose + cellobiose
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
catalytic domain of endoglucanase G
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
catalytic domain of endoglucanase G
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
glucose + cellobiose + cellotriose + cellotetraose
?
carboxymethylcellulose + H2O
additional information
-
-
-
various cellooligosaccharides
?
carboxymethylcellulose + H2O
additional information
-
Lenzites trabea
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
mainly glucose with small amounts of cellobiose and cellotriose
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
mainly glucose with small amounts of cellobiose and cellotriose
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
hydrolyzed by cellulase I and III, no hydrolysis with cellulase II
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
endoglucanase E1 exhibits higher activity
endoglucanase E2 produces glucose, cellobiose, cellotriose and higher oligosaccharides. The major end product produced by endoglucanase E1 is cellobiose and small amounts of glucose
?
carboxymethylcellulose + H2O
additional information
-
Thermochaetoides thermophila
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
cellohexaose + H2O
additional information
-
-
-
-
?
cellohexaose + H2O
additional information
-
-
-
-
?
cellohexaose + H2O
additional information
-
-
-
cellotriose + glucose + cellobiose + cellotetraose
?
cellohexaose + H2O
additional information
-
-
-
cellotriose + cellobiose + cellotriose
?
cellohexaose + H2O
additional information
-
Bacillus cellulyticus K-12
-
-
cellobiose + cellotetraose
?
cellohexaose + H2O
additional information
-
-
-
cellobiose + cellotetraose
?
cellohexaose + H2O
additional information
-
-
-
cellotriose + cellobiose + cellotetraose
?
cellohexaose + H2O
additional information
-
-
-
cellotriose is formed and then slowly degraded
?
cellohexaose + H2O
additional information
-
-
cellulase A, B, and C
-
-
?
cellohexaose + H2O
additional information
-
-
-
-
?
cellohexaose + H2O
additional information
-
-
-
-
-
?
cellohexaose + H2O
additional information
-
-
-
-
-
?
cellohexaose + H2O
additional information
-
-
-
-
?
cellohexaose + H2O
additional information
-
-
-
cellotriose + cellobiose + cellotetraose
?
cellohexaose + H2O
additional information
-
-
-
-
-
?
cellohexaose + H2O
additional information
-
-
-
-
-
?
cellohexaose + H2O
additional information
-
-
-
-
-
?
cellohexaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
enzyme form EGB and EGC
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
cellobiose + cellotriose + glucose
?
cellopentaose + H2O
additional information
-
Bacillus cellulyticus K-12
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
cellotetraose + glucose
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
cellobiose + cellotriose
?
cellopentaose + H2O
additional information
-
-
-
cellobiose + cellotriose
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
cellulase A, B, and C
-
-
?
cellopentaose + H2O
additional information
-
-
hydrolyzed by endo-beta-1,4-glucanase component YEG1 and YEG2
cellobiose + cellotriose
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
cellobiose + cellotriose
?
cellopentaose + H2O
additional information
-
-
-
cellobiose + cellotriose
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
-
-
-
?
cellopentaose + H2O
additional information
-
-
beta-configuration of the anomeric carbon atoms is retained
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl-beta-D-glucoside
-
-
?
additional information
?
-
-
no activity with cellobiose
-
-
?
additional information
?
-
-
modular enzyme that contains a family 30 carbohydrate-binding modules, CBM, and a family 9 catalytic module at its N-terminal moiety. The CBM is extremely important not only because it mediates the binding of the enzyme to the substrate but also because it participates in the catalytic function of the enzyme or contributes to maintain the correct tertiary structure of the family 9 catalytic module for expressing enzyme activity
-
-
?
additional information
?
-
-
substrates are acid swollen cellulose, lichenan, beta-glucan, carboxymethyl cellulose, galactomannans, oat spelt xylan, avicel, and steam exploded bagasse, no activity glucomannan and laminarin
-
-
?
additional information
?
-
-
final hydrolysed product produced from carboxymethyl cellulose by chimera 1 is glucose confirming both beta-1,4-endoglucanase and beta-1,4-glucosidase activities, while the products of CtGH5-F194A point mutant are cellobiose and cello-oligosaccharides. Product indentification by thin layer chromatography. Enzymatic hydrolysis of 1% w/v Sorghum stalk pretreated by 1% NaOH by mutant CtGH5-F194A with or without wild-type enzyme CtGH1, which exhibits beta-glucosidase activity. No activity of the wild-type enzyme and mutant F194A with 4-nitrophenyl beta-D-glucoside, which is a substrate of the beta-glucosidase activity of chimeric mutant CtGH1-CtGH5-F194A
-
-
?
additional information
?
-
-
modular enzyme that contains a family 30 carbohydrate-binding modules, CBM, and a family 9 catalytic module at its N-terminal moiety. The CBM is extremely important not only because it mediates the binding of the enzyme to the substrate but also because it participates in the catalytic function of the enzyme or contributes to maintain the correct tertiary structure of the family 9 catalytic module for expressing enzyme activity
-
-
?
additional information
?
-
no substrae: cellobiose
-
-
?
additional information
?
-
-
the enzyme is able to hydrolyse sugarcane bagasse, rice husk, and wheat bran, with the highest production of reducers/fermentable sugars within 24 h of saccharification for wheat bran (137.21 mg/g). Saccharification of agroindustrial residues, overview
-
-
?
additional information
?
-
-
the enzyme is able to hydrolyse sugarcane bagasse, rice husk, and wheat bran, with the highest production of reducers/fermentable sugars within 24 h of saccharification for wheat bran (137.21 mg/g). Saccharification of agroindustrial residues, overview
-
-
?
additional information
?
-
-
endo-beta-1,4-glucanase EG27 shows no activity with p-nitrophenyl-beta-D-cellobiose, salicin and starch
-
-
?
additional information
?
-
-
endo-beta-1,4-glucanase EG45 shows no activity with p-nitrophenyl-beta-D-cellobiose, salicin and starch
-
-
?
additional information
?
-
enzyme displays weak activity on weak on locust bean galactomannan, avicel, and filter paper
-
-
?
additional information
?
-
-
enzyme displays weak activity on weak on locust bean galactomannan, avicel, and filter paper
-
-
?
additional information
?
-
enzyme displays weak activity on weak on locust bean galactomannan, avicel, and filter paper
-
-
?
additional information
?
-
hydrolysis of rice and corn straws
-
-
?
additional information
?
-
-
hydrolysis of rice and corn straws
-
-
?
additional information
?
-
hydrolysis of rice and corn straws
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl-beta-D-glucoside
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl-beta-D-glucoside
-
-
?
additional information
?
-
-
no activity with cellobiose
-
-
?
additional information
?
-
-
no activity with cellobiose
-
-
?
additional information
?
-
no substrate: cellulose
-
-
?
additional information
?
-
no substrate: cellulose
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
Bacillus cellulyticus K-12
-
hydrolysis of filter paper
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
substrate specificity, overview. Poor activity with Avicel PH-101
-
-
?
additional information
?
-
-
enzyme displays both beta-glucosidase, EC 3.2.1.21, and cellulase activities
-
-
?
additional information
?
-
-
enzyme displays both beta-glucosidase, EC 3.2.1.21, and cellulase activities
-
-
?
additional information
?
-
-
trans-glucosidase activity also observed
-
-
?
additional information
?
-
-
investigation of substrate specificity
-
-
?
additional information
?
-
-
starch as a substrate shows a relative activity of 0% and xlycan shows a relative activity of 0.9%
-
-
?
additional information
?
-
-
the organism possesses carboxymethyl cellulase and cellulase activities, overview
-
-
?
additional information
?
-
enzyme hydrolyzes soluble cellulose substrates containing beta-1,4-linkages, such as carboxylmethyl cellulose and konjac glucomannan, but has no exoglucanase and beta-glucosidase activities
-
-
?
additional information
?
-
-
enzyme hydrolyzes soluble cellulose substrates containing beta-1,4-linkages, such as carboxylmethyl cellulose and konjac glucomannan, but has no exoglucanase and beta-glucosidase activities
-
-
?
additional information
?
-
enzyme hydrolyzes soluble cellulose substrates containing beta-1,4-linkages, such as carboxylmethyl cellulose and konjac glucomannan, but has no exoglucanase and beta-glucosidase activities
-
-
?
additional information
?
-
-
investigation of substrate specificity
-
-
?
additional information
?
-
-
starch as a substrate shows a relative activity of 0% and xlycan shows a relative activity of 0.9%
-
-
?
additional information
?
-
-
the organism possesses carboxymethyl cellulase and cellulase activities, overview
-
-
?
additional information
?
-
Bacillus sp. (in: Bacteria) No. 1139
-
trans-glucosidase activity also observed
-
-
?
additional information
?
-
-
wild-type and mutant can not hydrolyze Avicel, laminarin and chitosan
-
-
?
additional information
?
-
-
the enzyme shows multisubstrate specificity, showing significantly higher activity with lichenan and beta-glucan and lower activity with laminarin, hydroxyethylcellulose, and steam exploded bagasse
-
-
?
additional information
?
-
-
no substrates: 4-nitrophenyl beta-D-glucopyranoside, cellulose
-
-
?
additional information
?
-
-
no substrates: alpha-glucan, cellobiose and xylan
-
-
?
additional information
?
-
-
the enzyme shows multisubstrate specificity, showing significantly higher activity with lichenan and beta-glucan and lower activity with laminarin, hydroxyethylcellulose, and steam exploded bagasse
-
-
?
additional information
?
-
-
wild-type and mutant can not hydrolyze Avicel, laminarin and chitosan
-
-
?
additional information
?
-
-
no substrates: alpha-glucan, cellobiose and xylan
-
-
?
additional information
?
-
-
no substrates: 4-nitrophenyl beta-D-glucopyranoside, cellulose
-
-
?
additional information
?
-
no substrate: cellotriose, insoluble cellulose, avicel, birchwood xylan, oat grass xylan, laminarin, soluble chitin
-
-
?
additional information
?
-
Bellamya chinensis laeta UM-2014
no substrate: cellotriose, insoluble cellulose, avicel, birchwood xylan, oat grass xylan, laminarin, soluble chitin
-
-
?
additional information
?
-
Bgl7A can effectively hydrolyze beta-1,4 bonds and some beta-1,3 linkages in beta-glucan. Belonging to the group of non-specific endoglucanase, Bgl7A can hydrolyze not only beta-glucan and cellulose but also laminarin and oat spelt xylan
-
-
?
additional information
?
-
poor activity with laminarin and oat spelt xylan, no activity with Avicel
-
-
?
additional information
?
-
no activity with tamarind xyloglucan, barley (1-3)(1-4)-beta-D-glucan, wheat arabinoxylan or birchwood xylan
-
-
?
additional information
?
-
-
cellobiose and xylan are no substrates
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
-
inverting glycoside hydrolases catalyze bond cleavage using a single-displacement mechanism involving the participation of two acidic amino acid residues positioned opposite each other across the active site cleft or tunnel
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme harbors a carbohydrate binding module CBM2 and a glycoside hydrolase family 6 domain
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
the enzyme strongly binds to filter paper despite having no recognizable carbohydrate binding module. No activity with cellotriose, 2,4-dinitrophenyl beta-cellobioside and 6-chloro-4-methylumbelliferyl beta-cellobioside. No cleavage of the internal beta-1,3-linkage is detected
-
-
?
additional information
?
-
no activity on Avicel or xylan
-
-
?
additional information
?
-
-
no activity on Avicel or xylan
-
-
?
additional information
?
-
no activity on Avicel or xylan
-
-
?
additional information
?
-
-
glucanase hydrolyses beta-1,4-glycosidic bonds
-
-
?
additional information
?
-
-
glucanase hydrolyses beta-1,4-glycosidic bonds
-
-
?
additional information
?
-
-
CcCel6C exhibits high cellobiohydrolase activity
-
-
?
additional information
?
-
hydrolyzing internal beta-1,4-glycosidic bonds and resulting in a smear of polymers with different lengths. The hydrolytic products of tCfEG are one unit sugar less than those produced by nCfEG
-
-
?
additional information
?
-
-
hydrolyzing internal beta-1,4-glycosidic bonds and resulting in a smear of polymers with different lengths. The hydrolytic products of tCfEG are one unit sugar less than those produced by nCfEG
-
-
?
additional information
?
-
carboxymethyl cellulose sodium salt is a better substrate than insoluble cellulose substrate such as Avicel (0 U/mg), SIGMACELL cellulose (0 U/mg), and CM cellulose
-
-
?
additional information
?
-
no substrates: cellobiose and cellotriose
-
-
?
additional information
?
-
-
no substrates: cellobiose and cellotriose
-
-
?
additional information
?
-
-
Cel9A does not cleave xylan
-
-
?
additional information
?
-
EBI-244 is active on a range of high molecular weight carbohydrate substrates containing beta-1,4-linked glucose, including carboxymethyl cellulose, Avicel, and filter paper, it is active toward 4-nitrophenyl-cellobioside but inactive toward 4-nitrophenyl-glucoside
-
-
?
additional information
?
-
enzyme shows high endo-beta-1,4-mannanase activity versus various mannans, but low endo-beta-1,4 glucanase activity towards carboxymethylcellulose, andd negligible activity towards glucomannans
-
-
?
additional information
?
-
enzyme shows high endo-beta-1,4-mannanase activity versus various mannans, but low endo-beta-1,4 glucanase activity towards carboxymethylcellulose, andd negligible activity towards glucomannans
-
-
?
additional information
?
-
-
when the oligosaccharides are modified by reduction with sodium borotritide, the second linkage from the reducing end becomes significantly susceptible to the enzyme and is preferentially cleaved
-
-
?
additional information
?
-
-
no substrates: cellotriose, cellobiose
-
-
?
additional information
?
-
the enzyme shows high affinity for carboxymethyl cellulose, but is also active with other substrates like beta-1,4-linked polysaccharides, including xyloglucan, glucomannan, beta-glucan, lichenin, and galactomannan
-
-
?
additional information
?
-
-
the enzyme shows high affinity for carboxymethyl cellulose, but is also active with other substrates like beta-1,4-linked polysaccharides, including xyloglucan, glucomannan, beta-glucan, lichenin, and galactomannan
-
-
?
additional information
?
-
the enzyme shows high affinity for carboxymethyl cellulose, but is also active with other substrates like beta-1,4-linked polysaccharides, including xyloglucan, glucomannan, beta-glucan, lichenin, and galactomannan
-
-
?
additional information
?
-
the enzyme shows high affinity for carboxymethyl cellulose, but is also active with other substrates like beta-1,4-linked polysaccharides, including xyloglucan, glucomannan, beta-glucan, lichenin, and galactomannan
-
-
?
additional information
?
-
-
no hydrolysis of laminarin
-
-
?
additional information
?
-
-
no hydrolysis of laminarin
-
-
?
additional information
?
-
the enzyme has a unique catalytic efficiency on beta-1,4-glucans rather than mixed beta-1,3/1,4-glucans as compared to other GH45 endoglucanases. No activity on Avicel and 4-nitrophenyl beta-D-cellobioside
-
-
?
additional information
?
-
the enzyme has a unique catalytic efficiency on beta-1,4-glucans rather than mixed beta-1,3/1,4-glucans as compared to other GH45 endoglucanases. No activity on Avicel and 4-nitrophenyl beta-D-cellobioside
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
-
no substrates: chitosan, amylose
-
-
?
additional information
?
-
-
glucanase hydrolyses mainly beta-1,4-glycosidic bonds but is also capable of significant hydrolysis of beta-1,3-glycosidic bonds
-
-
?
additional information
?
-
-
glucanase hydrolyses mainly beta-1,4-glycosidic bonds but is also capable of significant hydrolysis of beta-1,3-glycosidic bonds
-
-
?
additional information
?
-
-
the organism possesses carboxymethyl cellulase and cellulase activities, overview
-
-
?
additional information
?
-
-
the organism possesses carboxymethyl cellulase and cellulase activities, overview
-
-
?
additional information
?
-
-
substrate specificity, overview. The GtGH45 is able to convert all tested oligosaccharides to glucose, however, small amounts of cellobiose, cellotriose, and cellotetraose are detected in the reaction products, indicating that the enzyme cannot convert efficiently small oligosaccharides probably due their mode of recognition in the enzyme catalytic cleft. The degradation of C5 and C6 by GtGH45 is almost complete with glucose being a main product
-
-
?
additional information
?
-
enzyme is strictly specific for the beta-1,4-glucoside linkage exhibiting activity toward barley beta-glucan, lichenan, and carboxymethyl cellulose sodium salt, but not toward laminarin (1,3-beta-glucan), birchwood xylan, avicel, and not toward 4-nitrophenyl beta-D-glucoside or 4-nitrophenyl cellobioside. Cel6C cleaves the internal glycosidic linkages of cellooligosaccharides randomly, the predominant product of polysaccharide hydrolysis is cellobiose
-
-
?
additional information
?
-
enzyme is strictly specific for the beta-1,4-glucoside linkage exhibiting activity toward barley beta-glucan, lichenan, and carboxymethyl cellulose sodium salt, but not toward laminarin (1,3-beta-glucan), birchwood xylan, avicel, and not toward 4-nitrophenyl beta-D-glucoside or 4-nitrophenyl cellobioside. Cel6C cleaves the internal glycosidic linkages of cellooligosaccharides randomly, the predominant product of polysaccharide hydrolysis is cellobiose
-
-
?
additional information
?
-
-
no activity with cellobiose
-
-
?
additional information
?
-
the enzyme also shows chitosanase activity. Colloidal chitosan, chitosan and glycol chitosan are hydrolyzed by Cel8A at 15-40% the activity of cellulose
-
-
?
additional information
?
-
the enzyme also shows chitosanase activity. Colloidal chitosan, chitosan and glycol chitosan are hydrolyzed by Cel8A at 15-40% the activity of cellulose
-
-
?
additional information
?
-
Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
-
-
?
additional information
?
-
Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
-
-
?
additional information
?
-
Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
-
-
?
additional information
?
-
-
Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
-
-
?
additional information
?
-
-
no substrate: 4-methylumbelliferyl-beta-D-lactoside
-
-
?
additional information
?
-
no substrate: 4-methylumbelliferyl-beta-D-lactoside
-
-
?
additional information
?
-
-
no substrate: 4-methylumbelliferyl-beta-D-lactoside
-
-
?
additional information
?
-
no substrate: 4-methylumbelliferyl-beta-D-lactoside
-
-
?
additional information
?
-
-
no degradation of oat spelt xylan and larch wood xylan
-
-
?
additional information
?
-
-
no degradation of oat spelt xylan and larch wood xylan
-
-
?
additional information
?
-
-
no substrates: starch, xylan, cellobiose, filter paper
-
-
?
additional information
?
-
enzyme is most active against lichenan and beta-glucans and lesser active toward filter paper, carboxymethyl cellulose, and phosphoric acid-swollen cellulose
-
-
?
additional information
?
-
enzyme is most active against lichenan and beta-glucans and lesser active toward filter paper, carboxymethyl cellulose, and phosphoric acid-swollen cellulose
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
-
no hydrolysis of cellobioside, cellotrioside, cellotetraoside, laminarin, curdlan, xylan, p-nitrophenyl beta-D-cellotrioside and p-nitrophenyl beta-D-cellotetraoside
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
-
no hydrolysis of cellobioside, cellotrioside, cellotetraoside, laminarin, curdlan, xylan, p-nitrophenyl beta-D-cellotrioside and p-nitrophenyl beta-D-cellotetraoside
-
-
?
additional information
?
-
-
no activity with laminarin, avicel, pullulan and pachyman
-
-
?
additional information
?
-
MG570051
low hydrolytic activities, toward birchwood xylan and laminarin
-
-
?
additional information
?
-
-
effect of carbon source on enzyme activity
-
-
?
additional information
?
-
-
effect of carbon source on enzyme activity
-
-
?
additional information
?
-
-
distribution of cellulase between the residual substrate and supernatant during the course of enzymatic hydrolysis of steam-exploded wheat straw
-
-
?
additional information
?
-
-
distribution of cellulase between the residual substrate and supernatant during the course of enzymatic hydrolysis of steam-exploded wheat straw
-
-
?
additional information
?
-
-
cellulase preparations that perform best on hardwood also show superior performance on the softwood substrates
-
-
?
additional information
?
-
-
amino acids E209 and E319 act as proton donor and nucleophile in substrate catalytic domain
-
-
?
additional information
?
-
amino acids E209 and E319 act as proton donor and nucleophile in substrate catalytic domain
-
-
?
additional information
?
-
-
very poor or no substrates: laminarin, xyloglucan, birchwood xylan, arabinan, arabinoxylan, 4-nitrophenyl-beta-D-glucoside. Amino acids E209 and E319 act as proton donor and nucleophile in the catalytic domain
-
-
?
additional information
?
-
very poor or no substrates: laminarin, xyloglucan, birchwood xylan, arabinan, arabinoxylan, 4-nitrophenyl-beta-D-glucoside. Amino acids E209 and E319 act as proton donor and nucleophile in the catalytic domain
-
-
?
additional information
?
-
-
very poor substrates: laminarin, xyloglucan. No substrates: birchwood xylan, arabinan, arabinoxylan, 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
very poor substrates: laminarin, xyloglucan. No substrates: birchwood xylan, arabinan, arabinoxylan, 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
very poor substrates: laminarin, xyloglucan, no substrates: birchwood xylan, arabinan, arabinoxylan, mannan, 4-nitrophenyl beta-D-glucopyranoside
-
-
?
additional information
?
-
-
very poor substrates: laminarin, xyloglucan, no substrates: birchwood xylan, arabinan, arabinoxylan, mannan, 4-nitrophenyl beta-D-glucopyranoside
-
-
?
additional information
?
-
no substrates: avicel, arabinoxylan and xyloglucan
-
-
?
additional information
?
-
no activity against birchwood xylan, 4-nitrophenyl cellobiose, 4-nitrophenyl beta-D-glucoside
-
-
?
additional information
?
-
no activity against birchwood xylan, 4-nitrophenyl cellobiose, 4-nitrophenyl beta-D-glucoside
-
-
?
additional information
?
-
-
no activity with cellobiose
-
-
?
additional information
?
-
-
no activity with crystalline cellulose or cellobiose
-
-
?
additional information
?
-
-
beta-1,4-endoglucanases show activities of the cleavage of the cellulose backbone due to an endocleavage. Oligosaccharides of different lengths as well as cellobiose and glucose are formed
-
-
?
additional information
?
-
EglA hydrolyzes shorter cellodextrins (DP <5) as well as the amorphous portions of polysaccharides which contain only beta-1,4 bonds such as carboxymethyl cellulose, microcrystalline cellulose, Whatman paper, and cotton linter. Kinetics studies with cellooliogsaccharides and p-nitrophenyl-cellooligosaccharides indicated that the enzyme had three glucose binding subsites (-I, -II, and -III) for the nonreducing end and two glucose binding subsites (+I and +II) for the reducing end from the scissile glycosidic linkage. No activity is detected on solely beta-1,3-linked oligosaccharides or polysaccharides
-
-
?
additional information
?
-
with substrate cellulose, the substrate position is fixed by the alignment of one cellobiose unit between the two aromatic amino acid residues at subsites +1 and +2. During the enzyme reaction, the glucose structure of cellulose substrates is distorted at subsite -1, and the beta-1,4-glucoside bond between glucose moieties is twisted between subsites -1 and +1. Subsite -2 specifically recognizes the glucose residue, but recognition by subsites +1 and +2 is loose during the enzyme reaction. This type of recognition is important for creation of the distorted boat form of the substrate at subsite -1
-
-
?
additional information
?
-
-
with substrate cellulose, the substrate position is fixed by the alignment of one cellobiose unit between the two aromatic amino acid residues at subsites +1 and +2. During the enzyme reaction, the glucose structure of cellulose substrates is distorted at subsite -1, and the beta-1,4-glucoside bond between glucose moieties is twisted between subsites -1 and +1. Subsite -2 specifically recognizes the glucose residue, but recognition by subsites +1 and +2 is loose during the enzyme reaction. This type of recognition is important for creation of the distorted boat form of the substrate at subsite -1
-
-
?
additional information
?
-
-
hydrolysis of phosphoric-acid swollen filter paper
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
enzyme displays broad substrate specificity and exhibits high activity on substrates containing beta-1,4-glycosidic bonds and beta-1,3-glycosidic bonds such as barley beta-glucan, laminarin, lichenan, carboxymethyl cellulose, carob bean gum, and birchwood xylan
-
-
?
additional information
?
-
no substrates: avicel, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-cellobioside
-
-
?
additional information
?
-
-
hydrolysis of phosphoric-acid swollen filter paper
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
enzyme does not release reducing sugars from Avicel microcrystalline cellulose, cellobiose, polygalacturonate, locust bean gum, xylan, Rhizobium leguminosarum bv. trifolii acidic heteropolysaccharide EPS types I, II, or III, or Sinorhizobium meliloti succinoglycan exopolysaccharide. Enzyme has a high substrate specificity for noncrystalline cellulose
-
-
?
additional information
?
-
-
enzyme does not release reducing sugars from Avicel microcrystalline cellulose, cellobiose, polygalacturonate, locust bean gum, xylan, Rhizobium leguminosarum bv. trifolii acidic heteropolysaccharide EPS types I, II, or III, or Sinorhizobium meliloti succinoglycan exopolysaccharide. Enzyme has a high substrate specificity for noncrystalline cellulose
-
-
?
additional information
?
-
enzyme does not release reducing sugars from Avicel microcrystalline cellulose, cellobiose, polygalacturonate, locust bean gum, xylan, Rhizobium leguminosarum bv. trifolii acidic heteropolysaccharide EPS types I, II, or III, or Sinorhizobium meliloti succinoglycan exopolysaccharide. Enzyme has a high substrate specificity for noncrystalline cellulose
-
-
?
additional information
?
-
-
no activity with avicell, xylan, galactan, arabinan, mannan or laminarin
-
-
?
additional information
?
-
-
no activity with Avicel, cotton, laminarin, and cellobiose
-
-
?
additional information
?
-
-
no hydrolysis of laminarin
-
-
?
additional information
?
-
-
no activity with cellobiose
-
-
?
additional information
?
-
no activity with p-nitrophenyl cellobiose
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl cellobiose
-
-
?
additional information
?
-
-
no cleavage of cellotetraose, cellotriose and p-nitrophenyl-cellobiose
-
-
?
additional information
?
-
-
no activity with cellobiose
-
-
?
additional information
?
-
-
no activity with cellobiose
-
-
?
additional information
?
-
the crude enzyme releases reducing sugars from acid-pretreated straw at 75-85°C
-
-
?
additional information
?
-
the crude enzyme releases reducing sugars from acid-pretreated straw at 75-85°C
-
-
?
additional information
?
-
the crude enzyme releases reducing sugars from acid-pretreated straw at 75-85°C
-
-
?
additional information
?
-
no hydrolysis of p-nitrophenyl-beta-D-cellobioside and p-nitrophenyl-beta-D-cellotrioside, no exocellulase activity
-
-
?
additional information
?
-
-
no hydrolysis of p-nitrophenyl-beta-D-cellobioside and p-nitrophenyl-beta-D-cellotrioside, no exocellulase activity
-
-
?
additional information
?
-
the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
-
-
?
additional information
?
-
the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
-
-
?
additional information
?
-
-
the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
-
-
?
additional information
?
-
the enzyme has a beta-1,4 hydrolytic mode of action. It shows no significant activity on PCM3/pachyman, microcrystalline cellulose, or on oat xylan. Concentrated solutions (8090% v/v) of ionic liquids such as 1-ethyl-3-methylimidazolium acetate and 1,3-dimethylimidazolium dimethylphosphate are able to dissolve crystalline cellulose like AvicelW and cell wall polysaccharides, making them more accessible to hydrolytic enzymes
-
-
?
additional information
?
-
-
the enzyme has a beta-1,4 hydrolytic mode of action. It shows no significant activity on PCM3/pachyman, microcrystalline cellulose, or on oat xylan. Concentrated solutions (8090% v/v) of ionic liquids such as 1-ethyl-3-methylimidazolium acetate and 1,3-dimethylimidazolium dimethylphosphate are able to dissolve crystalline cellulose like AvicelW and cell wall polysaccharides, making them more accessible to hydrolytic enzymes
-
-
?
additional information
?
-
no substrates: PCM3/pachyman, avicel, oat xylan
-
-
?
additional information
?
-
-
no substrates: PCM3/pachyman, avicel, oat xylan
-
-
?
additional information
?
-
no substrates: cellotriose, cellobiose, p-nitrophenyl beta-D-cellobioside and p-nitrophenyl beta-D-cellotrioside, xylan, laminarin and lichenan, crystalline cellulose
-
-
?
additional information
?
-
-
no substrates: cellotriose, cellobiose, p-nitrophenyl beta-D-cellobioside and p-nitrophenyl beta-D-cellotrioside, xylan, laminarin and lichenan, crystalline cellulose
-
-
?
additional information
?
-
no substrates: cellotriose, cellobiose, p-nitrophenyl beta-D-cellobioside and p-nitrophenyl beta-D-cellotrioside, xylan, laminarin and lichenan, crystalline cellulose
-
-
?
additional information
?
-
the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
-
-
?
additional information
?
-
the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
-
-
?
additional information
?
-
-
the enzyme does not hydrolyse 4-nitrophenyl beta-D-cellobioside and 4-nitrophenyl beta-D-cellotrioside. No activity could be detected with crystalline cellulose at both acidic and neutral pH values
-
-
?
additional information
?
-
the enzyme has a beta-1,4 hydrolytic mode of action. It shows no significant activity on PCM3/pachyman, microcrystalline cellulose, or on oat xylan. Concentrated solutions (8090% v/v) of ionic liquids such as 1-ethyl-3-methylimidazolium acetate and 1,3-dimethylimidazolium dimethylphosphate are able to dissolve crystalline cellulose like AvicelW and cell wall polysaccharides, making them more accessible to hydrolytic enzymes
-
-
?
additional information
?
-
no substrates: PCM3/pachyman, avicel, oat xylan
-
-
?
additional information
?
-
-
carboxymethyl cellulose and beta-glucan are the best substrates with relative activities of 100% and 83%, respectively, birch wood xylan and oat spelt xylan have moderate activities of 68% and 60%, respectively, which otherwise supports low level of cellulase activity, Avicel has the lowest activity of 12%, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme does not degrade curdran, xylan, laminarin and pectin (0.5% each) at all
-
-
?
additional information
?
-
-
the enzyme does not degrade curdran, xylan, laminarin and pectin (0.5% each) at all
-
-
?
additional information
?
-
-
possible role of the enzyme in the softening of pericarp tissue and in the liquefaction of locules that takes place during ripening. Cel1 EGase responds to pathogen infection and supports a relationship between EGases, plant defense responses and fruit ripening. mRNA abundance is down-regulated in response to fungal infection. It is rapidly reduced 1 day after pathagen infection and completely suppressed 4 days after infection
-
-
?
additional information
?
-
-
enzyme is essential for growth and development of potato cyst nematodes
-
-
?
additional information
?
-
-
possible role of the enzyme in the softening of pericarp tissue and in the liquefaction of locules that takes place during ripening. Cel1 EGase responds to pathogen infection and supports a relationship between EGases, plant defense responses and fruit ripening. mRNA abundance is down-regulated in response to fungal infection. It is rapidly reduced 1 day after pathagen infection and completely suppressed 4 days after infection
-
-
?
additional information
?
-
bioconversion of the pretreated Arundo donax lignocellulosic biomass by wild-type and mutant enzymes
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
beta-1,3-linkages, alpha-1,6-linkages and beta-1,6-linkages are also susceptible to hydrolysis
-
-
?
additional information
?
-
no substrates: laminarin, curdlan
-
-
?
additional information
?
-
-
no substrates: laminarin, curdlan
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
-
no substrates: beta-1,4-mannan, beta-1,4-glycol, chitosan or chitin
-
-
?
additional information
?
-
-
Arg78 participates in catalysis
-
-
?
additional information
?
-
-
Cel9A presents both exo- and endo-cellulase activities, reaction mode, existence of an active conformer prior to ligand binding, overview
-
-
?
additional information
?
-
Thermochaetoides thermophila
-
hydrolysis of cotton
-
-
?
additional information
?
-
Thermochaetoides thermophila
-
the enzyme does not hydrolyze cellobiose and cellotriose
-
-
?
additional information
?
-
Thermochaetoides thermophila
synergistic biodegradation of waste papers using a combination of thermostable endoglucanase CTendo45 and cellobiohydrolase CtCel6 from Chaetomium thermophilum. CtCel6 significantly enhances the bioconversion process, and CTendo45 synergistically increases the degradation, with a maximum degree of synergistic effect of 1.67 when the mass ratio of CTendo45/CtCel6 is 5:3. Enzymatic hydrolysis of different paper materials, e.g. filter paper and office paper giving high activity, or newspaper and cardboard resulting in low activity, foolscap paper gives moderate activity. For newspaper, the recalcitrance to the enzymatic action may be caused by the high contents of hemicelluloses, lignin and various inorganic components
-
-
?
additional information
?
-
Thermochaetoides thermophila
the bifunctional enzyme also shows endoxylanase activity (EC 3.2.1.8) hydrolyzing beta-1,4-D-xylan from beechwood. Substrate specificity, overview. No endoglucanase activity on (+)-arabinogalactan, D-galacto-D-mannan, amylose, chitin, and sucrose. The enzyme shows activity with pretreated wheat straw and filter paper. CTendo7 produces cellooligosaccharides and xylooligosaccharides from the continuous enzymatic saccharification of carboxymethyl cellulose-Na and xylan, respectively
-
-
?
additional information
?
-
Thermochaetoides thermophila CBS 144.50
synergistic biodegradation of waste papers using a combination of thermostable endoglucanase CTendo45 and cellobiohydrolase CtCel6 from Chaetomium thermophilum. CtCel6 significantly enhances the bioconversion process, and CTendo45 synergistically increases the degradation, with a maximum degree of synergistic effect of 1.67 when the mass ratio of CTendo45/CtCel6 is 5:3. Enzymatic hydrolysis of different paper materials, e.g. filter paper and office paper giving high activity, or newspaper and cardboard resulting in low activity, foolscap paper gives moderate activity. For newspaper, the recalcitrance to the enzymatic action may be caused by the high contents of hemicelluloses, lignin and various inorganic components
-
-
?
additional information
?
-
Thermochaetoides thermophila DSM 1495
synergistic biodegradation of waste papers using a combination of thermostable endoglucanase CTendo45 and cellobiohydrolase CtCel6 from Chaetomium thermophilum. CtCel6 significantly enhances the bioconversion process, and CTendo45 synergistically increases the degradation, with a maximum degree of synergistic effect of 1.67 when the mass ratio of CTendo45/CtCel6 is 5:3. Enzymatic hydrolysis of different paper materials, e.g. filter paper and office paper giving high activity, or newspaper and cardboard resulting in low activity, foolscap paper gives moderate activity. For newspaper, the recalcitrance to the enzymatic action may be caused by the high contents of hemicelluloses, lignin and various inorganic components
-
-
?
additional information
?
-
Thermochaetoides thermophila IMI 039719
synergistic biodegradation of waste papers using a combination of thermostable endoglucanase CTendo45 and cellobiohydrolase CtCel6 from Chaetomium thermophilum. CtCel6 significantly enhances the bioconversion process, and CTendo45 synergistically increases the degradation, with a maximum degree of synergistic effect of 1.67 when the mass ratio of CTendo45/CtCel6 is 5:3. Enzymatic hydrolysis of different paper materials, e.g. filter paper and office paper giving high activity, or newspaper and cardboard resulting in low activity, foolscap paper gives moderate activity. For newspaper, the recalcitrance to the enzymatic action may be caused by the high contents of hemicelluloses, lignin and various inorganic components
-
-
?
additional information
?
-
-
no substrates: xylan, avicel, alpha-cellulose, filter paper, laminarin, curdlan
-
-
?
additional information
?
-
-
hydrolysis of cotton
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
-
hydrolysis of cotton
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
-
substrate specificity, overview. Enzyme MtGH45 is unable to hydrolyze C3 and C4 oligosaccharides, cellobiose and cellotriose are detected as the main products when the enzyme is incubated with cellopentaose, which is completely hydrolyzed and the incubation with cellohexaose generates cellobiose, cellotriose, and cellotetraose as main products
-
-
?
additional information
?
-
-
enzyme exhibits both endoglucanase and xylanase activites, reactions of EC 3.2.1.4 and 3.2.1.8, respectively
-
-
?
additional information
?
-
transglycosylation activity with smaller soluble cellooligosaccharides
-
-
?
additional information
?
-
substrate-binding mode of cellulase 12A, overview. A network of interactions exists between the enzyme and its substrate. The sugar residues bound to the enzyme appear to be more ordered in the 22 and 21 subsites than in the 11, 12 and 23 subsites. In the E134C crystals the bound 21 sugar at the cleavage site consistently show the alpha-anomeric configuration, implicating an intermediate-like structure
-
-
?
additional information
?
-
-
substrate-binding mode of cellulase 12A, overview. A network of interactions exists between the enzyme and its substrate. The sugar residues bound to the enzyme appear to be more ordered in the 22 and 21 subsites than in the 11, 12 and 23 subsites. In the E134C crystals the bound 21 sugar at the cleavage site consistently show the alpha-anomeric configuration, implicating an intermediate-like structure
-
-
?
additional information
?
-
-
no activity against starch and Avicel. The recombinant enzyme saccharifies pre-treated wheat straw and bagasse to 3.32% and 3.2%, respectively after 6 h incubation at 85°C
-
-
?
additional information
?
-
-
no activity against starch and Avicel. The recombinant enzyme saccharifies pre-treated wheat straw and bagasse to 3.32% and 3.2%, respectively after 6 h incubation at 85°C
-
-
?
additional information
?
-
-
among the processings of medicinal and aromatic plants, distillation waste of Cymbopogon winterianus, and bioprocessings of Artemisia annua (an industrial pharmaceutically important plant and source of artemisnin, an antimalarial compound) are selected on the basis of their capability to support higher levels of production of total cellulases, whereas garden waste, primarily consisting of Cynodon dactylon, is considered as the control, representing other lignocellulosic waste. Marc of Artemisia annua, a waste produced in huge amounts after the processing of the Artemisia annua herb, is found to be the suitable substrate for this fungus for maximizing the production of all three constituents of cellulase
-
-
?
additional information
?
-
-
among the processings of medicinal and aromatic plants, distillation waste of Cymbopogon winterianus, and bioprocessings of Artemisia annua (an industrial pharmaceutically important plant and source of artemisnin, an antimalarial compound) are selected on the basis of their capability to support higher levels of production of total cellulases, whereas garden waste, primarily consisting of Cynodon dactylon, is considered as the control, representing other lignocellulosic waste. Marc of Artemisia annua, a waste produced in huge amounts after the processing of the Artemisia annua herb, is found to be the suitable substrate for this fungus for maximizing the production of all three constituents of cellulase
-
-
?
additional information
?
-
-
hydrolysis of cotton
-
-
?
additional information
?
-
-
among the processings of medicinal and aromatic plants, distillation waste of Cymbopogon winterianus, and bioprocessings of Artemisia annua (an industrial pharmaceutically important plant and source of artemisnin, an antimalarial compound) are selected on the basis of their capability to support higher levels of production of total cellulases, whereas garden waste, primarily consisting of Cynodon dactylon, is considered as the control, representing other lignocellulosic waste. Marc of Artemisia annua, a waste produced in huge amounts after the processing of the Artemisia annua herb, is found to be the suitable substrate for this fungus for maximizing the production of all three constituents of cellulase
-
-
?
additional information
?
-
-
free cellulase compared with cellulase immobilized onto Si wafers and amino-terminated surfaces, amount of glucose produced by free cellulase is about 20% higher than that obtained from immobilized cellulase
-
-
?
additional information
?
-
-
the fungal enzyme binds specifically to cyst wall cellulose of Acanthamoeba ssp., which causes keratitis in human cornea, overview
-
-
?
additional information
?
-
-
cellulase preparations that perform best on hardwood also show superior performance on the softwood substrates
-
-
?
additional information
?
-
-
among the processings of medicinal and aromatic plants, distillation waste of Cymbopogon winterianus, and bioprocessings of Artemisia annua (an industrial pharmaceutically important plant and source of artemisnin, an antimalarial compound) are selected on the basis of their capability to support higher levels of production of total cellulases, whereas garden waste, primarily consisting of Cynodon dactylon, is considered as the control, representing other lignocellulosic waste. Marc of Artemisia annua, a waste produced in huge amounts after the processing of the Artemisia annua herb, is found to be the suitable substrate for this fungus for maximizing the production of all three constituents of cellulase
-
-
?
additional information
?
-
-
among the processings of medicinal and aromatic plants, distillation waste of Cymbopogon winterianus, and bioprocessings of Artemisia annua (an industrial pharmaceutically important plant and source of artemisnin, an antimalarial compound) are selected on the basis of their capability to support higher levels of production of total cellulases, whereas garden waste, primarily consisting of Cynodon dactylon, is considered as the control, representing other lignocellulosic waste. Marc of Artemisia annua, a waste produced in huge amounts after the processing of the Artemisia annua herb, is found to be the suitable substrate for this fungus for maximizing the production of all three constituents of cellulase
-
-
?
additional information
?
-
-
hydrolysis of cotton
-
-
?
additional information
?
-
-
hydrolysis of cotton
-
-
?
additional information
?
-
-
the low-molecular weight enzyme form is able to form free fibres from filter paper
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
-
hydrolysis of filter paper
-
-
?
additional information
?
-
-
the hydrolase exhibited chitosanase activity and cellulase activity
-
-
?
additional information
?
-
no activity towards the insoluble substrates crystalline cellulose and Avicel, and against curdlan, laminarin, xyloglucan, and xylan
-
-
?
additional information
?
-
enzyme displays highest specific activity against beta-1,4-glycosidic bonds of various linear glucan polysaccharides. Poor or no substrates: avicel, pachyman, laminarin, starch
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl cellobioside
-
-
?
additional information
?
-
Umcel9y-1 is an efficient endoglucanase and also exhibits high activities of exoglucanase and transglycosylation. The transglycosylation products of Umcel9y-1 including sophorose, laminaribiose, and gentiobiose, and transglycosylation are detected under all activated conditions. The decreasing order of catalytic efficiency for polysaccharides, cellooligosaccharides, and aryl-beta-glycosides is p-nitrophenyl-D-cellobioside, barley glucan, cellopentaose, cellotetraose, cellotriose, hydroxyethylcellulose, cellohexaose, laminarin, and carboxymethylcellulose, respectively
-
-
?
additional information
?
-
-
he later dominance of the dimeric product suggests that the trimer is slowly converted
-
-
?
additional information
?
-
no activity with starch
-
-
?
additional information
?
-
the enzyme is active with beta-D-glucans containing (1->3)- and (1->4)-bonds (EC 3.2.1.73, licheninase) and with beta-D-glucans containing only (1->4)-bonds (EC 3.2.1.4, cellulase). It shows an exclusive endoacting mechanism. No activity with 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-cellobioside, avicel, curdlan, laminarin, cellulose, carboxymethyl cellulose, and xylan
-
-
?
additional information
?
-
-
no hydrolysis of cellobiose
-
-
?
additional information
?
-
poor activity against filter paper and avicel
-
-
?
additional information
?
-
Rucel5B is active towards carboxymethyl cellulose, barley glucan, lichenan, pNPC, PASC, avicel and Whatman NO.1 filter paper, but not active towards laminarin, beta-1,6-glucan and birchwood xylan
-
-
?
additional information
?
-
-
no activity against crystalline forms of cellulose such as filter-paper or avicel and the beta-1,3-linked glucan laminarin. No activity with xylan
-
-
?
additional information
?
-
-
no hydrolysis of cellulose, cotton, oat splet xylan and birchwood xylan
-
-
?
additional information
?
-
-
enzymatic deinking experiments, the ink removal rate in samples treated with the catalytic module is only slightly higher (about 8%), than that of untreated controls, whereas that of the EG1-treated samples is 100% higher. Bio-stoning of denim with EG1-CM results in increases of 48% and 40% in weight loss and indigo dye removal, respectively compared with untreated controls. These increases are considerably lower than the corresponding values of 219% and 133% obtained when samples are treated with EG1
-
-
?
additional information
?
-
Xf818 carries out transglycosylation. The enzyme is unable to hydrolyse alpha-cellulose and laminarin (a beta-1,3 linked glucan)
-
-
?
additional information
?
-
-
Xf818 carries out transglycosylation. The enzyme is unable to hydrolyse alpha-cellulose and laminarin (a beta-1,3 linked glucan)
-
-
?
additional information
?
-
the enzyme consists of an N-terminal signal peptide, two glycosyl hydrolase family 5 catalytic modules, two novel carbohydrate-binding modules, two linker sequences, and a C-terminal sequence with an unknown function. Removal of the carbohydrate-binding modules from rCel5A reduces the catalytic activities with various polysaccharides remarkably
-
-
?
additional information
?
-
-
the enzyme consists of an N-terminal signal peptide, two glycosyl hydrolase family 5 catalytic modules, two novel carbohydrate-binding modules, two linker sequences, and a C-terminal sequence with an unknown function. Removal of the carbohydrate-binding modules from rCel5A reduces the catalytic activities with various polysaccharides remarkably
-
-
?
xylan + H2O
additional information
-
-
no activity
-
-
?
xylan + H2O
additional information
-
-
hydrolysis with endoglucanase B, no action with endoglucanase A and C
-
-
?
xylan + H2O
additional information
-
-
endoglucanase B
-
-
?
xylan + H2O
additional information
-
-
6% of the activity with barley beta-glucan with the insoluble xylan from oats spelt, 27% of the activity with barley beta-glucan with the soluble xylan from oats spelt, catalytic domain of endoglucanase G
-
-
?
xylan + H2O
additional information
-
Lenzites trabea
-
-
-
-
?
xylan + H2O
additional information
-
-
-
main products: cellobiose + cellotetraose
?
xylan + H2O
additional information
-
-
-
-
-
?
xylan + H2O
additional information
-
-
-
-
-
?
xylan + H2O
additional information
-
-
-
-
-
?
xylan + H2O
additional information
-
-
-
-
-
?
xylan + H2O
additional information
-
-
-
-
-
?
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1-butyl-3-methylimidazolium chloride
92.8% and 43.8% activity remaining in 10% and 20% 1-butyl-3-methylimidazolium chloride
1-butyl-3-methylimidazolium methylsulfate
-
the enzyme precipitates immediately on addition to the reaction mixture
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
100 mM, 98% inhibition
4-chloromercuribenzoate
-
5 mM, 90% of initial activity
4-hydroxybenzoic acid
-
-
acetonitril
-
11.4% inhibition at 5%
acetonitrile
-
10% v/v, 89% loss of activity
Al3+
Thermochaetoides thermophila
slight inhibition at 10 mM
alpha-chymotrypsin
-
denaturant
-
benzol
-
96.2% inhibition at 5%
butanol
-
10.9% inhibition at 5%
CaCl2
-
5 mM, 52% residual activity
carboxymethylcellulose
-
binding of the cellulose-binding domain to avicel is inhibited by carboxymethylcellulose, but not by barley beta-glucan and glucose at concentration of 0.1% and 0.5%
-
cetyltrimethylammonium bromide
1 mM, 31% residual activity
CoCl2
-
5 mM, 35% loss of activity
Cr2+
-
1 mM, 27% residual activity
CuSO4
-
5 mM, 38% residual activity
D-gluconic acid lactone
-
strong inhibition of membrane-bound cellulase
Dextran
-
partial inhibition of membrane-bound cellulase
diethyl dicarbonate
-
10 mM, 17.6% residual activity
Dimethylsulfoxide
-
30% v/v, 50% inhibition
EGTA
10 mM, 24% inhibition
FeCl2
-
5 mM, 38% residual activity
glucosamine
-
inhibition of CM-cellulase activity of enzyme E1, E3a, E3b and E4
guanidinium hydrochloride
72.2% at 3%
KMnO4
-
0.1 mM, complete inhibition of cellulase II-A
lactose
-
51000 Da subunit from the multicomponent cellulase complexes
lignin
-
at 45°C, lignin derived from acid hydrolyzed liquid hot water pretreated bagasse completely adsorbes cellulolytic enzymes from Trichoderma reesei within 90 min, while lignin derived from enzyme hydrolyzed liquid hot water pretreated bagasse adsorbes only 60% of Trichoderma reesei endoglucanase, exoglucanase and beta-glucosidase activities, overview. At 30°C, adsorption of all of the enzymes is minimal and enzyme hydrolysis at 30°C approaches that at 45°C after 168 h. Simultaneous saccharification and fermentation (SSF) and consolidated bioprocessing (CBP), both carried out at 30-32°C, offer viable options for mitigating lignin-derived inhibition effects. Method overview. Specific surface area and surface characteristics of lignocellulose particles
-
linear alkyl benzene sulfonate
LAS
methylcellulose
-
poor inhibitor of carboxymethylcellulase activity of enzyme form E3a, E3b and E4
-
MgCl2
-
5 mM, 52% residual activity
MnCl2
-
5 mM, 67% loss of activity
Monoiodoacetic acid
1 mM, 10% inhibition
NaN3
0.1%, 45.2% inhibition of activity with carboxymethyl cellulose, 12.25% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
o-phenanthroline
1 mM, 75% inhibition
p-chloromercuribenzoate
0.01 mM, 20% inhibition
Pb(CH3COO)2
-
34% inhibition at 1 mM
PbCl2
-
5 mM, 37% loss of activity
Phenylmethyl sulfonylfluoride
-
1 mM, 30% residual activity
phenylmethylsulfonyl fluoride
sodium dodecyl benzene sulfonate
-
-
sodium picryl sulfate
-
2 mM, cellulase I
SrCl2
-
5 mM, 36% loss of activity
starch
-
inhibits hydrolysis of glucan
Teepol
-
detergent, 0.1%, 80% inhibition
-
Tris
Tris almost completely suppresses CtCel9Q hydrolase activity, a Tris molecule is bound to three catalytic residues of CtCel9Q and occupies subsite -1 of the CtCel9Q active-site cleft, enzyme mutant crystal structure analysis, overview
Tween 20
31% inhibition at 20%
Tween-20
-
1%, 79% residual activity
2-mercaptoethanol
-
10 mM, 51% residual activity
2-mercaptoethanol
-
70% of initial activity
2-mercaptoethanol
-
5 mM, 82.3% residual activity, 50%, 48 h, crude enzyme preparation
Ag+
5 mM, no residual activity
Ag+
-
1 mM, 75% inhibition
Ag+
1 mM, 86% residual activity
Ag+
-
0.1 mM, strong inhibition
Ag+
-
AgNO3, endoglucanase E1 and E2
Ag+
Thermochaetoides thermophila
-
-
Ag+
Thermochaetoides thermophila
-
1 mM, 1% residual activity
Ag+
Thermochaetoides thermophila
23% inhibition at 1 mM, 68% inhibition at 5 mM; 5 mM, 62.5% loss of activity, substrate: xylan; 5 mM, 68.25% loss of activity, substrate: carboxymethyl cellulose
Ag+
Thermochaetoides thermophila
slight inhibition at 10 mM
Ag+
-
1 mM, partial inhibition
Ag+
complete inhibition at 5 mM
Ba2+
-
-
Ba2+
Thermochaetoides thermophila
-
-
Ba2+
Thermochaetoides thermophila
-
1 mM, 38% residual activity
Ba2+
-
1 mM, 79%inhibition
Ca2+
-
-
Ca2+
10 mM, 90% residual activity
Ca2+
5 mM, 52% residual activity
Ca2+
-
1 mM, slight inhibition
Ca2+
-
slight inhibition of endoglucanase E2 activity
Ca2+
-
5 mM, 76% residual activity
Ca2+
23.8% inhibition at 5 mM
Ca2+
-
1 mM, 74%inhibition
Ca2+
12.7% inhibition at 10 mM
Cd2+
10 mM, 16.5% residual activity
Cd2+
-
1 mM CdCl2, complete inhibition
Cd2+
2 mM, 70% of initial activity
Cd2+
10 mM, almost 30% loss of activity
Cd2+
-
14% inhibition at 10 mM
cellobiose
-
-
cellobiose
-
51000 Da subunit from the multicomponent cellulase complexes
cellobiose
Bacillus cellulyticus K-12
-
inhibits hydrolysis of carboxymethylcellulose and avicel
cellobiose
-
80 mM, 14% loss of activity, endoglucanase Z
cellobiose
very low activity against 4-methyl-umberriferyl-beta-D-lactoside is almost totally inhibited by 0.005 M cellobiose
cellobiose
-
5 mM, complete inhibition of carboxymethyl cellulose hydrolysis
cellobiose
-
inhibits hydrolysis of carboxymethylcellulose and avicel
cellobiose
the non-complete saccharification of cellulose by thr enzyme seems to be due to product-feedback inhibition by cellobiose
cellobiose
-
inhibition of endoglucanase E3a, E3b and E4
cellobiose
-
endoglucanase Cel 5A; endoglucanase Cel 7B
Co2+
5 mM, 90% of initial activity
Co2+
-
1 mM CoCl2, 44% inhibition
Co2+
5 mM, 37% residual activity
Co2+
-
5 mM, 76% residual activity
Co2+
MG570051
2 mM, less than 50% of initial activity
Co2+
-
5 mM, 43% of initial activity
Co2+
10 mM, almost 30% loss of activity
Co2+
Thermochaetoides thermophila
5 mM, 2% loss of activity, substrate: xylan
Co2+
Thermochaetoides thermophila
activates 38% at 2 mM, inhibits 20% at 10 mM
Co2+
-
1 mM, 62% residual activity
Co2+
-
1 mM, represses the enzyme activity up to 37%
Co2+
10.1% inhibition at 10 mM
Cr3+
-
Cr3+
5 mM, 34% residual activity
Cr3+
Thermochaetoides thermophila
-
Cu2+
-
inhibition of cellulose hydrolysis, no carboxymethylcellulose hydrolysis
Cu2+
10 mM, 27% residual activity
Cu2+
Bacillus cellulyticus K-12
-
CuCl2
Cu2+
-
1 mM, 40% residual activity
Cu2+
-
1 mM CuCl2, 41% inhibition
Cu2+
-
1 mM, 18% residual activity
Cu2+
-
5 mM, about 30% inhibition
Cu2+
-
1 mM, 72% of initial activity
Cu2+
5 mM, 38% residual activity
Cu2+
10 mM, almost 30% loss of activity
Cu2+
-
1 mM CuCl2, 55% inhibition
Cu2+
-
6.5% inhibition at 1 mM
Cu2+
5 mM, 41% residual activity
Cu2+
-
22% inhibition at 10 mM
Cu2+
5 mM, 1.6fold activation of activity with carboxymethyl cellulose, 16.4% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Cu2+
Thermochaetoides thermophila
-
-
Cu2+
Thermochaetoides thermophila
-
1 mM, 10% residual activity
Cu2+
Thermochaetoides thermophila
5 mM, complete loss of activity, substrate: carboxymethyl cellulose; 5 mM, complete loss of activity, substrate: xylan; 75% inhibition at 1 mM, complete inhibition at 5 mM
Cu2+
Thermochaetoides thermophila
complete inhibition at 2-10 mM
Cu2+
-
5 mM, 12% residual activity
Cu2+
-
1 mM, partial inhibition
Cu2+
complete inhibition at 5 mM
Cu2+
-
1 mM, 12% loss of activity
Cu2+
37.7% inhibition at 10 mM
dithiothreitol
-
10 mM, 67% residual activity
dithiothreitol
-
78% inhibition
EDTA
5 mM, 76% of initial activity
EDTA
10 mM, 58% residual activity
EDTA
-
5 mM, 75% loss of activity
EDTA
-
10 mM, 28% residual activity
EDTA
-
27% residual activity
EDTA
5 mM, complete inhibition of mutant enzyme DELTA1-90
EDTA
-
5 mM, 40% inhibition
EDTA
-
1 mM, 17% residual activity
EDTA
-
5 mM, 17.9% residual activity, 50%, 48 h, crude enzyme preparation
EDTA
-
10 mM, 11.2% residual activity
EDTA
1 mM, 91% residual activity
EDTA
5 mM, 68% residual activity
EDTA
-
5 mM, 63% of initial activity
EDTA
-
1 mM, 55% inhibition
EDTA
5 mM, 46% residual activity
EDTA
5 mM, 90.6% inhibition of activity with carboxymethyl cellulose, 1.1fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
EDTA
-
1 mM, 66% residual activity
EDTA
5 or 10 mM of EDTA reduce barley beta-glucan hydrolysis by 39% and 34%, respectively
EDTA
-
50 mM, 14% inhibition
ethanol
5%, 16% inhibition of activity with carboxymethyl cellulose, 24% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
ethanol
-
30% v/v, 92% loss of activity
Fe2+
-
-
Fe2+
-
1 mM, 55% inhibition
Fe2+
10 mM, 30% residual activity
Fe2+
-
10% inhibition at 5 mM
Fe2+
-
1 mM, 37% residual activity
Fe2+
-
1 mM, 65% residual activity
Fe2+
-
complete inhibition
Fe2+
-
5 mM, 77% of initial activity
Fe2+
10 mM, complete inhibition
Fe2+
-
1 mM FeCl2, 13% inhibition
Fe2+
-
2 mM, 67% inhibition
Fe2+
5 mM, 2.9fold activation of activity with carboxymethyl cellulose, 6.7% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Fe2+
Thermochaetoides thermophila
-
-
Fe2+
Thermochaetoides thermophila
-
1 mM, no residual activity
Fe2+
-
complete inhibition
Fe2+
complete inhibition at 5 mM
Fe3+
-
-
Fe3+
-
39% inhibition by 0.1 mM, 52% inhibition by 1 mM
Fe3+
-
5 mM, 5% residual activity
Fe3+
-
1.0 mM, significant inhibition
Fe3+
5 mM, 1.1fold activation of activity with carboxymethyl cellulose, 9.1% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Fe3+
Thermochaetoides thermophila
14% inhibition at 1 mM, 70% inhibition at 5 mM; 5 mM, 70.3% loss of activity, substrate: carboxymethyl cellulose; 5 mM, 78.5% loss of activity, substrate: xylan
Fe3+
Thermochaetoides thermophila
complete inhibition at 2-10 mM
Fe3+
-
1 mM, 62% residual activity
Fe3+
61.4% inhibition at 5 mM
Fe3+
-
1 mM, 73% inhibition
glucose
-
162 mM, 23% loss of activity, endoglucanase Z
glucose
-
moderate inhibition
glucose
-
end-product inhibition, 70% loss of activity by 0.3% glucose
glucose
-
29 mM, 12% inhibition of endoglucanase E4, no inhibition of endoglucanase E1 and E3a
Hg2+
-
inhibition of cellulose hydrolysis and carboxymethylcellulose hydrolysis
Hg2+
-
1 mM, 67% inhibition
Hg2+
-
1 mM, 67% inhibition
Hg2+
-
73.5% inhibition at 5 mM
Hg2+
Bacillus cellulyticus K-12
-
HgCl2
Hg2+
-
1 mM, 30% residual activity
Hg2+
-
1 mM HgCl2, complete inhibition
Hg2+
-
21% inhibition at 1 mM
Hg2+
5 mM, 45% residual activity
Hg2+
-
5 mM, 10% residual activity
Hg2+
-
1 mM, 40% residual activity
Hg2+
-
5 mM, 46% residual activity
Hg2+
-
5 mM, 95% inhibition
Hg2+
-
1 mM, 12% residual activity
Hg2+
-
5 mM, 21.9% residual activity, 50%, 48 h, crude enzyme preparation
Hg2+
-
5 mM, 58% inhibition
Hg2+
-
1.0 mM, significant inhibition
Hg2+
1 mM, complete inhibition
Hg2+
-
1 mM, no residual activity
Hg2+
-
1 mM, complete loss of activity
Hg2+
-
Hg(acetate)2, restored by Cys or Cl-
Hg2+
-
1 mM, strong inhibition
Hg2+
10 mM, complete inhibition
Hg2+
-
1 mM HgCl2, complete inhibition
Hg2+
-
2 mM, 20% inhibition
Hg2+
-
endoglucanase E1 and E2; HgCl2
Hg2+
Thermochaetoides thermophila
-
-
Hg2+
Thermochaetoides thermophila
-
1 mM, 2% residual activity
Hg2+
-
5 mM, no residual activity
Hg2+
-
1 mM, represses the enzyme activity up to 22%
Hg2+
-
1 mM, complete inhibition
Hg2+
-
1 mM, complete inactivation
HgCl2
-
5 mM, 76% loss of activity
HgCl2
-
5 mM, 25% residual activity
iodoacetamide
-
-
Isopropanol
5%, 21.6% inhibition of activity with carboxymethyl cellulose, 53% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
K+
slight inhibition
K+
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 13% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
K+
10.2% inhibition at 5 mM
KCl
-
5 mM, 23% loss of activity
KCl
-
5 mM, 74% residual activity
Li+
slight inhibition
Li+
2 mM, 70% of initial activity
Li+
5 mM, 71% residual activity
mercaptoethanol
-
-
mercaptoethanol
-
1 mM, slight inhibition
methanol
5%, 26.5% inhibition of activity with carboxymethyl cellulose, 13.5% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
methanol
-
30% v/v, 62% loss of activity
Mg2+
10 mM, 86% residual activity
Mg2+
-
31% inhibition at 1 mM
Mg2+
5 mM, 44% residual activity
Mg2+
-
2 mM, slight inhibition
Mg2+
5 mM, 62% residual activity
Mg2+
5 mM, 2.3fold activation of activity with carboxymethyl cellulose, 6.5% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Mg2+
-
slight inhibition of endoglucanase E2 activity
Mg2+
Thermochaetoides thermophila
-
-
Mg2+
Thermochaetoides thermophila
-
10 mM, 12% residual activity
Mg2+
Thermochaetoides thermophila
5 mM, 51% loss of activity, substrate: xylan; 5 mM, 64.5% loss of activity, substrate: carboxymethyl cellulose; 6% inhibition at 1 mM, 64.5% inhibition at 5 mM
Mg2+
-
1 mM, 54% residual activity
Mg2+
8.1% inhibition at 5 mM
Mn2+
5 mM, 44% of initial activity
Mn2+
10 mM, 57% residual activity
Mn2+
-
54% inhibition at 0.1 mM, 71% inhibition at 1 mM
Mn2+
-
5 mM, 77% residual activity
Mn2+
-
5 mM, about 30% inhibition
Mn2+
-
5 mM, 82.5% residual activity, 50%, 48 h, crude enzyme preparation
Mn2+
1 mM, 59% residual activity
Mn2+
5 mM, 28% residual activity
Mn2+
MG570051
2 mM, less than 50% of initial activity
Mn2+
-
5 mM, 60% of initial activity
Mn2+
-
1 mM MnCl2, 18% inhibition
Mn2+
Thermochaetoides thermophila
-
-
Mn2+
Thermochaetoides thermophila
-
1 mM, 46% residual activity
Mn2+
-
1 mM, represses the enzyme activity up to 40%
Mn2+
59.3% inhibition at 5 mM
Mn2+
-
5 mM, 20% inhibition
N-bromosuccinimide
-
-
N-bromosuccinimide
-
5 mM, 56% loss of activity
N-bromosuccinimide
-
0.001 mM, complete inactivation
N-bromosuccinimide
-
1 mM, 35% residual activity
N-bromosuccinimide
1 mM, 99% inhibition
N-bromosuccinimide
-
1 mM, 90% inhibition
Na+
5 mM, 65% of initial activity
Na+
-
23% inhibition at 5 mM
Na+
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 6% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
NaCl
5 mM, 84% residual activity
NaCl
7.1% inhibition at 5 mM
NEM
-
70% inhibition of cellulase 4.5 at 10 mM, no effect on cellulase 4.8
NH4+
-
5 mM, 10% inhibition
NH4+
-
1 mM, 84% of initial activity
NH4+
Thermochaetoides thermophila
-
-
NH4+
Thermochaetoides thermophila
-
10 mM, 9% residual activity
Ni2+
slight inhibition
Ni2+
-
1 mM NiCl2, 68% inhibition
Ni2+
5 mM, 52% residual activity
Ni2+
-
1 mM, 27% residual activity
Ni2+
Thermochaetoides thermophila
activates 8% at 2 mM, inhibits 8% at 10 mM
Ni2+
-
5 mM, no residual activity
Ni2+
12.1% inhibition at 10 mM
NiCl2
-
5 mM, 40% loss of activity
NiCl2
-
5 mM, 48% residual activity
Pb2+
5 mM, 56% of initial activity
Pb2+
-
1 mM Pb(CH3COO)-, 36% inhibition
Pb2+
-
2 mM, slight inhibition
Pb2+
no remaining activity; no remaining activity
Pb2+
-
14.9% inhibition at 1 mM
Pb2+
-
65% inhibition at 10 mM
Pb2+
Thermochaetoides thermophila
-
Pb2+
-
5 mM, 9% residual activity
Pb2+
-
1 mM, 30% residual activity
PCMB
-
-
PCMB
Bacillus cellulyticus K-12
-
-
PCMB
-
0.4 M, 60% inhibition
PCMB
-
0.1 mM, 90% loss of activity of cellulase 4.5, 50% loss of activity of cellulase 4.8
phenylmethylsulfonyl fluoride
-
10 mM, 18.1% residual activity
phenylmethylsulfonyl fluoride
-
1 mM, 60% residual activity
PMSF
-
5 mM, 10.1% residual activity, 50%, 48 h, crude enzyme preparation
PMSF
1 mM, 89% inhibition
SDS
-
-
SDS
-
42% inhibition at 5%
SDS
Bacillus cellulyticus K-12
-
10 mM, 98% inhibition
SDS
0.4%, 10% of initial activity
SDS
-
0.25 mM, complete inactivation
SDS
-
10 mM, 49.2% residual activity
SDS
0.5%, 60% residual activity
SDS
-
1%, 12% of initial activity
SDS
10 mM, 35% remaining activity; 10 mM, 54% remaining activity
SDS
-
0.1%, 56% residual activity
SDS
complete inhibition at 0.1%
SDS
-
1% v/v, almost complete loss of activity
SDS
52.1% inhibition at 1%
Sn2+
-
2 mM
sodium dodecylsulfate
5 mM, 5% of initial activity
sodium dodecylsulfate
-
1%, 73% residual activity
sodium dodecylsulfate
-
1%, 32% residual activity
sodium dodecylsulfate
-
7% residual activity
sodium dodecylsulfate
1 mM, 76% residual activity
sodium hypochlorite
-
-
Triton X-100
-
19.7% inhibition at 5%
Triton X-100
10%, 20% of initial activity
Triton X-100
0.5%, 73% residual activity
Triton X-100
slight inhibition
Urea
-
denaturant
Urea
-
10 mM, 45% residual activity
Urea
9.7% inhibition at 5 mM
Urea
82.3% inhibition at 10%, 42.3% at 7%, and 24.3 at 5%
Zn2+
-
inhibition of cellulose hydrolysis, no inhibition of carboxymethylcellulose hydrolysis
Zn2+
10 mM, 95% residual activity
Zn2+
-
1 mM ZnSO4, 88% inhibition
Zn2+
5 mM, 19% residual activity
Zn2+
-
1 mM, 21% residual activity
Zn2+
2 mM, 65% of initial activity
Zn2+
5 mM, 51% residual activity
Zn2+
-
5 mM, 22% of initial activity
Zn2+
10 mM, almost 30% loss of activity
Zn2+
-
74% inhibition at 10 mM
Zn2+
Thermochaetoides thermophila
-
-
Zn2+
Thermochaetoides thermophila
-
1 mM, 19% residual activity
Zn2+
Thermochaetoides thermophila
5 mM, 4.4% loss of activity, substrate: carboxymethyl cellulose; 5 mM, 55% loss of activity, substrate: xylan
Zn2+
-
5 mM, no residual activity
Zn2+
-
1 mM, 64% residual activity
Zn2+
complete inhibition at 5 mM
Zn2+
about 60-80% inhibition at 5-10 mM
Zn2+
73% inhibition at 10 mM
Zn2+
-
1 mM, 78%inhibition
additional information
not inhibitory: EDTA, Ca2+
-
additional information
-
more than 50% of the original activity is retained after incubation with sodium alkyl sulfonate, sodium alkyl sulfate, polyoxyethylene alkyl sulfonate, alpha-olefin sulfonate
-
additional information
-
below 10% inhibition by propan-2-ol, ethanol, methanol, tert-amyl alcohol, acetone, chloroform, hexane, toluene, ethyl acetate, glycerol, Tween 80, and Tween 20 at 5%, and by Ca2+, Mg2+, Zn2+, (NH4)2SO4, urea, NaN2, and EDTA at 5 mM
-
additional information
-
no inhibition by N-bromosuccinimide and iodoacetamide
-
additional information
-
is minutely inhibited by anionic detergent and oxidizing agent comparable with inhibition by commercial enzyme
-
additional information
BglA7 is highly resistant to both pepsin and trypsin
-
additional information
-
enzyme retains 84.1 and 71.4% of the control activity in the presence of 0.5 and 2.0 mol/l NaCl, respectively
-
additional information
-
no inhibition by EDTA, EGTA, 1,10-phenanthroline, monoiodoacetate, NEM, DTNB, PCMB and diethylpyrocarbonate
-
additional information
-
glucose (2 mM), cellobiose (1.25 mM), methylcellulose (0.5%, w/v) and gluconolactone (100 mM) do not inhibit the hydrolysis of carboxymethylcellulose by any of the endocellulases
-
additional information
-
no effect by DTT and EDTA at 10 mM
-
additional information
-
the enzyme displays optimal activity even in the existence of divalent and trivalent metallic cations: Ca2+, Mg2+, Pb2+, Cd2+, Cu2+, Ni2+ and Fe3+
-
additional information
-
no inhibition by cellobiose
-
additional information
-
gallic acid, cinnamic acid, ferulic acid, 4-coumaric acid, sinapic acid, vanilin, syringaldehyde, and 4-hydroxybenzoic acid are poor inhibitors
-
additional information
-
2,3-di-O-methylated regions in 2,3-di-O-methylated cellulose, having a trace amount of unsubstituted glucose units competitively inhibit the hydrolysis of glucose in other molecular chains
-
additional information
no or poor effect by 5 mM of SDS, DTT, and EDTA
-
additional information
organic solvents at 10-20%
-
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0.018
-
TfCel9A wild-type, activity on 600 microM G5
0.03
substrate carboxymethylcellulose, pH 5.0, 50°C
0.037
-
TfCel9A W256A mutant, activity on 600 microM G5
0.04
-
substrate: carboxymethylcellulose, pH 5.0, 50°C
0.048
-
partially purified enzyme, pH 4.5, 55°C
0.049
Sporotrichum pulverulentum
-
partially purified enzyme, pH 4.5, 55°C
0.075
-
substrate: carboxymethylcellulose, pH 5.0, 50°C
0.1
-
substrate: carboxymethylcellulose, pH 5.0, 70°C
0.13
-
substrate: carboxymethylcellulose, pH 5.0, 70°C
0.16
substrate phosphoric acid swollen cellulose, pH 6.0, 60°C
0.166
-
after DEAE anion exchange chromatography
0.175
-
substrate: carboxymethylcellulose, pH 5.0, 50°C
0.25
wild-type, pH 7.0, 60°C
0.39
mutant S365P, pH 7.0, 40°C
0.44
mutant K94R, pH 7.0, 60°C
0.54
substrate filter paper , pH 6.0, 60°C
0.56
-
cells in bioreactor
0.673
-
foregut proventriculus
0.68
Thermochaetoides thermophila
substrate carboxymethylcellulose, mutant Y30F/Y173F, pH 4.0, 60°C
0.7
-
wild-type, pH 4.8, 50°C
0.89
-
substrate filter paper, pH 5.5, 60°C
1.02
substrate beta-glucan, pH 6.0, 60°C
1.2
substrate: N-[2-N-[(S-(4-deoxy-4-dimethylaminophenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate, pH 1.8, 80°C
1.3
-
purified enzyme MtGH45, substrate phosphoric acid swollen cellulose, pH 6.5, 50°C
1.35
Thermochaetoides thermophila
substrate carboxymethylcellulose, mutant Y30F, pH 4.0, 60°C
1.52
Thermochaetoides thermophila
substrate carboxymethylcellulose, pH 4.0, 70°C
1.67
Thermochaetoides thermophila
substrate beta-D-glucan, mutant Y173F, pH 4.0, 60°C
1.87
Thermochaetoides thermophila
substrate carboxymethylcellulose, mutant Y173F, pH 4.0, 60°C
1.91
-
Cel5A, carboxymethyl cellulose as substrate
10
-
37°C, pH 5.0, release of D-glucose from carboxymethyl cellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
10.9
purified recombinant enzyme, pH 5.0, 60°C, substrate Avicel PH-101
101
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
103
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
105.8
-
presence of 0.5% Tween-20, pH 6.0, 65°C
108
substrate hydroxyethyl cellulose, pH 5.5, 92°C
109
-
purified recombinant mutant K429A
11.02
-
carboxymethyl cellulase, pH 4.8, 45°C, culture from cutter-milled rice straw as carbon source
11.61
-
after DEAE anion exchange chromatography
117
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week, Exophiala sp. aff. salmonis, GenBank Accession: HQ630990
12.8
-
purified enzyme MtGH45, substrate cotton, pH 6.5, 50°C
120
-
pH 5.5, 80°C, substrate carboxymethyl cellulose
123
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
125
-
37°C, pH 5.0, release of D-glucose from carboxymethyl cellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
127.2
-
presence of 96% glycerol, pH 4.8, 4°C
13.9
substrate barley beta-glucan, pH 3.5, 40°C
130
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks, Phoma sp. aff. glomerata, GenBank Accession: HQ630999
134
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
134.22
purified recombinant enzyme, pH 5.0, 60°C, substrate lichenin
137
-
purified recombinant mutant G91A
138
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
1443
substrate beta-glucan, pH 5.0, 50°C
15
-
37°C, pH 5.0, release of D-glucose from carboxymethyl cellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks, Phoma sp. aff. glomerata, GenBank Accession: HQ630999
150
-
activity with carboxymethylcellulose
154
-
purified recombinant mutant Y97W
156
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
16
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
16.5
-
catalytic domain of endoglucanase G
16.76
-
carboxymethyl cellulase, pH 4.8, 45°C, culture from Solka Floc as carbon source
162
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
17.3
-
avicelase activity, pH 5.5, 50°C
170.7
-
purified enzyme GtGH45, substrate beta-glucan, pH 6.5, 50°C
174
substrate carboxymethyl cellulose, pH 5.0, 50°C
18.63
-
carboxymethyl cellulase, pH 4.8, 45°C, culture from dry ball-milled rice straw as carbon source
186
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
19.73
-
carboxymethyl cellulase, pH 4.8, 45°C, culture from freeze-dried rice straw after wet disk milling at 7 days as carbon source
192
-
substrate medium viscosity carboxymethyl cellulose, pH 5.5, 60°C
193
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
1970
substrate carboxymethyl cellulose, pH 5.5, 30°C
2.14
Thermochaetoides thermophila
substrate beta-1,4-D-glucan, pH 4.0, 70°C
2.22
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, pH 5.0, 55°C, substrate beta-glucan
2.8
debranched arabinan, relative activity 51%
2.9
arabinan, relative activity 53%
20
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
20.5
substrate lichenan, pH 3.5, 40°C
200.6
-
purified enzyme GtGH45, substrate carboxymethyl cellulose, pH 6.5, 50°C
202
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
202.6
-
purified enzyme MtGH45, substrate carboxymethyl cellulose, pH 6.5, 50°C
2020
substrate barley beta-glucan, pH 5.0, 60°C
208
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
209.9
purified recombinant His-tagged enzyme, pH 6.0, 115°C, substrate lichenan
21.8
substrate konjac mannan, pH 6.5, 50°C
210.7
purified recombinant His-tagged enzyme, pH 6.0, 115°C, substrate barley beta-glucan
218.9
-
substrate cellobiose, crude enzyme preparation, pH 8.0, 60°C
220
Rucel5B, pH 6.5, 60°C, substrate carboxymethyl cellulose
229
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
23
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
234
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
234.6
-
substrate cotton straw, crude enzyme preparation, pH 8.0, 60°C
24.1
-
isoform endoglucanase 2, pH 5.0, 50°C
246
-
substrate low viscosity carboxymethyl cellulose, pH 5.5, 60°C
248.7
recombinant CSCMCase
25
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
2500
-
pH not specified in the publication, temperature not specified in the publication
251
-
37°C, pH 5.0, release of D-glucose from carboxymethyl cellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
2549
-
purified native enzyme
256
substrate barley beta-glucan, pH 6.5, 50°C
257.8
-
substrate wheat straw, crude enzyme preparation, pH 8.0, 60°C
26
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
264.7
presence of 96% glycerol, pH 4.8, 4°C
269
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
27
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
27.3
substrate 4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside, pH 6.0, 40°C
272
substrate lichenan, pH 5.5, 92°C
28.1
cellulase activity is estimated by the AZO-carboxymethylcellulose standard assay, last purification step
280
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
29
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
297.15
purified recombinant His-tagged enzyme, pH 5.0, 55°C, substrate carboxymethyl cellulose
3.88
-
M44-11 mutant, carboxymethyl cellulose as substrate
315
-
recombinant enzyme from cytoplasmic supernatant of Escherichia coli
315.2
-
substrate 4-nitrophenyl beta-D-glucopyranoside, crude enzyme preparation, pH 8.0, 60°C
317
substrate barley beta-glucan, pH 5.5, 92°C
32.4
-
purified native enzyme
34.4
wild-type, pH 7.0, 50°C
3413
substrate lichenan, pH 4.5, 90°C
349
-
purified recombinant mutant G91A/Y97W
35.6
-
purified enzyme MtGH45, substrate lichenan, pH 6.5, 50°C
35.8
substrate carboxymethylcellulose, pH 3.5, 40°C
354.1
-
substrate rice straw, crude enzyme preparation, pH 8.0, 60°C
357
-
purified recombinant mutant Y97W/K429A
372
substrate barley beta-glucan, pH 6.5, 70°C
38.5
purified recombinant His-tagged enzyme, pH 6.0, 115°C, substrate carboxymethyl cellulose
38.7
Thermochaetoides thermophila
-
pH 5.0, 60°C
384
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
39.2
-
carboxymethylcellulase activity, pH 5.5, 50°C
4
birchwood xylan, relative activity 73%
4.2
oat spelt xylan, relative activity 76%
4.6
beechwood xylan, relative activity 84%
4.84
-
S75 mutant, carboxymethyl cellulose as substrate
4.88
-
S78 mutant, carboxymethyl cellulose as substrate
4.93
carboxymethyl cellulose sodium salt
40
-
enzyme mutant F194A, pH 5.5, 50°C
4040
substrate Hordeum vulgare beta-glucan
4059
substrate laminarin, pH 4.5, 90°C
42.3
-
substrate carboxymethyl cellulose, pH 5.5, 40°C
4240
-
purified type I CMCase, pH 4.8, 40°C
4254
substrate barley beta-glucan, pH 4.5, 90°C
429.7
-
substrate corn stover, crude enzyme preparation, pH 8.0, 60°C
43.02
-
purified native enzyme, pH 6.5, 60°C
469
-
purified recombinant mutant G91A/Y97W/K429A
47
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
47.6
substrate 4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside, pH 4.5, 40°C
5.13
-
after DEAE anion exchange chromatography
5.5
carboxymethylcellulose, relative activity 100%
5.55
-
mutant E289V, pH 4.8, 55°C
51
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
510.8
-
substrate carboxymethyl cellulose, crude enzyme preparation, pH 8.0, 60°C
52
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
52.2
substrate 4''',6'''-O-benzylidene 2-chloro-4-nitrophenyl-beta-cellotrioside, pH 6.0, 40°C
52.5
-
purified enzyme MtGH45, substrate beta-glucan, pH 6.5, 50°C
54.2
-
purified enzyme GtGH45, substrate lichenan, pH 6.5, 50°C
57.92
-
purified native enzyme, pH 5.0, 50°C
59.1
-
carboxymethyl cellulase supernatant, xylose as a substrate
6.4
pH 7.0, 40°C, presence of 2 M NaCl
60
-
wild-type, substrate barley beta-glucan, pH 5.0, 40°C
61
purified recombinant mutant S127C/A165C, substrate beta-glucan, pH and temperature not specified in the publication
624
substrate carboxymethyl cellulose, pH 4.5, 90°C
64.17
-
purified native enzyme
64.8
-
catalytic domain expressed in Escherichia coli
65.53
purified recombinant enzyme, pH 5.0, 60°C, substrate carboxymethyl cellulose
66
purified recombinant mutant Y171C/L201C, substrate carboxymethyl cellulose, pH and temperature not specified in the publication
66.1
-
endo-beta-1,4-glucanase E1
66.4
-
endo-beta-1,4-glucanase E2 and E3
67
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
692
substrate carboxymethyl cellulose, pH 5.5, 92°C
7.43
-
after gel filtration chromatography
74
-
37°C, pH 5.0, release of D-glucose from carboxymethyl cellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
76
substrate carboxymethyl cellulose, pH 5.0, 50°C
77
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
78
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
8.13
purified recombinant enzyme, pH 5.0, 60°C, substrate laminarin
8.5
-
purified enzyme GtGH45, substrate cotton, pH 6.5, 50°C
81
-
mutant N194A, substrate barley beta-glucan, pH 5.0, 40°C
82
substrate carboxymethyl cellulose, pH 6.0, 40°C
83
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
84
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
846.8
-
purified type II CMCase, pH 4.8, 40°C
87
purified recombinant His-tagged enzyme, substrate phosphoric acid swollen cellulose, pH 5.0, 50°C
9
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
9.06
-
isoform endoglucanase 1, pH 5.0, 50°C
92.29
purified recombinant enzyme, pH 5.0, 60°C, substrate barley beta-glucan
92.5
-
gel filtration chromatography, last purification step
94
substrate lichenan, pH 5.0, 50°C
96
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
97.95
-
purified native enzyme, pH 5.0, 70°C
0.05
-
partially purified enzyme, pH 4.5, 55°C
0.05
-
substrate: carboxymethylcellulose, pH 5.0, 50°C
0.14
substrate barley beta-glucan, pH 5.0, 50°C
0.14
-
substrate: carboxymethylcellulose, pH 5.0, 70°C
0.19
substrate lichenan, pH 5.0, 50°C
0.19
-
substrate: carboxymethylcellulose, pH 5.0, 70°C
0.21
substrate carboxymethyl cellulose, pH 6.0, 60°C
0.21
-
substrate: carboxymethylcellulose, pH 5.0, 70°C
0.33
mutant S365P, pH 7.0, 60°C
0.33
wild-type, pH 7.0, 40°C
0.45
mutant K94R, pH 7.0, 40°C
0.45
Thermochaetoides thermophila
substrate beta-D-glucan, mutant Y30F/Y173F, pH 4.0, 60°C
0.8
substrate: N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate, pH 3, 80°C, chimeric fusion protein CelA-SSO1949-CelA, that consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA
0.8
substrate: N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate, pH and temperature not specified in the publication, hybrid protein (CelA-SSO1949-CelA, consisting of 262 amino acids) based on beta-endoglucanase from Sulfolobus solfataricus P2 and beta-endoglucanase from Thermotoga maritima
0.8
substrate N-[2-N-[(S-(4-deoxy-4-dimethylamino-phenylazophenylthioureido-beta-D-glucopyranosyl)-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl)-2-thioacetyl]aminoethyl]-1-naphthylamine-5-sulfonate, pH 3, 80°C, chimeric fusion protein CelA-SSO1949-CelA, that consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA
1
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
1
Thermochaetoides thermophila
substrate beta-D-glucan, wild-type, pH 4.0, 60°C
1.05
CM cellulose
1.05
substrate lichenan, pH 6.0, 60°C
1.21
Thermochaetoides thermophila
substrate beta-D-glucan, mutant Y30F, pH 4.0, 60°C
1.21
Thermochaetoides thermophila
substrate carboxymethylcellulose, wild-type, pH 4.0, 60°C
11
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
11
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
115
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
115
substrate xyloglucan, pH 6.5, 50°C
12.3
-
carboxymethyl cellulase supernatant, glucose as a substrate
12.3
substrate birchwood xylan, pH 4.5, 90°C
12.74
-
last purification step
12.74
-
after gel filtration chromatography
13
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
13
-
37°C, pH 5.0, release of D-glucose from carboxymethyl cellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
14
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
14
-
37°C, pH 5.0, release of D-glucose from carboxymethyl cellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
1444
substrate barley beta-glucan, pH 5.0, 50°C
1444
substrate beta-glucan, pH 5.0, 50°C
159
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
159
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks, Exophiala sp. aff. salmonis, GenBank Accession: HQ630990
159
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
17
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
17
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
176
substrate carob bean gum, pH 4.5, 90°C
176
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
18
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
18
-
37°C, pH 5.0, release of D-glucose from carboxymethyl cellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
18
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
19
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
19
-
recombinant protein, pH 7, 60°C
19.09
-
last purification step
19.09
-
after gel filtration chromatography
2
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
2
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
21
-
37°C, pH 5.0, release of D-glucose from carboxymethyl cellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
21
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
22
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
22
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
22
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
24
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
24
purified recombinant His-tagged enzyme, substrate lichenan, pH 5.0, 50°C
24
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
24
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
24
purified recombinant His-tagged enzyme, substrate barley beta-glucan, pH 6.0, 30°C
248
-
substrate barley beta-glucan, pH 5.5, 60°C
248
-
purified recombinant mutant G91A/K429A
3
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
3
-
purified enzyme MtGH45, substrate Avicel, pH 6.5, 50°C
3.3
substrate carboxymethylcellulose, pH 6.5, 50°C
3.3
-
purified enzyme GtGH45, substrate phosphoric acid swollen cellulose, pH 6.5, 50°C
3.3
Thermochaetoides thermophila
-
pH 5.0, 50°C
31
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
31
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week, Phoma sp. aff. glomerata, GenBank Accession: HQ630999
32
purified recombinant His-tagged enzyme, substrate beta-glucan, pH 5.0, 50°C
32
-
37°C, pH 5.0, release of D-glucose from carboxymethyl cellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
33
presence of 2.5 M NaCl, pH 5.0, 55°C
33
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
34
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
34
substrate phosphoric acid-swollen cellulose, pH 5.5, 92°C
35
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
35
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
39
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
39
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
42
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks, Exophiala sp. aff. spinifera, GenBank Accession: HQ631027
42
-
mutant N19A, substrate carboxymethylcellulose, pH 5.0, 40°C
428
-
recombinant enzyme from granules produced by Escherichia coli
428
purified recombinant His-tagged enzyme, pH 4.0, 95°C, substrate carboxymethyl cellulose
44
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
44
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
450
-
after ion-exchange chromatography
46
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks
46
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks, Phoma sp. aff. glomerata, GenBank Accession: HQ630999
48
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
48
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
53
-
mutant N19A, substrate barley beta-glucan, pH 5.0, 40°C
53
purified recombinant wild-type enzyme, substrate beta-glucan, pH and temperature not specified in the publication
53
substrate carboxymethyl cellulose, pH 6.0, 40°C
57
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
57
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
57
-
wild-type, substrate carboxymethylcellulose, pH 5.0, 40°C
57
purified recombinant wild-type enzyme, substrate carboxymethyl cellulose, pH and temperature not specified in the publication
58
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
58
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks, Exophiala sp. aff. salmonis, GenBank Accession: HQ630990
622
substrate glucomannan, pH 5.0, 50°C
622
substrate glucomannan, pH 5.0, 50°C
64
purified recombinant His-tagged enzyme, substrate glucomannan, pH 5.0, 50°C
64
-
mutant N42A, substrate carboxymethylcellulose, pH 5.0, 40°C
64
purified recombinant mutant Y171C/L201C, substrate beta-glucan, pH and temperature not specified in the publication
65
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 4 weeks
65
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 2 weeks, Phoma sp. aff. glomerata, GenBank Accession: HQ630999
68
-
mutant N42A, substrate barley beta-glucan, pH 5.0, 40°C
68
purified recombinant mutant S127C/A165C, substrate carboxymethyl cellulose, pH and temperature not specified in the publication
68
substrate carboxymethyl cellulose, pH 4.5, 40°C
694
substrate carboxymethyl cellulose, pH 5.0, 50°C
694
substrate carboxymethyl cellulose, pH 5.0, 50°C
75
substrate beta-glucan, pH 5.0, 50°C
75
-
mutant N194A, substrate carboxymethylcellulose, pH 5.0, 40°C
79
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 1 week
79
purified recombinant His-tagged enzyme, substrate carboxymethyl cellulose, pH 5.0, 50°C
8.8
pH 5.5, 37°C
8.8
-
purified enzyme GtGH45, substrate Avicel, pH 6.5, 50°C
80
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks, Exophiala sp. aff. salmonis, GenBank Accession: HQ630990
80
-
37°C, pH 5.0, release of D-glucose from carboxymethylcellulose, activity in crude-cell-free fungal extract collected from fungal cultures on Miscanthus cell walls after 8 weeks
additional information
-
-
additional information
-
-
additional information
-
purified native enzyme, 1289.83 U/ml, pH 5.0, 50°C
additional information
-
-
additional information
2.82 U/ml for the native extracellular enzyme, 6.78-8.54 U/ml for the recombinant extracellular enzyme expressed in Escherichia coli strain BL21(DE3)
additional information
-
2.82 U/ml for the native extracellular enzyme, 6.78-8.54 U/ml for the recombinant extracellular enzyme expressed in Escherichia coli strain BL21(DE3)
additional information
-
-
additional information
recombinant crude enzyme, 5.772 U/ml
additional information
-
recombinant crude enzyme, 5.772 U/ml
additional information
-
-
additional information
Lenzites trabea
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
pH 5.0, specific activity of the enzyme recombinantly expressed in Sulfolobus solfataricus is about 200fold higher compared to the specific activity of the enzyme recombinantly expressed in Escherichia coli
additional information
-
pH 5.0, specific activity of the enzyme recombinantly expressed in Sulfolobus solfataricus is about 200fold higher compared to the specific activity of the enzyme recombinantly expressed in Escherichia coli
additional information
Sporotrichum pulverulentum
-
discontinuous test based on the specific determination of the cellobiose produced during the cellulase reaction with an ancillary cellobiose dehydrogenase
additional information
substrate carboxymethyl cellulose, recombinant wild-type enzyme shows 70.4 mU/ml activity, activities of enzyme mutants G263C/R307H, G145D/N207K, P228R, T67N/D142E/S218N/V242D/D330E, and T157I/G251D/V259D are 103.8, 88.6, 112.6, 89.1, and 102.9 mU/ml, respectively
additional information
-
discontinuous test based on the specific determination of the cellobiose produced during the cellulase reaction with an ancillary cellobiose dehydrogenase
additional information
-
-
additional information
-
-
additional information
-
discontinuous test based on the specific determination of the cellobiose produced during the cellulase reaction with an ancillary cellobiose dehydrogenase
additional information
-
assay methods
additional information
-
-
additional information
-
assay methods
additional information
-
staining techniques for the detection
additional information
-
assay methods
additional information
-
discontinuous test based on the specific determination of the cellobiose produced during the cellulase reaction with an ancillary cellobiose dehydrogenase
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?
-
x * 76000, SDS-PAGE
?
-
x * 56000, enzyme form EGA, SDS-PAGE
?
-
x * 40000, enzyme form EGB, SDS-PAGE
?
-
x * 66000, enzyme form EGB, SDS-PAGE
?
-
x * 65000, enzyme form EGD, SDS-PAGE
?
-
x * 64000, recombinant truncated mutant, SDS-PAGE
?
x * 51400 and x * 57100, without and with signal peptide, respectively, SDS-PAGE
?
Actinomyces sp. 40 Korean Native Goat 40
-
x * 51400 and x * 57100, without and with signal peptide, respectively, SDS-PAGE
-
?
x * 59000, wild.type, x * 49500, mutant lacking the IgG-like domain, SDS-PAGE and calculated
?
-
x * 39000, SDS-PAGE
-
?
-
x * 27000, endo-beta-1,4-glucanase EG27, SDS-PAGE
?
-
x * 45000, endo-beta-1,4-glucanase EG45, SDS-PAGE
?
x * 27000, SDS-PAGE of recombinant protein
?
-
x * 38831, calculation from nucleotide sequence
?
x * 55000, about, recombinant enzyme, SDS-PAGE, x * 52800, about, sequence calculation
?
-
x * 55000, about, recombinant enzyme, SDS-PAGE, x * 52800, about, sequence calculation
-
?
-
x * 55000, SDS-PAGE
-
?
-
x * 65000, SDS-PAGE
-
?
-
x * 55118, calculated from sequence
?
-
x * 54000, SDS-PAGE
-
?
-
x * 55118, calculated from sequence
-
?
-
x * 62000, SDS-PAGE
-
?
-
x * 40000, SDS-PAGE
-
?
-
x * 62000, SDS-PAGE
-
?
-
x * 40000, SDS-PAGE
-
?
-
x * 80000, SDS-PAGE
-
?
-
x * 37000, about, SDS-PAGE
?
x * 27000, recombinant CelL73, SDS-PAGE
?
x * 52000, recombinant extracellular enzyme, SDS-PAGE
?
x * 54000, recombinant CelL15, SDS-PAGE
?
-
x * 30000, SDS-PAGE
-
?
-
x * 52000, recombinant extracellular enzyme, SDS-PAGE
-
?
-
x * 56000, SDS-PAGE
-
?
-
x * 27000, recombinant CelL73, SDS-PAGE
-
?
-
x * 54000, recombinant CelL15, SDS-PAGE
-
?
-
x * 80000, SDS-PAGE
-
?
-
x * 28000, calculated, x * 28000, and x * 33000, SDS-PAGE of unglycosylated and glycosylated protein, respectively
?
Bellamya chinensis laeta UM-2014
-
x * 70000, SDS-PAGE
-
?
x * 48000, deglycosylated Bgl7A, SDS-PAGE, x * 60000-80000, recombinant glycosylated enzyme, SDS-PAGE
?
x * 130000, mutant enzyme DELTA1-90, SDS-PAGE
?
x * 45450, about, sequence calculation
?
x * 48250, about, sequence calculation
?
-
x * 48250, about, sequence calculation
-
?
-
x * 45450, about, sequence calculation
-
?
-
x * 48250, about, sequence calculation
-
?
-
x * 45450, about, sequence calculation
-
?
-
x * 48250, about, sequence calculation
-
?
-
x * 45450, about, sequence calculation
-
?
-
x * 48250, about, sequence calculation
-
?
-
x * 45450, about, sequence calculation
-
?
-
x * 48250, about, sequence calculation
-
?
-
x * 45450, about, sequence calculation
-
?
-
x * 48250, about, sequence calculation
-
?
-
x * 45450, about, sequence calculation
-
?
x * 96798, calculated from sequence
?
-
x * 96798, calculated from sequence
-
?
-
x * 25000, endoglucanase EG25, SDS-PAGE
?
-
x * 28000, endoglucanase EG28, SDS-PAGE
?
-
x * 44000, endoglucanase EG44, SDS-PAGE
?
-
x * 47000, endoglucanase EG47, SDS-PAGE
?
-
x * 51000, endoglucanase EG51, SDS-PAGE
?
-
x * 60000, endoglucanase EG60, SDS-PAGE
?
x * 42000, SDS-PAGE, x * 39100, calculated
?
-
x * 65100, calculated
-
?
-
x * 38800, calculated
-
?
-
x * 35000, endoglucanase Y, SDS-PAGE
?
-
x * 50000, enzymatically active domain, SDS-PAGE
?
-
x * 58000, SDS-PAGE
-
?
-
x * 50000, enzymatically active domain, SDS-PAGE
-
?
-
x * 35000, endoglucanase 35, SDS-PAGE
?
-
x * 47000, endoglucanase 47, SDS-PAGE
?
x * 30000, about, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 30000, about, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 41000, SDS-PAGE
-
?
x * 41241, calculated from sequuence
?
-
x * 41000, SDS-PAGE
-
?
-
x * 41241, calculated from sequuence
-
?
-
x * 68000, SDS-PAGE
-
?
-
x * 50000, SDS-PAGE
-
?
-
x * 20000, SDS-PAGE
-
?
-
x * 37300, endoglucanase III, SDS-PAGE
?
-
x * 46500, endoglucanase I, SDS-PAGE
?
-
x * 30000, endoglucanase IV, SDS-PAGE
?
-
x * 21000, endoglucanase II, SDS-PAGE
?
-
x * 31200, SDS-PAGE
-
?
x * 52200, calculated, x * 60000, SDS-PAGE of recombinant protein
?
-
x * 56463, calculation from nucleotide sequence
?
x * 60000, SDS-PAGE and calculated
?
MG570051
x * 103500, calculated, x * 93000, SDS-PAGE, truncated form produced by the proteolytic cleavage of the C-terminus
?
x * 43000, SDS-PAGE and calculated
?
x * 43000, SDS-PAGE and calculated
?
x * 53000, SDS-PAGE of recombinant protein
?
-
x * 53000, SDS-PAGE of recombinant protein
-
?
-
x * 70000, 1,4-beta-glucanase II, SDS-PAGE
?
-
x * 15000, 1,4-beta-glucanase I, SDS-PAGE
?
-
x * 52700, calculated from sequence
?
-
x * 52200, recombinant His-tagged enzyme, SDS-PAGE
?
x * 35900, calculated from sequence
?
x * 35988, calculated from sequence
?
x * 45561, wild-type enzyme (389 amino acids) expressed with both N(28 residues)- and C(42 residues)-terminal truncations (full length EGPh contains 458 amino acids) with a signal peptide sequence of 28 residues and a C-terminal region involved in anchoring
?
-
x * 45561, wild-type enzyme (389 amino acids) expressed with both N(28 residues)- and C(42 residues)-terminal truncations (full length EGPh contains 458 amino acids) with a signal peptide sequence of 28 residues and a C-terminal region involved in anchoring
-
?
-
x * 43000, SDS-PAGE
-
?
x * 36800, calculated, x * 37000, SDS-PAGE of deglycosylated enzyme
?
x * 46842, calculated, x * 66000, SDS-PAGE, x * 51475, MALDI-TOF of recombinant protein, x * 47206, MALDI-TOF of recombinant deglycosylated protein
?
-
x * 36800, calculated, x * 37000, SDS-PAGE of deglycosylated enzyme
-
?
-
x * 42000, endo-beta-1,4-glucanase component YEG1, SDS-PAGE
?
-
x * 41000, endo-beta-1,4-glucanase component YEG2, SDS-PAGE
?
-
x * 56000, SDS-PAGE
-
?
-
x * 54618, the enzyme contains a catalytic domain belonging to family 9 and a dockering domain, it is a component of the cellulosome, calculation from nucleotide sequence
?
x * 93800, calculation from nucleotide sequence
?
x * 94000, recombinant enzyme, SDS-PAGE
?
-
x * 42000, recombinant enzyme, SDS-PAGE
?
x * 42000, truncated enzyme form expressed in Escherichia coli
?
x * 67103, calculation from nucleotide sequence
?
-
x * 42000, truncated enzyme form expressed in Escherichia coli
-
?
-
x * 67103, calculation from nucleotide sequence
-
?
x * 35128, sequence calculation
?
-
x * 35128, sequence calculation
-
?
-
x * 35128, sequence calculation
-
?
x * 37300, calculated from sequence
?
x * 35154, enzyme recombinantly expressed in Escherichia coli, calculated from sequence
?
x * 35500, enzyme recombinantly expressed in Escherichia coli, SDS-PAGE
?
x * 29000, chimeric fusion protein CelA-SSO1949-CelA consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA, SDS-PAGE
?
x * 37508, calculated from sequence
?
x * 37000, SDS-PAGE, x * 37508, calculated
?
-
x * 37000, SDS-PAGE, x * 37508, calculated
-
?
-
x * 57000, SDS-PAGE
-
?
-
x * 37300, calculated from sequence
-
?
-
x * 37000, SDS-PAGE
-
?
-
x * 37508, calculated from sequence
-
?
-
x * 29000, chimeric fusion protein CelA-SSO1949-CelA consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA, SDS-PAGE
-
?
-
x * 38000, SDS-PAGE
-
?
x * 33297, sequence calculation, x * 34000, SDS-PAGE
?
-
x * 34000, native enzyme, x * 47000, recombinant enzyme expressed in Pichia pastoris
?
-
x * 33297, sequence calculation, x * 34000, SDS-PAGE
-
?
-
x * 27000, SDS-PAGE, recombinant protein
?
x * 35000, about, sequence calculation
?
-
x * 40000, CMCase 1, SDS-PAGE
?
-
x * 48000, CMCase 2, SDS-PAGE
?
-
x * 29000, catalytic domain, SDS-PAGE
?
-
x * 29000, catalytic domain, SDS-PAGE
-
?
-
x * 27000, tpe I CMCase, SDS-PAGE, x * 24000, type II CMCase, SDS-PAGE
?
-
x * 26000, SDS-PAGE
-
?
-
x * 55000, SDS-PAGE
-
?
-
x * 35000, SDS-PAGE
-
?
-
1 * 94000, endoglucanase E1, SDS-PAGE
?
Thermochaetoides thermophila
-
x * 53000, SDS-PAGE
?
Thermochaetoides thermophila
-
x * 60000, isoform cellobiohydrolase I, and x * 40000, cellobiohydrolase II, SDS-PAGE
?
Thermochaetoides thermophila
x * 32000, SDS-PAGE, x * 24500, calculated
?
Thermochaetoides thermophila
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
?
Thermochaetoides thermophila CBS 144.50
-
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
-
?
Thermochaetoides thermophila DSM 1495
-
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
-
?
Thermochaetoides thermophila IMI 039719
-
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
-
?
x * 29000, chimeric fusion protein CelA-SSO1949-CelA consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA, SDS-PAGE
?
x* 40600, calculated from sequence
?
x * 46000, including 4 kDa signal peptide, calculated
?
-
x * 46000, including 4 kDa signal peptide, calculated
-
?
x * 44230, plus a signal peptide of 21 amino acids, calculated
?
-
x * 78100, SDS-PAGE
-
?
-
x * 48000, endoglucanase 2, SDS-PAGE
?
-
x * 52000, endoglucanase I, SDS-PAGE
?
-
x * 48000, endoglucanase 2, SDS-PAGE
-
?
-
x * 52000, endoglucanase I, SDS-PAGE
-
?
-
x * 50000, endoglucanase IV, SDS-PAGE
?
-
x * 45000, endoglucanase II, SDS-PAGE
?
-
x * 52000, endoglucanase VI, SDS-PAGE
?
-
x * 57000, endoglucanase V, SDS-PAGE
?
-
x * 585000, endoglucanase III, SDS-PAGE
?
-
x * 50000, endoglucanase I, SDS-PAGE
?
-
x * 23500, endoglucanase IV, SDS-PAGE
?
-
x * 50000, endoglucanase IV, SDS-PAGE
-
?
-
x * 45000, endoglucanase II, SDS-PAGE
-
?
-
x * 52000, endoglucanase VI, SDS-PAGE
-
?
-
x * 57000, endoglucanase V, SDS-PAGE
-
?
-
x * 585000, endoglucanase III, SDS-PAGE
-
?
x * 55400, about, sequence calculation
?
x * 62300, calculated, x * 60000, SDS-PAGE
?
x * 22500, about, sequence calculation, x * 37000, recombinant enzyme, SDS-PAGE
?
x * 46500, about, sequence calculation
?
x * 62600, about, recombinant enzyme, sequence calculation
?
-
x * 31000, SDS-PAGE
-
?
x * 55000, calculated including His-tag
?
x * 40000, recombinant His-tagged Rucel5B, SDS-PAGE, x * 38400, about, Rucel5B, sequence calculation
?
-
x * 42100, calculated from sequence
?
x * 49500, calculated, x * 50900, SAXS data
?
-
x * 49500, calculated, x * 50900, SAXS data
-
?
x * 127047, the enzyme consists of an N-terminal signal peptide, two glycosyl hydrolase family 5 catalytic modules, two novel carbohydrate-binding modules, two linker sequences, and a C-terminal sequence with an unknown function, MW calculated from sequence
?
-
x * 45000, isoform endoglucanase 1, x * 46500, isoform endoglucanse 2, SDS-PAGE
?
-
x * 45000, isoform endoglucanase 1, x * 46500, isoform endoglucanse 2, SDS-PAGE
-
dimer
-
1 * 22000 + 1 * 32000, SDS-PAGE
dimer
-
2 * 35500, endo-beta-1,4-glucanase E1, E2 and E3, SDS-PAGE
dimer
-
2 * 35500, endo-beta-1,4-glucanase E1, E2 and E3, SDS-PAGE
-
dimer
Bx-ENG-2 exists in a glycosylated dimeric form
dimer
Bx-ENG-3 exists in a glycosylated dimeric form
monomer
-
1 * 65000, SDS-PAGE
monomer
-
1 * 40000, SDS-PAGE
monomer
-
1 * 26000, SDS-PAGE
monomer
-
1 * 40000, SDS-PAGE
-
monomer
-
1 * 41000, SDS-PAGE
monomer
-
1 * 41000, SDS-PAGE
-
monomer
Bacillus cellulyticus K-12
-
1 * 64000, SDS-PAGE
monomer
Bx-ENG-1 exists in an unglycosylated monomeric form
monomer
1 * 40000, SDS-PAGE, 1 * 40457, calculated
monomer
-
1 * 40000, SDS-PAGE, 1 * 40457, calculated
-
monomer
-
1 * 48000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
monomer
-
1 * 36000, SDS-PAGE
monomer
-
1 * 36000, SDS-PAGE
-
monomer
-
1 * 27000, SDS-PAGE
monomer
-
1 * 27000, SDS-PAGE
-
monomer
-
1 * 45600, SDS-PAGE
monomer
-
1 * 66000, SDS-PAGE, 1 * 42000, SDS-PAGE of deglycosylated protein
monomer
-
1 * 82000, SDS-PAGE
monomer
-
1 * 82000, SDS-PAGE
-
monomer
-
1 * 47000, SDS-PAGE
monomer
-
1 * 35000, SDS-PAGE
monomer
-
1 * 59000, SDS-PAGE
monomer
-
1 * 59000, SDS-PAGE
-
monomer
-
1 * 29000, SDS-PAGE
monomer
-
1 * 56000, SDS-PAGE
monomer
-
1 * 34000, cellulase III, SDS-PAGE
monomer
-
1 * 48000, cellulase II, SDS-PAGE
monomer
-
1 * 34000, cellulase III
monomer
-
1 * 51000, cellulase II
monomer
Thermochaetoides thermophila
-
1 * 36000, SDS-PAGE
monomer
Thermochaetoides thermophila
-
1 * 67800, SDS-PAGE
monomer
Thermochaetoides thermophila CT2
-
1 * 67800, SDS-PAGE
-
monomer
-
1 * 40000, SDS-PAGE
monomer
-
1 * 47000, SDS-PAGE
monomer
-
1 * 47000, SDS-PAGE
-
monomer
-
1 * 46000, SDS-PAGE
monomer
-
1 * 66000, SDS-PAGE
monomer
1 * 62600, calculated
tetramer
-
4 * 25000, SDS-PAGE
tetramer
-
4 * 42000, SDS-PAGE
tetramer
-
4 * 42000, SDS-PAGE
-
additional information
-
enzyme form C2, 33000 Da, is likely to by a trimer of endoglucanase C3, 104000 Da
additional information
-
modular enzyme that contains a family 30 carbohydrate-binding modules, CBM, and a family 9 catalytic module at its N-terminal moiety. The CBM is extremely important not only because it mediates the binding of the enzyme to the substrate but also because it participates in the catalytic function of the enzyme or contributes to maintain the correct tertiary structure of the family 9 catalytic module for expressing enzyme activity
additional information
the precursor form of CtCel9Q comprises a signal peptide, a glycoside hydrolase family 9 catalytic domain, a type 3c carbohydrate-binding module (CBM), and a type I dockerin domain
additional information
-
the precursor form of CtCel9Q comprises a signal peptide, a glycoside hydrolase family 9 catalytic domain, a type 3c carbohydrate-binding module (CBM), and a type I dockerin domain
additional information
-
modular enzyme that contains a family 30 carbohydrate-binding modules, CBM, and a family 9 catalytic module at its N-terminal moiety. The CBM is extremely important not only because it mediates the binding of the enzyme to the substrate but also because it participates in the catalytic function of the enzyme or contributes to maintain the correct tertiary structure of the family 9 catalytic module for expressing enzyme activity
-
additional information
the exoglucanase activity is located in the amino-terminal domain of the enzyme and the endoglucanase activity is located in the carboxy-terminal domain
additional information
Coleus scutellarioides
-
2 major protein bands detected by SDS-PAGE, 56000 Da and 62000 Da
additional information
-
CcCel6C consists of a distorted seven-stranded beta/alpha barrel and has an enclosed tunnel, that remains wide, structure, overview
additional information
a multidomain cellulase
additional information
the GH5 endoglucanase exhibits a (betaalpha)8 TIM barrel structure
additional information
-
the GH5 endoglucanase exhibits a (betaalpha)8 TIM barrel structure
additional information
-
the content of alpha-helix and beta-sheet increases in 5% butanol solution. The increasing of alpha-helix and beta-sheet content leads to higher activity and better thermostability in butanol solution
additional information
modular enzyme composed of a catalytic domain of family 5 of glycosyl hydrolases, a domain of unknown function, and a dockerin domain responsible for cellulosome assembly. The enzyme is a component of the cellulosome
additional information
-
modular enzyme composed of a catalytic domain of family 5 of glycosyl hydrolases, a domain of unknown function, and a dockerin domain responsible for cellulosome assembly. The enzyme is a component of the cellulosome
additional information
-
modular enzyme composed of a catalytic domain of family 5 of glycosyl hydrolases, a domain of unknown function, and a dockerin domain responsible for cellulosome assembly. The enzyme is a component of the cellulosome
-
additional information
the enzyme contains two domains, a core domain having a high similarity with endoglucanases family 5 and a cellulose-binding domain having similarities with those of exo-type cellulases of family 1, linked together by a serine-threonine-rich region, peptide mapping, mass spectrometric analysis
additional information
the enzyme contains two domains, a core domain having a high similarity with endoglucanases family 5 and a cellulose-binding domain having similarities with those of exo-type cellulases of family 1, linked together by a serine-threonine-rich region, peptide mapping, mass spectrometric analysis
additional information
the enzyme contains two domains, a core domain having a high similarity with endoglucanases family 5 and a cellulose-binding domain having similarities with those of exo-type cellulases of family 1, linked together by a serine-threonine-rich region, peptide mapping, mass spectrometric analysis
additional information
-
the enzyme contains two domains, a core domain having a high similarity with endoglucanases family 5 and a cellulose-binding domain having similarities with those of exo-type cellulases of family 1, linked together by a serine-threonine-rich region, peptide mapping, mass spectrometric analysis
additional information
-
the enzyme contains two domains, a core domain having a high similarity with endoglucanases family 5 and a cellulose-binding domain having similarities with those of exo-type cellulases of family 1, linked together by a serine-threonine-rich region, peptide mapping, mass spectrometric analysis
-
additional information
STCE1 consists of three distinct domains: an N-terminal catalytic domain (family 45), a linker domain, and a C-terminal carbohydrate-binding module (family 1)
additional information
-
STCE1 consists of three distinct domains: an N-terminal catalytic domain (family 45), a linker domain, and a C-terminal carbohydrate-binding module (family 1)
additional information
-
STCE1 consists of three distinct domains: an N-terminal catalytic domain (family 45), a linker domain, and a C-terminal carbohydrate-binding module (family 1)
-
additional information
the GH5 endoglucanase exhibits a (betaalpha)8 TIM barrel structure
additional information
-
the GH5 endoglucanase exhibits a (betaalpha)8 TIM barrel structure
additional information
domain organization, lack of a carbohydrate binding module
additional information
modeled tertiary structure of NMgh45, overview
additional information
-
the enzyme consists of a glycoside hydrolase family 6 catalytic domain (GH6) and a family 2 carbohydrate binding module (CBM2) that are connected by a linker rich in prolines and threonines
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D79A
site-directed mutagenesis
E186Q
-
mutant has no cellulase activity
E359Q
-
mutant has no cellulase activity
E435A
site-directed mutagenesis
F194A
-
site-directed mutagenesis, the mutant shows 2fold increased activity compared to wild-type enzyme
I62T/L79I/A93T/S308P/I370V/L374P/M416V/F472I/I484V/W494R
-
S40 mutant, DNA shuffling. Higher hydrolytic activities than the wild-type enzyme
K120E/D272H/S283G/S308P/L374P
-
M1-23 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme
K120E/S283G/S308P/L374P
-
M1 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme, shows 1.25fold increase in activity
N39D/K120E/N175H/V255A/S308P/L386S/K398R
-
S75 mutant, DNA shuffling. Higher hydrolytic activities than the wild-type enzyme
T32I/N39D/K120E/S248G/S283G/S308P/R314G/I370N/L374P/N403D/N451D/S467N
-
S78 mutant, DNA shuffling. Higher hydrolytic activities than the wild-type enzyme
V74A/K120E/D272G/K337E/S355P/D459G/K479E/K482E/K491N
-
M44 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme, shows 1.56fold increase in activity
V74A/K120E/D272G/K337E/S355P/T449I/D459G/K479E/K482E/D488N/K491N
-
M44-11 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme
K120E/D272H/S283G/S308P/L374P
-
M1-23 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme
-
K120E/S283G/S308P/L374P
-
M1 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme, shows 1.25fold increase in activity
-
V74A/K120E/D272G/K337E/S355P/D459G/K479E/K482E/K491N
-
M44 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme, shows 1.56fold increase in activity
-
V74A/K120E/D272G/K337E/S355P/T449I/D459G/K479E/K482E/D488N/K491N
-
M44-11 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme
-
DELTA1-90
expressed as a soluble protein in Pichia pastoris, the wild-type enzyme is anchored to membrane
A211D
-
site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme
A253S
-
site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme
D216C
-
replacement of Asp with cysteinesulfinate by combination of site-directed mutagenesis and chemical modification, the substituted cysteinyl residue is oxidized to cysteine sulfinic acid with hydrogen peroxide, the resulting protein product retains its native structure, almost inactive mutant
D216N
-
site-directed mutagenesis, the mutant shows reduced activity and a shift in pH dependence compared to the wild-type enzyme
D252C
-
site-directed mutagenesis, substitution of the catalytic acid residue Asp252, almost inactive mutant
D287C
-
site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme
D287E
-
site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme
D287N
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
D392A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D392C
-
replacement of Asp with cysteinesulfinate by combination of site-directed mutagenesis and chemical modification, the substituted cysteinyl residue is oxidized to cysteine sulfinic acid with hydrogen peroxide, the resulting protein product retains its native structure. Oxidation of the Asp392Cys mutant enzyme restores 52% of wild-type activity when assessed at pH 7.5. The replacement of Asp392 with cysteine sulfinate induced an acidic shift in the pH profile of the enzyme such that this enzyme derivative is more active than wild-type CenA below pH 5.5
D392N
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D392S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E368A
-
site-directed mutagenesis, the mutant shows reduced activity at pH values of pH 7 and pH 9, but increased activity at pH 5, compared to the wild-type enzyme
E368A/E407A
-
site-directed mutagenesis, the double mutant shows decreased activity at pH 5.0 compared to the wild-type enzyme
E407A
-
site-directed mutagenesis, the mutant shows reduced activity at pH values of pH 7 and pH 9, but increased activity at pH 5, compared to the wild-type enzyme
K292A
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
K292A/E407A
-
site-directed mutagenesis, the double mutant shows increased activity at pH 5.0 compared to the wild-type enzyme
L387P
-
site-directed mutagenesis, the mutant shows reduced activity at pH values of pH 7 and pH 9, but increased activity at pH 5, compared to the wild-type enzyme
N320C
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
N320D
-
site-directed mutagenesis, the mutant shows highly reduced activity at different pH values compared to the wild-type enzyme
N320E
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
N360D
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
N360H
-
site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme
N360K
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
N360R
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
Q256C
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
Q256D
-
site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme
Q256E
-
site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme
S319A
-
site-directed mutagenesis, the mutant shows reduced activity at different pH values compared to the wild-type enzyme
S319D
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
S319H
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
S319K
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
S319R
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
Y321A
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
Y321F
-
site-directed mutagenesis, the mutant shows reduced activity at pH values of pH 7 and pH 9, but increased activity at pH 5, compared to the wild-type enzyme
Y321F/E407A
-
site-directed mutagenesis, the double mutant shows increased activity at pH 5.0 compared to the wild-type enzyme
Y321H
-
site-directed mutagenesis, the mutant shows highly reduced activity at different pH values compared to the wild-type enzyme
Y321K
-
site-directed mutagenesis, almost inactive mutant, residual activity ta pH 7.0
Y321R
-
site-directed mutagenesis, the mutant shows highly reduced activity at different pH values compared to the wild-type enzyme
K94R
increase in specific activity
K94R/S365P
optimal temperature of K94R/S365P is increased by 7.5°C compared to wild-type. K94R/S365P retains 78.3% relative activity at 70°C, while the wild-type retains 5.8%. K94R/S365P shows 45.1fold higher activity than the wild-type at 70°C and 3.1fold higher activity at 42.5°C, which is the optimal temperature ofthe wild type. K94R/S365P is stimulated in 2.5fold lower concentration of CaCl2 and displays delayed aggregation temperature in the presence of CaCl2 compared to the wild type. In long-term hydrolysis, K94R/S365P reduces the newly released reducing sugars after 12 h reaction
S365P
increase in specific activity
K94R
-
increase in specific activity
-
K94R/S365P
-
optimal temperature of K94R/S365P is increased by 7.5°C compared to wild-type. K94R/S365P retains 78.3% relative activity at 70°C, while the wild-type retains 5.8%. K94R/S365P shows 45.1fold higher activity than the wild-type at 70°C and 3.1fold higher activity at 42.5°C, which is the optimal temperature ofthe wild type. K94R/S365P is stimulated in 2.5fold lower concentration of CaCl2 and displays delayed aggregation temperature in the presence of CaCl2 compared to the wild type. In long-term hydrolysis, K94R/S365P reduces the newly released reducing sugars after 12 h reaction
-
S365P
-
increase in specific activity
-
G117S
1.6fold increase in activity, mutation might directly affect the substratebinding affinity
V9A/K353E
1.4fold increase in activity, mutation might directly affect the substratebinding affinity
D117N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N95D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D117N
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
N95D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
A241E
improved thermal stability
D114A
complete loss of activity
D85A
about 10% of wild-type activity
F206Y
improved thermal stability
M259I
improved thermal stability
M259L
improved thermal stability
N125K
improved thermal stability
N92D
replaxement of the general base in the catalytic mechanism, drastic decrease in activity. Unlike Asn92, residue Asp92 is mobile
Q204K
improved thermal stability
Q307R/A309S
improved thermal stability
Q381S/F382L
improved thermal stability
S183T
improved thermal stability
S22P
thermostability similar to wild-type
T112S
improved thermal stability
T130I/S134Q
improved thermal stability
T130I/S134Q/M259I/A241E/S183T/Q307R/A309S
temperature required to reduce the initial activity by 50% within 120 min is increased by 4.4 degrees compared to wild-type
T130I/S134Q/M259I/A241E/S183T/Q307R/A309S/T112S/N125K/Q204K/F206Y/I365
temperature required to reduce the initial activity by 50% within 120 min is increased by 5.4 degrees compared to wild-type, specific activity is the same as wild-type
T342HI365V
improved thermal stability
W154A
about 50% of wild-type activity
Y18A
about 80% of wild-type activity
C106A/C159A
kcat/KM for p-nitrophenyl cellobiose is 1.3fold higher than wild-type value. Activity towards carboxymethyl cellulose is increased by 1.7fold
C106A/C159A/C372A/C412A
kcat/KM for p-nitrophenyl cellobiose is 1.4fold higher than wild-type value. Activity towards carboxymethyl cellulose is increased by 2.1fold
C106S
melting temperature of the mutant enzyme is 2°C lower than the wild-type enzyme
C159A
kcat/KM for p-nitrophenyl cellobiose is 1.8fold lower than wild-type value
C372/AC412A
kcat/KM for p-nitrophenyl cellobiose is 2.9fold higher than wild-type value. Activity towards carboxymethyl cellulose is increased by 1.6fold
D385N
activity towards carboxymethyl cellulose is 29.9% of wild-type activity
DELTAQ1-G5
activity towards carboxymethyl cellulose is 135.6% of wild-type activity. kcat/Km for p-nitrophenyl cellobiose is 2.3fold higher than wild-type value. Thermostability is not significantly influenced
E163A
kcat/KM for p-nitrophenyl cellobiose is 6fold lower than wild-type value
E201Q
activity towards carboxymethyl cellulose is 1.12% of wild-type activity. kcat/Km for p-nitrophenyl cellobiose is 43fold lower than wild-type value
E342Q
activity towards carboxymethyl cellulose is 0.01% of wild-type activity
G158A
kcat/KM for p-nitrophenyl cellobiose is 2fold lower than wild-type value
H155A
kcat/KM for p-nitrophenyl cellobiose is 140fold lower than wild-type value
H161A
kcat/KM for p-nitrophenyl cellobiose is neatrly identical to wild-type value
H297A
activity towards carboxymethyl cellulose is 0.08% of wild-type activity
H297N
activity towards carboxymethyl cellulose is 1.31% of wild-type activity. pH-optimum is 7.0, compared to 5.5-6 for wild-type enzyme
I157A
kcat/KM for p-nitrophenyl cellobiose is nearly identical to wild-type value
I162A
kcat/KM for p-nitrophenyl cellobiose is 140fold lower than wild-type value
N200A
activity towards carboxymethyl cellulose is 5.43% of wild-type activity
P164A
kcat/KM for p-nitrophenyl cellobiose is 6fold lower than wild-type value
P74C
melting temperature of the mutant enzyme is 2°C lower than the wild-type enzyme
P74C/C106S
melting temperature of the mutant enzyme is 2°C lower than the wild-type enzyme
Q306A
25% of the activity with avicel as compared to wild-type enzyme
R102A
activity towards carboxymethyl cellulose is 0.67% of wild-type activity
R156A
kcat/KM for p-nitrophenyl cellobiose is 10fold lower than wild-type value
T160A
kcat/KM for p-nitrophenyl cellobiose is nearly identical to wild-type value
W82A
75% of the activity with avicel as compared to wild-type enzyme
Y299A
activity towards carboxymethyl cellulose is 0.21% of wild-type activity
C106S
-
melting temperature of the mutant enzyme is 2°C lower than the wild-type enzyme
-
P74C
-
melting temperature of the mutant enzyme is 2°C lower than the wild-type enzyme
-
P74C/C106S
-
melting temperature of the mutant enzyme is 2°C lower than the wild-type enzyme
-
Q306A
-
25% of the activity with avicel as compared to wild-type enzyme
-
W377A
-
complete loss of activity with avicel
-
W82A
-
75% of the activity with avicel as compared to wild-type enzyme
-
Y299F
-
complete loss of activity with avicel
-
A3V/A6Q/T7K/A8P/N10T/E18K/P22D/P58T/Y60L/N157A/D181N/E183Q
mutant is more active and stable than wild-type Cel7A or Trichoderma reesei Cel7A in aqueous ionic liquids solutions, i.e. up to 43% (w/w) 1,3-dimethylimdazolium dimethylphosphate and 20% (w/w) 1-ethyl-3-methylimidazolium acetate
A6L/A8E/N10V/P58E/T59S/Y60L/L73V/G80A/V84I/S87N/S89D/K92T/L105V/L108M/Q109E/N220T/V222F/S301K/I308V/S311G/N312K/Q316N/P317S/N318E/D320T/I321W/T325G/T438N/G439P/T440P/P441G/S442G/H471M
mutant is more active and stable than wild-type Cel7A or Trichoderma reesei Cel7A in aqueousionic liquids solutions, i.e. up to 43% (w/w) 1,3-dimethylimdazolium dimethylphosphate and 20% (w/w) 1-ethyl-3-methylimidazolium acetate. Increase in melting temperature of 1.9-3.9°C compared to wild-type
G266C/D320C
introduction of an additional disulfide bridge, decrease in activity
G4C/A72C
introduction of an additional disulfide bridge, improves thermostability
G4C/A72C/N54C/P191C/T243C/A375C
introduction of 3 additional disulfide bridges, improves thermostability
N54C/P191C
introduction of an additional disulfide bridge, improves thermostability
Q190C/I200C
introduction of an additional disulfide bridge, decrease in activity
T243C/A375C
introduction of an additional disulfide bridge, improves thermostability
A170S
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
A87S
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D53X
-
site-directed mutagenesis, inactive mutant
D56X
-
site-directed mutagenesis, inactive mutant
E411X
-
site-directed mutagenesis, inactive mutant
G147R
-
site-directed mutagenesis, inactive mutant
G91A
-
site-directed mutagenesis, the mutant has 3-4fold higher activity towards carboxymethyl cellulose than the wild type enzyme
G91A/K429A
-
site-directed mutagenesis, the double mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects
G91A/Y97W
-
site-directed mutagenesis, the double mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects
G91A/Y97W/G147R
-
site-directed mutagenesis, inactive mutant
G91A/Y97W/K429A
-
site-directed mutagenesis, the triple mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects
G91I
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
I347V
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K429A
-
site-directed mutagenesis, the mutant has 3-4fold higher activity towards carboxymethyl cellulose than the wild type enzyme
L103I
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N245S
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N38D
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Q202K
-
site-directed mutagenesis, almost inactive mutant
Q42N/K43N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S173A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S25A
-
site-directed mutagenesis, almost inactive mutant
S90D
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y329F
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y97F
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y97W
-
site-directed mutagenesis, the mutant has 3-4fold higher activity towards carboxymethyl cellulose than the wild type enzyme
Y97W/K429A
-
site-directed mutagenesis, the double mutant has 7-13fold higher activity towards carboxymethyl cellulose than the wild type enzyme, the mutations show synegistic effects
E410Q
-
mutation totally inactivates carboxymethyl cellulase activity of the protein
E44Q
inactive mutant enzyme
E55Q
inactive mutant enzyme
G145D/N207K
random mutagenesis, the mutant shows increased activity with carboxymethyl cellulose compared to the wild-type enzyme
G263C/R307H
random mutagenesis, the mutant shows increased activity with carboxymethyl cellulose compared to the wild-type enzyme
P228R
random mutagenesis, the mutant shows increased activity with carboxymethyl cellulose compared to the wild-type enzyme
T157I/G251D/V259D
random mutagenesis, the mutant shows increased activity with carboxymethyl cellulose compared to the wild-type enzyme
T67N/D142E/S218N/V242D/D330E
random mutagenesis, the mutant shows increased activity with carboxymethyl cellulose compared to the wild-type enzyme
N194A
-
mutation in potential N-glycosylation site, no notable effect on the enzyme thermostability. Slight shift of pH optimum 4.5 for wild-type to 5.0 and 32-35% increase in the specific activity against carboxymethylcellulose and barley beta-glucan
N19A
-
mutation in potential N-glycosylation site, no notable effect on the enzyme thermostability but 26% decrease in the specific activity against carboxymethylcellulose and 12% against barley beta-glucan
N42A
-
mutation in potential N-glycosylation site, no notable effect on the enzyme thermostability. Slight shift of pH optimum 4.5 for wild-type to 5.0 and 12-13% increase in the specific activity against carboxymethylcellulose and barley beta-glucan
S127C/A165C
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB2, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
Y171C/L201C
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB3, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
S127C/A165C
-
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB2, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
-
Y171C/L201C
-
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB3, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
-
S127C/A165C
-
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB2, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
-
Y171C/L201C
-
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB3, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
-
S127C/A165C
-
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB2, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
-
Y171C/L201C
-
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB3, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
-
S127C/A165C
-
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB2, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
-
Y171C/L201C
-
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB3, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
-
S127C/A165C
-
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB2, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
-
Y171C/L201C
-
site-directed mutagenesis, introduction of a disulfide bond into mutant DSB3, the mutant enzyme displays 15-21% increased specific activity against carboxymethylcellulose and beta-glucan, and increased thermostability compared to wild-type enzyme EGLII
-
D117A
-
activity with carboxymethyl cellulose is 0.03% of wild-type activity, activity with phosphoric acid-swollen cellulose is 0.02% of wild-type activity
D261A/R378K
-
Cel9A mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center. Mutant has weak chitinase activity, but no soluble products are detected
D55A
activity with carboxymethyl cellulose is 0.2% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.2% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 1.6% of wild-type activity
D55A/D58A
activity with carboxymethyl cellulose is less than 0.1% of wild-type activity, activity with phosphoric acid-swollen cellulose is 0.13% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 0.5% of wild-type activity
D55N
activity with carboxymethyl cellulose is 0.3% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.6% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 2.2% of wild-type activity
D58A
activity with carboxymethyl cellulose is 0.4% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.8% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 3.5% of wild-type activity, mutant enzyme loses about 90% of the initial activity after 15 h at 65°C, compared to 10% loss of wild-type activity
D58N
activity with carboxymethyl cellulose is 0.45% of wild-type activity, activity with phosphoric acid-swollen cellulose is 2% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 2.7% of wild-type activity, mutant enzyme loses about 20% of the initial activity after 15 h at 65°C, compared to 10% loss of wild-type activity
DELTAT245-L251/R252K
activity with carboxymethyl cellulose, acid-swollen cellulose or bacterial microcrystalline cellulose from Acetobacter xylinum is nearly identical to wild-type activity
E424A
activity with carboxymethyl cellulose is 0.13% of wild-type activity, activity with phosphoric acid-swollen cellulose is 0.2% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 0.43% of wild-type activity, kcat/Km for 2,4-dinitrophenyl beta-D-cellobioside is 8.5fold higher than the wild-type value
E424G
activity with carboxymethyl cellulose is 0.3% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.1% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 2.5% of wild-type activity, kcat/Km for 2,4-dinitrophenyl beta-D-cellobioside is 123.8fold higher than the wild-type value
E424Q
activity with carboxymethyl cellulose is less than 0.1% of wild-type activity, activity with phosphoric acid-swollen cellulose is 0.15% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 1.1% of wild-type activity
G234S
-
Cel6B mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center
R78A
-
activity with phosphoric acid-swollen cellulose is less than 1.3% of the wild-type activity, activity with carboxymethylcellulose is less than 0.9% of the wild-type activity, activity with bacterial microcrystalline cellulose is less than 18.7% of the wild-type activity
R78K
-
activity with phosphoric acid-swollen cellulose is 54% of the wild-type activity, activity with carboxymethylcellulose is 15% of the wild-type activity, activity with bacterial microcrystalline cellulose is 52% of the activity with wild-type enzyme
W209S
-
active site mutant
W256A
-
active site mutant
W313G
-
active site mutant
W329C
-
Cel6B mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center
W332A
-
Cel6B mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center
Y318A
activity with carboxymethyl cellulose is 5fold higher than wild-type activity, activity with phosphoric acid-swollen cellulose is 28% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 14.2% of wild-type activity, mutant enzyme loses about 30% of the initial activity after 15 h at 65°C, compared to 10% loss of wild-type activity
Y318F
activity with carboxymethyl cellulose is 6.7fold higher than wild-type activity, activity with phosphoric acid-swollen cellulose is 75% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 16.6% of wild-type activity
Y73F
-
activity with carboxymethyl cellulose is 8.4% of wild-type activity, activity with phosphoric acid-swollen cellulose is 5.7% of wild-type activity
Y73S
-
activity with carboxymethyl cellulose is 0.022% of wild-type activity, activity with phosphoric acid-swollen cellulose is 0.088% of wild-type activity
D55A
-
activity with carboxymethyl cellulose is 0.2% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.2% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 1.6% of wild-type activity
-
D55N
-
activity with carboxymethyl cellulose is 0.3% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.6% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 2.2% of wild-type activity
-
D58A
-
activity with carboxymethyl cellulose is 0.4% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.8% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 3.5% of wild-type activity, mutant enzyme loses about 90% of the initial activity after 15 h at 65°C, compared to 10% loss of wild-type activity
-
D58N
-
activity with carboxymethyl cellulose is 0.45% of wild-type activity, activity with phosphoric acid-swollen cellulose is 2% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 2.7% of wild-type activity, mutant enzyme loses about 20% of the initial activity after 15 h at 65°C, compared to 10% loss of wild-type activity
-
Y173F
Thermochaetoides thermophila
1.9fold increased the enzyme's specific activity. Mutation significantly improves the enzymes heat resistance at 80°C and 90°C
Y30F
Thermochaetoides thermophila
1.4fold increased the enzyme's specific activity
Y30F/Y173F
Thermochaetoides thermophila
mutant shows considerably higher stability at elevated temperatures but does not display the increased catalytic efficiency of its single mutant counterparts
A153V
mutant with increased activity on 1-ethyl-3-methylimidazolium acetate pretreated biomass. Mutant displays 130% of wild-type activity with carboxymethyl cellulose
E134C
site-directed mutagenesis, the catalytically inactive active-site mutant adopts a beta-jellyroll protein fold typical of the GH12-family enzymes, with two curved beta-sheets A and B and a central active-site cleft, crystal structure determination, overview
E225H/K207G
mutant based on homology modeling and rational design, display significantly improved activity and thermostability
E225H/K207G/D37V
mutant based on homology modeling and rational design, display significantly improved activity and thermostability
H138R
mutant with increased activity on 1-ethyl-3-methylimidazolium acetate pretreated biomass. Mutant displays 130% of wild-type activity with carboxymethyl cellulose
N236D
mutant with increased activity on 1-ethyl-3-methylimidazolium acetate pretreated biomass. Mutant displays 142% of wild-type activity with carboxymethyl cellulose
R60A
about 45% of wild-type activity
R60K
about 70% of wild-type activity
Y61A
about 120% of wild-type activity
Y61del
about 10% of wild-type activity
Y61F
about 140% of wild-type activity
Y61G
about 170% of wild-type activity. Mutant also shows a wider range of working temperatures than does the wild type, along with retention of the hyperthermostability. The kcat and Km values of Y61G are both higher than those of the wild type. The higher endoglucanase activity is probably due to facile dissociation of the cleaved sugar moiety at the reducing end
Y61GG
insertion mutant, about 40% of wild-type activity
Y61R
about 70% of wild-type activity
Y61W
about 80% of wild-type activity
Y66F
mutant with increased activity on 1-ethyl-3-methylimidazolium acetate pretreated biomass. Mutant displays 132% of wild-type activity with carboxymethyl cellulose
A153V
-
mutant with increased activity on 1-ethyl-3-methylimidazolium acetate pretreated biomass. Mutant displays 130% of wild-type activity with carboxymethyl cellulose
-
E225H/K207G
-
mutant based on homology modeling and rational design, display significantly improved activity and thermostability
-
E225H/K207G/D37V
-
mutant based on homology modeling and rational design, display significantly improved activity and thermostability
-
H138R
-
mutant with increased activity on 1-ethyl-3-methylimidazolium acetate pretreated biomass. Mutant displays 130% of wild-type activity with carboxymethyl cellulose
-
N236D
-
mutant with increased activity on 1-ethyl-3-methylimidazolium acetate pretreated biomass. Mutant displays 142% of wild-type activity with carboxymethyl cellulose
-
Y66F
-
mutant with increased activity on 1-ethyl-3-methylimidazolium acetate pretreated biomass. Mutant displays 132% of wild-type activity with carboxymethyl cellulose
-
G155C/G169C
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 54.9°C, decrease in activity with filter paper and avicel
G155C/N182C
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.5°C, decrease in activity with filter paper and avicel
G155C/N182C/N160C/G183C
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.9°C, decrease in activity with filter paper
G170C
Tm is 2.1°C higher than wild-type value, specific activity is 1.2fold higher than wild-type enzyme
G170C/P201C
Tm is 0.7°C higher than wild-type value, specific activity is 38% of wild-type value
G170C/P201C/V210C
Tm is 3.9°C higher than wild-type value, specific activity is 14% of wild-type value
G170C/V210C
specific activity is 1.4fold higher than wild-type value
G4C/E73C
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.9°C, decrease in activity with filter paper and avicel
G4C/F71C
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.9°C, decrease in activity with avicel
G4C/F71C/G155C/N182C
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 60.7°C, increase in activity with filter paper and avicel
G4C/F71C/G155C7N182C/N160C/G183C
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 60.6°C, decrease in activity with filter paper and avicel
G4C/F71C/N160C/G183C
introduction of disulfide bonds for stabilization of the catalytic domain, melting temperature 60.4°C, decrease in activity with filter paper and avicel
G4C/F71C/N160C/G183C/S168T
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 62.8°C, increase in activity with filter paper and avicel
G81C/V105C
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 55.9°C, decrease in activity with filter paper and avicel
K272F
mutation predicted to be thermostabilizing. Both high temperature and room temperature molecular dynamics simulations supported a stabilizing effect. Mutant exhibits higher thermostability compared with native EGI, but the specific activity of the mutant is lower
N160C/G183C
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.8°C, decrease in activity with filter paper and avicel
Q126F
mutation predicted to be thermostabilizing. Both high temperature and room temperature molecular dynamics simulations supported a stabilizing effect. Mutant exhibits higher thermostability compared with native EGI, but the specific activity of the mutant is lower
Q274V
mutation predicted to be thermostabilizing. Both high temperature and room temperature molecular dynamics simulations supported a stabilizing effect. Mutant exhibits higher thermostability compared with native EGI, but the specific activity of the mutant is lower
S213C/A296C
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 55.3°C, decrease in activity with filter paper and avicel
T57N/E53D/S79P/T80E/V101I/S133R/N155E/G189S/F191V/T233V/G239E/V265T/D271Y/G293A7S309W/S318P
thermostable mutant combining previously identified stabilizing mutations. Mutant has an optimal temperature 17°C higher than wild type and hydrolyzes 1.5 times as much cellulose over 60 h at its optimum temperature compared to the wild type enzyme at its optimal temperature
Y326C/G343C
introduction of disulfide bonds for stabilization of the catalytic domain, melting temperature 57.3°C, increase in activity with filter paper and decrease in activity with avicel
G155C/G169C
-
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 54.9°C, decrease in activity with filter paper and avicel
-
G155C/N182C
-
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.5°C, decrease in activity with filter paper and avicel
-
G4C/E73C
-
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.9°C, decrease in activity with filter paper and avicel
-
G4C/F71C
-
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.9°C, decrease in activity with avicel
-
G81C/V105C
-
introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 55.9°C, decrease in activity with filter paper and avicel
-
T57N/E53D/S79P/T80E/V101I/S133R/N155E/G189S/F191V/T233V/G239E/V265T/D271Y/G293A7S309W/S318P
-
thermostable mutant combining previously identified stabilizing mutations. Mutant has an optimal temperature 17°C higher than wild type and hydrolyzes 1.5 times as much cellulose over 60 h at its optimum temperature compared to the wild type enzyme at its optimal temperature
-
D99A
106% of wild-type activity, temperature of the midpoint of the thermal denaturation transition is decreased by 1.9°C
Q40A
94% of wild-type activity
Q40A/D99A
97% of wild-type activity, temperature of the midpoint of the thermal denaturation transition is decreased by 5.0°C
E289V
-
mutation identified by error-prone rolling circle amplification. Mutation results in a 7.93-fold increase in its enzymatic activity
E289V
-
mutation identified by error-prone rolling circle amplification. Mutation results in a 7.93-fold increase in its enzymatic activity
-
E201A
activity towards carboxymethyl cellulose is 0.01% of wild-type activity
E201A
site-directed mutagenesis, crystal structure determination with bound ligands
E342A
activity towards carboxymethyl cellulose is 0.08% of wild-type activity, no activity with p-nitrophenyl cellobiose
E342A
site-directed mutagenesis, crystal structure determination with bound ligands
W377A
activity towards carboxymethyl cellulose is 1.02% of wild-type activity
W377A
complete loss of activity with avicel
Y299F
activity towards carboxymethyl cellulose is 2.15% of wild-type activity. pH-optimum is 8.5, compared to 5.5-6 for wild-type enzyme
Y299F
site-directed mutagenesis, crystal structure determination with bound ligands, the mutant shows reduced activity compare to the wild-type enzyme, and a rare enzyme-substrate complex structure
Y299F
complete loss of activity with avicel
Y206F
activity with carboxymethyl cellulose is 7% of wild-type activity, activity with phosphoric acid-swollen cellulose is 4.1% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 8.3% of wild-type activity, mutant enzyme loses about 20% of the initial activity after 15 h at 65°C, compared to 10% loss of wild-type activity
Y206F
-
Cel9A mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center
Y206S
activity with carboxymethyl cellulose is 0.5% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.3% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 1.8% of wild-type activity
Y206S
-
Cel9A mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center
P201C
Tm is 0.7°C higher than wild-type value, specific activity is 50% of wild-type value
P201C
Tm is 3.9°C higher than wild-type value, specific activity is 80% of wild-type value
V210C
Tm is 0.1°C higher than wild-type value, specific activity is 1.8fold of the wild-type value
V210C
Tm is identical to wild-type value, specific activity is 80% of wild-type value
additional information
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construction of truncated enzyme forms
additional information
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deletion variants
additional information
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construction of a His6-tagged truncated enzyme mutant CtLic26A-Cel5
additional information
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replacement of carbohydrate-binding module either with a family 3 microcrystalline cellulose-directed carbohydrate-binding module from Clostridium josui scaffoldin, or a family 6 xylan-directed carbohydrate-binding module from Clostridium stercorarium xylanase 11A. Chimeric endoglucanases show enhanced activity that is affected by carbohydrate-binding module binding specificity. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls
additional information
construction of a C-terminally truncated enzyme, CtCel9QDELTAc
additional information
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construction of a C-terminally truncated enzyme, CtCel9QDELTAc
additional information
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enzyme mutant CtGH5-F194A is fused with a beta-1,4-glucosidase, CtGH1 from Clostridium thermocellum to develop a chimeric enzyme. Improved structural integrity, thermostability and enhanced bifunctional enzyme activities of the chimeric mutant compared to the single point mutant
additional information
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replacement of carbohydrate-binding module either with a family 3 microcrystalline cellulose-directed carbohydrate-binding module from Clostridium josui scaffoldin, or a family 6 xylan-directed carbohydrate-binding module from Clostridium stercorarium xylanase 11A. Chimeric endoglucanases show enhanced activity that is affected by carbohydrate-binding module binding specificity. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls
-
additional information
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construction of truncated enzyme forms
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additional information
deletion of the Ig-like domain in the N-terminus of the catalytic domain increases the catalytic efficiency of the truncated enzyme up to 3fold without any significant changes in the Km of the enzyme and shifts pH and temperature optimum for activity from 6.5 to 7.5 and from 65 to 60°C, respectively
additional information
creation of a hybrid enzyme of GH5 endoglucanase AnCel5A from Aspergillus niger with elements of the mesophilic endoglucanase Cel5 from Stegonsporium opalus (SoCel5). The expressed hybrid enzyme exhibits increased enzyme activity relative to the values for the mesophilic parent enzyme. The mutant demonstrates improved catalytic efficiency on selected substrates. Method validation, overview
additional information
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improvement of endoglucanase activity by utilizing error-prone rolling circle amplification, supplemented with 1.7 mM MnCl2. The procedure generates random mutations in the Bacillus amyloliquefaciens endoglucanase gene with a frequency of 10 mutations per kilobase
additional information
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improvement of endoglucanase activity by utilizing error-prone rolling circle amplification, supplemented with 1.7 mM MnCl2. The procedure generates random mutations in the Bacillus amyloliquefaciens endoglucanase gene with a frequency of 10 mutations per kilobase
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additional information
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construction of chimeric enzymes between the Bacillus subtilis cellulase and an alkalophilic Bacillus cellulase
additional information
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C-terminus truncation mutant Egl330, truncation of the cellulose binding domain, a great improvement in thermal stability is observed in Egl330
additional information
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variants (M44-11, S75 and S78) show 2.03fold to 2.68fold increased activities toward sodium carboxymethyl cellulose
additional information
generation of a set of chimeric proteins derived from the recombination of Geobacillus sp. CelA and Bacillus subtilis 168 Cel5A. The designed chimeras are assembled from 16 gene fragments of the two parents. Chimeric cellulase C10 shows significantly higher activity (22%-43%) and higher thermostability compared to the parental enzymes. A 310 helix is responsible for the improved thermostability. In the presence of ionic calcium and crown ether, the chimeric C10 retains 40% residual activity even after heat treatment at 90°C
additional information
cellulolytic activity of Paenibacillus sp. strain CAA11 is significantly enhanced by expressing a heterologous endoglucanase 168Cel5 from Bacillus subtilis under both aerobic and anaerobic conditions. The strain harboring the 168cel5 gene reveals 2fold bigger halo zone on Congo-red plate and 1.75fold more aerobic cellulose utilization in liquid medium compared with the negative control. Under anaerobic conditions, the recombinant strain expressing 168Cel5 consumes 1.83fold more cellulose (5.10 g/l) and produces 5fold more ethanol (0.65 g/l) along with 5fold more total acids (1.6 g/l) compared with the control, resulting in 2.73fold higher yields
additional information
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cellulolytic activity of Paenibacillus sp. strain CAA11 is significantly enhanced by expressing a heterologous endoglucanase 168Cel5 from Bacillus subtilis under both aerobic and anaerobic conditions. The strain harboring the 168cel5 gene reveals 2fold bigger halo zone on Congo-red plate and 1.75fold more aerobic cellulose utilization in liquid medium compared with the negative control. Under anaerobic conditions, the recombinant strain expressing 168Cel5 consumes 1.83fold more cellulose (5.10 g/l) and produces 5fold more ethanol (0.65 g/l) along with 5fold more total acids (1.6 g/l) compared with the control, resulting in 2.73fold higher yields
additional information
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generation of a set of chimeric proteins derived from the recombination of Geobacillus sp. CelA and Bacillus subtilis 168 Cel5A. The designed chimeras are assembled from 16 gene fragments of the two parents. Chimeric cellulase C10 shows significantly higher activity (22%-43%) and higher thermostability compared to the parental enzymes. A 310 helix is responsible for the improved thermostability. In the presence of ionic calcium and crown ether, the chimeric C10 retains 40% residual activity even after heat treatment at 90°C
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additional information
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cellulolytic activity of Paenibacillus sp. strain CAA11 is significantly enhanced by expressing a heterologous endoglucanase 168Cel5 from Bacillus subtilis under both aerobic and anaerobic conditions. The strain harboring the 168cel5 gene reveals 2fold bigger halo zone on Congo-red plate and 1.75fold more aerobic cellulose utilization in liquid medium compared with the negative control. Under anaerobic conditions, the recombinant strain expressing 168Cel5 consumes 1.83fold more cellulose (5.10 g/l) and produces 5fold more ethanol (0.65 g/l) along with 5fold more total acids (1.6 g/l) compared with the control, resulting in 2.73fold higher yields
-
additional information
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variants (M44-11, S75 and S78) show 2.03fold to 2.68fold increased activities toward sodium carboxymethyl cellulose
-
additional information
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C-terminus truncation mutant Egl330, truncation of the cellulose binding domain, a great improvement in thermal stability is observed in Egl330
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additional information
construction of deletion mutants expressing solely the carboxyterminal domain containing the endoglucanase activity. Temperature optimum and stability of the deletion mutants are the same as wild-type
additional information
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construction of a chimeric xylanase/endoglucanase with an internal cellulase-binding domain by fusing the Bacillus subtilis xyn gene fragment to the 5'-end of the Cellulomonas fimi cenA. The hybrid protein behaves like the parental endoglucanase or xylanase when assayed on a number of soluble and insoluble substrates or xylans
additional information
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engineering of cellulase A from Cellulomonas fimi as a model to replace residues that potentially influence the pH-activity profile of the enzyme based on sequence alignments and analysis of the known three-dimensional structures of other CAZy family 6 glycoside hydrolases with the aim to lower its pH optimum, overview
additional information
EngHDELTACBM devoid of the carbohydrate binding module loses activity toward all substrates including carboxymethylcellulose
additional information
EngHDELTACBM devoid of the carbohydrate binding module loses activity toward all substrates including carboxymethylcellulose
additional information
EngHDELTACBM devoid of the carbohydrate binding module loses activity toward all substrates including carboxymethylcellulose
additional information
EngHDELTACBM devoid of the carbohydrate binding module loses activity toward all substrates including carboxymethylcellulose
additional information
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EngHDELTACBM devoid of the carbohydrate binding module loses activity toward all substrates including carboxymethylcellulose
additional information
EngMDELTSACBM, devoid of the carbohydrate binding module has activity toward CMC (0.003 U/mg), in contrast with no activity toward any other substrate
additional information
EngMDELTSACBM, devoid of the carbohydrate binding module has activity toward CMC (0.003 U/mg), in contrast with no activity toward any other substrate
additional information
EngMDELTSACBM, devoid of the carbohydrate binding module has activity toward CMC (0.003 U/mg), in contrast with no activity toward any other substrate
additional information
EngMDELTSACBM, devoid of the carbohydrate binding module has activity toward CMC (0.003 U/mg), in contrast with no activity toward any other substrate
additional information
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EngMDELTSACBM, devoid of the carbohydrate binding module has activity toward CMC (0.003 U/mg), in contrast with no activity toward any other substrate
additional information
EngYDELTSACBM, devoid of the carbohydrate binding module loses activity toward all substrates including carboxymethylcellulose
additional information
EngYDELTSACBM, devoid of the carbohydrate binding module loses activity toward all substrates including carboxymethylcellulose
additional information
EngYDELTSACBM, devoid of the carbohydrate binding module loses activity toward all substrates including carboxymethylcellulose
additional information
EngYDELTSACBM, devoid of the carbohydrate binding module loses activity toward all substrates including carboxymethylcellulose
additional information
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EngYDELTSACBM, devoid of the carbohydrate binding module loses activity toward all substrates including carboxymethylcellulose
additional information
C-terminal His-tagged form (tCfEG) shows hydrolytic activity on cellulosic substrates
additional information
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C-terminal His-tagged form (tCfEG) shows hydrolytic activity on cellulosic substrates
additional information
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fusion of the cellulose binding domain of cellobiohydrolase I from Trichoderma reesei to the C-terminus of Cryptococcus sp. carboxymethyl cellulase and expression in a recombinant expression system of Cryptococcus sp. S-2. The recombinant fusion enzymes display optimal pH similar to those of the native enzyme. Compared with Cryptococcus sp. carboxymethyl cellulase, the recombinant fusion enzymes have acquired an increased binding affinity to insoluble cellulose, and the cellulolytic activity toward insoluble cellulosic substrates, SIGMACELL and Avicel, is higher than that of native enzyme, confirming the presence of cellulose binding domains improve the binding and the cellulolytic activity of carboxymethyl cellulase on insoluble substrates
additional information
generation of a set of chimeric proteins derived from the recombination of Geobacillus sp. CelA and Bacillus subtilis 168 Cel5A. The designed chimeras are assembled from 16 gene fragments of the two parents. Chimeric cellulase C10 shows significantly higher activity (22%-43%) and higher thermostability compared to the parental enzymes. A 310 helix is responsible for the improved thermostability. In the presence of ionic calcium and crown ether, the chimeric C10 retains 40% residual activity even after heat treatment at 90°C
additional information
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generation of a set of chimeric proteins derived from the recombination of Geobacillus sp. CelA and Bacillus subtilis 168 Cel5A. The designed chimeras are assembled from 16 gene fragments of the two parents. Chimeric cellulase C10 shows significantly higher activity (22%-43%) and higher thermostability compared to the parental enzymes. A 310 helix is responsible for the improved thermostability. In the presence of ionic calcium and crown ether, the chimeric C10 retains 40% residual activity even after heat treatment at 90°C
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additional information
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gene celF knockout prevents growth on cellulose although the mutant strain grows perfectly well on glucose, but does not affect other cellulase genes expressions, overview
additional information
cellulolytic activity of Paenibacillus sp. strain CAA11 is significantly enhanced by expressing a heterologous endoglucanase 168Cel5 from Bacillus subtilis (DNA sequences encoding P43 promoter, signal peptide of Bacillus subtilis nprB, and mature Bacillus subtilis strain 168 Cel5 residues 30-499) under both aerobic and anaerobic conditions. The strain harboring the 168cel5 gene reveals 2fold bigger halo zone on Congo-red plate and 1.75fold more aerobic cellulose utilization in liquid medium compared with the negative control. Under anaerobic conditions, the recombinant strain expressing 168Cel5 consumes 1.83fold more cellulose (5.10 g/l) and produces 5fold more ethanol (0.65 g/l) along with 5fold more total acids (1.6 g/l) compared with the control, resulting in 2.73fold higher yields. Optimal growth of the engineered strain at 37°C, evaluation of optimal growth conditions, overview
additional information
both the full-length enzyme and the catalytic domain have carboxymethylcellulase and filter paper hydrolase activity . The catalytic domain can also bind the cellulose substrate. The aromatic amino acids at the bottom of the barrel fold and those adjacent to the catalytic site significantly affect the cellulolytic activity and the cellulose binding affinity of the catalytic domain
additional information
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both the full-length enzyme and the catalytic domain have carboxymethylcellulase and filter paper hydrolase activity . The catalytic domain can also bind the cellulose substrate. The aromatic amino acids at the bottom of the barrel fold and those adjacent to the catalytic site significantly affect the cellulolytic activity and the cellulose binding affinity of the catalytic domain
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additional information
amino acids, E209 and E319, act as proton donor and nucleophile in the catalytic domain
additional information
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amino acids, E209 and E319, act as proton donor and nucleophile in the catalytic domain
additional information
PopCel1 mRNA is accumulated in seven transgenic lines of Paraserianthes falcataria
additional information
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hybrid cellulase with the Thermomonospora fusca E2 cellulose-binding domain at its C terminus joined to the Prevotella ruminicola 40500 Da carboxymethylcellulase
additional information
a truncated EGPf (EGPfDELTAN30) mutant lacking the proline and hydroxyl-residue rich region at the N-terminus is constructed
additional information
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a truncated EGPf (EGPfDELTAN30) mutant lacking the proline and hydroxyl-residue rich region at the N-terminus is constructed
additional information
mutant enzyme lacking 5 residues at the C-terminus: hydrolytic activity towards carboxymethyl cellulose is 112% of wild-type activity, kcat/Km for p-nitrophenyl cellobiose is 1.2fold higher than wild-type value. Mutant enzyme lacking 5 residues at the C-terminus and 5 residues at the N-terminus: activity towards carboxymethyl cellulose is 111% of wild-type activity, kcat/Km for p-nitrophenyl cellobiose is 1.8fold higher than wild-type value. Thermostability is not significantly influenced
additional information
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mutant enzyme lacking 5 residues at the C-terminus: hydrolytic activity towards carboxymethyl cellulose is 112% of wild-type activity, kcat/Km for p-nitrophenyl cellobiose is 1.2fold higher than wild-type value. Mutant enzyme lacking 5 residues at the C-terminus and 5 residues at the N-terminus: activity towards carboxymethyl cellulose is 111% of wild-type activity, kcat/Km for p-nitrophenyl cellobiose is 1.8fold higher than wild-type value. Thermostability is not significantly influenced
additional information
preparation of a fusion enzyme so that the thermostable chitin-binding domain of chitinase from Pyrococcus furiosus is joined to the C-terminus of EGPh and its variants. The fusion enzymes show stronger activities than the wild-type EGPh toward both carboxymethyl cellulose and crystalline cellulose (Avicel)
additional information
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preparation of a fusion enzyme so that the thermostable chitin-binding domain of chitinase from Pyrococcus furiosus is joined to the C-terminus of EGPh and its variants. The fusion enzymes show stronger activities than the wild-type EGPh toward both carboxymethyl cellulose and crystalline cellulose (Avicel)
additional information
EGPhDELTAC5, truncated form of the enzyme shows similar enzymatic properties to the wild-type protein. EGPhDELTAC10, lacking ten residues at the C-terminus showed significantly decreased activity. Three truncated mutants (EGPhDELTAN5, EGPhDELTAC5 and EGPhDELTAN5C5) which show no change in enzymatic properties are prepared and screened for crystallization
additional information
sequential deletion analyses from both N and C termini, removing 10 amino acids at a time, are carried out to determine whether a shorter enzyme with improved characteristics could becreated. Among the three C-terminal deletions, only the C10 mutant, which misses the last 10 amino acids, maintained activity. In contrast, all N-terminal deletion mutants (N10, N20, and N30) retains activity except N40. Detailed analysis of the aligned sequences reveals that the highly conserved sequence begins at L35, after the 34 N-terminal residues of EGPh. Therefore, a mutant with a deletion betweenN30 and N40 (N34) is prepared and expressed. This mutant retains enzymatic activity like N30, suggesting that the critical residues for enzyme activity start from L35. Each of the active N-terminal deletions is combined with the C10 deletion to establish the minimal sequence required for activity. When enzyme function is tested in the presence of CMC, only the N10C10 mutant exhibits activity, suggesting that the loss of activity may be due to the loss of thermostability. To test this, enzymatic activity assays are performed at 60°C. At this lower temperature, the N20C10, N30C10, and N34C10 mutants all exhibit carboxymethyl cellulase (CMCase) activity, but the N40, C20, and C30 mutants do not. Therefore, the shortest EGPh sequence maintaining hydrolytic activity isN34C10, representing an 11% reduction in amino acid residues. In addition to the decreased optimal temperature of C mutants,N and C combination mutants (except N10C10) are active at 60°C but not at 80°C. At 80°C, the wild type and the N10 mutant are stable, whereas N20, N30, and N34 show gradually decreasing activity. A longer deletion leads to a more severe decrease in activity, and theN34 mutant exhibits the shortest t1/2 of 8 h. Both C10 andN10C10 lose more than 50% activity in less than 2 h at 80°C, suggesting that the decreased activity of C-terminal deletion mutants is due to decreased thermostability
additional information
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sequential deletion analyses from both N and C termini, removing 10 amino acids at a time, are carried out to determine whether a shorter enzyme with improved characteristics could becreated. Among the three C-terminal deletions, only the C10 mutant, which misses the last 10 amino acids, maintained activity. In contrast, all N-terminal deletion mutants (N10, N20, and N30) retains activity except N40. Detailed analysis of the aligned sequences reveals that the highly conserved sequence begins at L35, after the 34 N-terminal residues of EGPh. Therefore, a mutant with a deletion betweenN30 and N40 (N34) is prepared and expressed. This mutant retains enzymatic activity like N30, suggesting that the critical residues for enzyme activity start from L35. Each of the active N-terminal deletions is combined with the C10 deletion to establish the minimal sequence required for activity. When enzyme function is tested in the presence of CMC, only the N10C10 mutant exhibits activity, suggesting that the loss of activity may be due to the loss of thermostability. To test this, enzymatic activity assays are performed at 60°C. At this lower temperature, the N20C10, N30C10, and N34C10 mutants all exhibit carboxymethyl cellulase (CMCase) activity, but the N40, C20, and C30 mutants do not. Therefore, the shortest EGPh sequence maintaining hydrolytic activity isN34C10, representing an 11% reduction in amino acid residues. In addition to the decreased optimal temperature of C mutants,N and C combination mutants (except N10C10) are active at 60°C but not at 80°C. At 80°C, the wild type and the N10 mutant are stable, whereas N20, N30, and N34 show gradually decreasing activity. A longer deletion leads to a more severe decrease in activity, and theN34 mutant exhibits the shortest t1/2 of 8 h. Both C10 andN10C10 lose more than 50% activity in less than 2 h at 80°C, suggesting that the decreased activity of C-terminal deletion mutants is due to decreased thermostability
additional information
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sequential deletion analyses from both N and C termini, removing 10 amino acids at a time, are carried out to determine whether a shorter enzyme with improved characteristics could becreated. Among the three C-terminal deletions, only the C10 mutant, which misses the last 10 amino acids, maintained activity. In contrast, all N-terminal deletion mutants (N10, N20, and N30) retains activity except N40. Detailed analysis of the aligned sequences reveals that the highly conserved sequence begins at L35, after the 34 N-terminal residues of EGPh. Therefore, a mutant with a deletion betweenN30 and N40 (N34) is prepared and expressed. This mutant retains enzymatic activity like N30, suggesting that the critical residues for enzyme activity start from L35. Each of the active N-terminal deletions is combined with the C10 deletion to establish the minimal sequence required for activity. When enzyme function is tested in the presence of CMC, only the N10C10 mutant exhibits activity, suggesting that the loss of activity may be due to the loss of thermostability. To test this, enzymatic activity assays are performed at 60°C. At this lower temperature, the N20C10, N30C10, and N34C10 mutants all exhibit carboxymethyl cellulase (CMCase) activity, but the N40, C20, and C30 mutants do not. Therefore, the shortest EGPh sequence maintaining hydrolytic activity isN34C10, representing an 11% reduction in amino acid residues. In addition to the decreased optimal temperature of C mutants,N and C combination mutants (except N10C10) are active at 60°C but not at 80°C. At 80°C, the wild type and the N10 mutant are stable, whereas N20, N30, and N34 show gradually decreasing activity. A longer deletion leads to a more severe decrease in activity, and theN34 mutant exhibits the shortest t1/2 of 8 h. Both C10 andN10C10 lose more than 50% activity in less than 2 h at 80°C, suggesting that the decreased activity of C-terminal deletion mutants is due to decreased thermostability
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additional information
post-translational modification of the N-terminal glutamine residue to diglutamate via glutaminyl cyclase enhances the stability of Cel7A and variants
additional information
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post-translational modification of the N-terminal glutamine residue to diglutamate via glutaminyl cyclase enhances the stability of Cel7A and variants
additional information
creation of 10 hybrid enzymes of GH5 endoglucanase Egl5A from Talaromyces emersonii (TeEgl5A) with elements of the mesophilic endoglucanase Cel5 from Stegonsporium opalus (SoCel5). Five of the expressed hybrid enzymes exhibit enzyme activity. Two of these hybrids exhibit pronounced increases in the temperature optimum (10 and 20°C), the temperature T50 at which the protein loses 50% of its activity (15 and 19°C), and the melting temperature Tm (16.5 and 22.9°C) and extended half-lives (240fold and 650fold at 55°C) relative to the values for the mesophilic parent enzyme. The mutants demonstrate improved catalytic efficiency on selected substrates. Method validation, molecular dynamics simulations of both the SoCel5 and TeEgl5A parent enzymes, overview. Improved hydrophobic packing of the interface between alpha2 and alpha3 is the primary mechanism by which the hybrid enzymes increase their thermostability relative to that of the mesophilic parent SoCel5. Comparison of structures and molecular masses of the SoCel5-TeEgl5A hybrid enzymes. Mechanism of improved thermostability
additional information
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creation of 10 hybrid enzymes of GH5 endoglucanase Egl5A from Talaromyces emersonii (TeEgl5A) with elements of the mesophilic endoglucanase Cel5 from Stegonsporium opalus (SoCel5). Five of the expressed hybrid enzymes exhibit enzyme activity. Two of these hybrids exhibit pronounced increases in the temperature optimum (10 and 20°C), the temperature T50 at which the protein loses 50% of its activity (15 and 19°C), and the melting temperature Tm (16.5 and 22.9°C) and extended half-lives (240fold and 650fold at 55°C) relative to the values for the mesophilic parent enzyme. The mutants demonstrate improved catalytic efficiency on selected substrates. Method validation, molecular dynamics simulations of both the SoCel5 and TeEgl5A parent enzymes, overview. Improved hydrophobic packing of the interface between alpha2 and alpha3 is the primary mechanism by which the hybrid enzymes increase their thermostability relative to that of the mesophilic parent SoCel5. Comparison of structures and molecular masses of the SoCel5-TeEgl5A hybrid enzymes. Mechanism of improved thermostability
additional information
symbiotic phenotype of an ANU843 celC2 knockout mutant derivative strain ANU843DELTAcelC2
additional information
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symbiotic phenotype of an ANU843 celC2 knockout mutant derivative strain ANU843DELTAcelC2
additional information
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symbiotic phenotype of an ANU843 celC2 knockout mutant derivative strain ANU843DELTAcelC2
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additional information
after bioinformatic analysis hybrid proteins based on beta-endoglucanase from Sulfolobus solfataricus P2 and beta-endoglucanase from Thermotoga maritima are constructed which should successfully combine the advantageous properties of both cellulases, i.e. recombinant expression in Escherichia coli, acidophily and thermophily. both hybrids are expressed insoluble in Escherichia coli, but one hybrid enzyme was successfully refolded from washed inclusion bodies
additional information
targeted construction of chimeric enzymes of cellulase from Sulfolobus solfataricus P2 and cellulase CelA from Thermotoga maritima. The fusion protein SSO1949-CelA-SSO1949 consists of 193 amino acids SSO1949 followed by 76 amino acids CelA and 39 amino acids SSO1949. The catalytic center with the two catalytic glutamate residues is derived from SSO1949 whereas the reducing end of the substrate binding cleft comes from CelA. The fusion protein CelA-SSO1949-CelA consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA. Most of the active center is derived from SSO1949
additional information
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after bioinformatic analysis hybrid proteins based on beta-endoglucanase from Sulfolobus solfataricus P2 and beta-endoglucanase from Thermotoga maritima are constructed which should successfully combine the advantageous properties of both cellulases, i.e. recombinant expression in Escherichia coli, acidophily and thermophily. both hybrids are expressed insoluble in Escherichia coli, but one hybrid enzyme was successfully refolded from washed inclusion bodies
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additional information
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targeted construction of chimeric enzymes of cellulase from Sulfolobus solfataricus P2 and cellulase CelA from Thermotoga maritima. The fusion protein SSO1949-CelA-SSO1949 consists of 193 amino acids SSO1949 followed by 76 amino acids CelA and 39 amino acids SSO1949. The catalytic center with the two catalytic glutamate residues is derived from SSO1949 whereas the reducing end of the substrate binding cleft comes from CelA. The fusion protein CelA-SSO1949-CelA consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA. Most of the active center is derived from SSO1949
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additional information
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post-transcriptional silencing of cel7 and cel9C1 with effects on nematode growth and development
additional information
creation of 10 hybrid enzymes of GH5 endoglucanase Egl5A from Talaromyces emersonii (TeEgl5A) with elements of the mesophilic endoglucanase Cel5 from Stegonsporium opalus (SoCel5). Five of the expressed hybrid enzymes exhibit enzyme activity. Two of these hybrids exhibit pronounced increases in the temperature optimum (10 and 20°C), the temperature T50 at which the protein loses 50% of its activity (15 and 19°C), and the melting temperature Tm (16.5 and 22.9°C) and extended half-lives (240fold and 650fold at 55°C) relative to the values for the mesophilic parent enzyme. The mutants demonstrate improved catalytic efficiency on selected substrates. Method validation, molecular dynamics simulations of both the SoCel5 and TeEgl5A parent enzymes, overview. Improved hydrophobic packing of the interface between alpha2 and alpha3 is the primary mechanism by which the hybrid enzymes increase their thermostability relative to that of the mesophilic parent SoCel5. Comparison of structures and molecular masses of the SoCel5-TeEgl5A hybrid enzymes. Mechanism of improved thermostability
additional information
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creation of 10 hybrid enzymes of GH5 endoglucanase Egl5A from Talaromyces emersonii (TeEgl5A) with elements of the mesophilic endoglucanase Cel5 from Stegonsporium opalus (SoCel5). Five of the expressed hybrid enzymes exhibit enzyme activity. Two of these hybrids exhibit pronounced increases in the temperature optimum (10 and 20°C), the temperature T50 at which the protein loses 50% of its activity (15 and 19°C), and the melting temperature Tm (16.5 and 22.9°C) and extended half-lives (240fold and 650fold at 55°C) relative to the values for the mesophilic parent enzyme. The mutants demonstrate improved catalytic efficiency on selected substrates. Method validation, molecular dynamics simulations of both the SoCel5 and TeEgl5A parent enzymes, overview. Improved hydrophobic packing of the interface between alpha2 and alpha3 is the primary mechanism by which the hybrid enzymes increase their thermostability relative to that of the mesophilic parent SoCel5. Comparison of structures and molecular masses of the SoCel5-TeEgl5A hybrid enzymes. Mechanism of improved thermostability
additional information
development of biocatalysts for enhanced hydrolysis of (hemi)cellulose into monosaccharides with random diversity by directed evolution of the gene coding for bacterial endo-beta-1,4-glucanase from Streptomyces sp. G12, improved catalysis of lignocellulose conversion, screening of a library of 10000 random mutants, detection of variants with higher activity than the wild-type enzyme, and structure-function relationships of the mutants, overview. Mutations T67N, D142E, T157I, and S218N are located in the catalytic module and mutations G251D, V259D, V242D, and D330E in the carbohydrate binding module (CBM)
additional information
molecular dynamics simulations reveal that the introduced disulfide bond rigidified a global structure of DSB2 and DSB3 mutant variants, thus enhancing their thermostability
additional information
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molecular dynamics simulations reveal that the introduced disulfide bond rigidified a global structure of DSB2 and DSB3 mutant variants, thus enhancing their thermostability
additional information
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molecular dynamics simulations reveal that the introduced disulfide bond rigidified a global structure of DSB2 and DSB3 mutant variants, thus enhancing their thermostability
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additional information
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molecular dynamics simulations reveal that the introduced disulfide bond rigidified a global structure of DSB2 and DSB3 mutant variants, thus enhancing their thermostability
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additional information
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molecular dynamics simulations reveal that the introduced disulfide bond rigidified a global structure of DSB2 and DSB3 mutant variants, thus enhancing their thermostability
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additional information
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molecular dynamics simulations reveal that the introduced disulfide bond rigidified a global structure of DSB2 and DSB3 mutant variants, thus enhancing their thermostability
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additional information
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molecular dynamics simulations reveal that the introduced disulfide bond rigidified a global structure of DSB2 and DSB3 mutant variants, thus enhancing their thermostability
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additional information
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
additional information
the FnIII-like domain is deleted from Cel19A-90, reducing activity with bacterial microcrystalline cellulose to 43% of the wild-type
additional information
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the FnIII-like domain is deleted from Cel19A-90, reducing activity with bacterial microcrystalline cellulose to 43% of the wild-type
additional information
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the FnIII-like domain is deleted from Cel19A-90, reducing activity with bacterial microcrystalline cellulose to 43% of the wild-type
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additional information
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exo-endo-1,4-beta-glucanase fusion protein
additional information
targeted construction of chimeric enzymes of cellulase from Sulfolobus solfataricus P2 and cellulase CelA from Thermotoga maritima. The fusion protein SSO1949-CelA-SSO1949 consists of 193 amino acids SSO1949 followed by 76 amino acids CelA and 39 amino acids SSO1949. The catalytic center with the two catalytic glutamate residues is derived from SSO1949 whereas the reducing end of the substrate binding cleft comes from CelA. The fusion protein CelA-SSO1949-CelA consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA. Most of the active center is derived from SSO1949
additional information
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targeted construction of chimeric enzymes of cellulase from Sulfolobus solfataricus P2 and cellulase CelA from Thermotoga maritima. The fusion protein SSO1949-CelA-SSO1949 consists of 193 amino acids SSO1949 followed by 76 amino acids CelA and 39 amino acids SSO1949. The catalytic center with the two catalytic glutamate residues is derived from SSO1949 whereas the reducing end of the substrate binding cleft comes from CelA. The fusion protein CelA-SSO1949-CelA consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA. Most of the active center is derived from SSO1949
additional information
engineering of mutants of isoform Cel5A with higher activity on 1-ethyl-3-methylimidazolium acetate pretreated biomass by screening of a random mutagenesis library. Twelve mutants with 2542% improvement in specific activity on carboxymethyl cellulose and up to 30% improvement on ionic-liquid pretreated switchgrass could be isolated and characterized. Mmost of the mutations in the improved variants are located distally to the active site on the protein surface and are not directly involved with substrate binding
additional information
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engineering of mutants of isoform Cel5A with higher activity on 1-ethyl-3-methylimidazolium acetate pretreated biomass by screening of a random mutagenesis library. Twelve mutants with 2542% improvement in specific activity on carboxymethyl cellulose and up to 30% improvement on ionic-liquid pretreated switchgrass could be isolated and characterized. Mmost of the mutations in the improved variants are located distally to the active site on the protein surface and are not directly involved with substrate binding
additional information
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engineering of mutants of isoform Cel5A with higher activity on 1-ethyl-3-methylimidazolium acetate pretreated biomass by screening of a random mutagenesis library. Twelve mutants with 2542% improvement in specific activity on carboxymethyl cellulose and up to 30% improvement on ionic-liquid pretreated switchgrass could be isolated and characterized. Mmost of the mutations in the improved variants are located distally to the active site on the protein surface and are not directly involved with substrate binding
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additional information
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endoglucanase IV is reconstructed by fusing EGIV with an additional catalytic module (EGIVCM). The genes eg4 and eg4-cm are expressed in recombinant Pichia strains (Pichia pastoris EGIV1 and Pichia pastoris EGIV-CM1). The activities towards carboxymethyl cellulose of cultivation supernatant of Pichia pastoris EGIV1 and Pichia pastoris EGIV-CM1 are 2.4 U/ml and 4.3 U/ml, respectively. Modification of the EGIV structure with an additional catalytic module improves the specific activity about 4fold
additional information
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construction of disruption mutants of genes cbh1 and cbh2, encoding the 1,4-beta-D-glucan cellobiohydrolases, does not affect egl1 and egl3 expression, overview
additional information
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enzyme immobilization, e.g. by cross-linking with glutaraldehyde, enzyme activity and method evaluation
additional information
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usage of gene egl3 promoter for expression of gene bgl1, encoding a beta-glucosidase, in Trichoderma reesei, the mutant strain shows 4fold increased beta-glucosidase activity compared to the wild-type enzyme
additional information
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fusion of the cellulose binding domain of cellobiohydrolase I from Trichoderma reesei to the C-terminus of Cryptococcus sp. carboxymethyl cellulase and expression in a recombinant expression system of Cryptococcus sp. S-2. The recombinant fusion enzymes display optimal pH similar to those of the native enzyme. Compared with Cryptococcus sp. carboxymethyl cellulase, the recombinant fusion enzymes have acquired an increased binding affinity to insoluble cellulose, and the cellulolytic activity toward insoluble cellulosic substrates, SIGMACELL and Avicel, is higher than that of native enzyme, confirming the presence of cellulose binding domains improve the binding and the cellulolytic activity of carboxymethyl cellulase on insoluble substrates
additional information
elimination of all of the glycosylation sites induces expression of the unfolded protein response target genes, and secretion of this CBH1 variant is severely compromised in a calnexin gene deletion strain. The thermal reactivity of CBH1 is significantly decreased by removal of either Asn45 or Asn384 glycosylation site during the catalyzed hydrolysis of soluble substrate. Combinatorial loss of these two N-linked glycans further exacerbates the temperature-dependent inactivation. Removal of N-glycosylation at Asn384 has a more pronounced effect on the integrity of regular secondary structure compared to the loss of Asn45 or Asn270
additional information
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elimination of all of the glycosylation sites induces expression of the unfolded protein response target genes, and secretion of this CBH1 variant is severely compromised in a calnexin gene deletion strain. The thermal reactivity of CBH1 is significantly decreased by removal of either Asn45 or Asn384 glycosylation site during the catalyzed hydrolysis of soluble substrate. Combinatorial loss of these two N-linked glycans further exacerbates the temperature-dependent inactivation. Removal of N-glycosylation at Asn384 has a more pronounced effect on the integrity of regular secondary structure compared to the loss of Asn45 or Asn270
additional information
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usage of gene egl3 promoter for expression of gene bgl1, encoding a beta-glucosidase, in Trichoderma reesei, the mutant strain shows 4fold increased beta-glucosidase activity compared to the wild-type enzyme
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additional information
a mutant lacking the immunoglobulin-like domain shows 1% of wild-type activity and a decrease in the temperature of the midpoint of the thermal denaturation transition by 6.3°C
additional information
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construction of mutant mgCel6ADELTACBM lacking the carbohydrate binding module 2 (CBM2)
additional information
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endoglucanase 1 (EG1) and its catalytic module (EG1-CM) exhibit very similar specific activities towards the soluble substrates carboxymethyl cellulose, lichenan and mannan, and insoluble H3PO4 acid-swollen cellulose, whereas the specific activities of EG1-CM towards the insoluble substrates alpha-cellulose, Avicel and filter paper are approximately 58%, 43% and 38%, respectively compared to EG1
additional information
the enzyme consists of an N-terminal signal peptide, two glycosyl hydrolase family 5 catalytic modules, two novel carbohydrate-binding modules, two linker sequences, and a C-terminal sequence with an unknown function. Removal of the carbohydrate-binding modules from rCel5A reduces the catalytic activities with various polysaccharides remarkably
additional information
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the enzyme consists of an N-terminal signal peptide, two glycosyl hydrolase family 5 catalytic modules, two novel carbohydrate-binding modules, two linker sequences, and a C-terminal sequence with an unknown function. Removal of the carbohydrate-binding modules from rCel5A reduces the catalytic activities with various polysaccharides remarkably
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10 - 70
-
purified native enzyme, highly stable in the temperature range of 10-40°C, the activity declines rapidly as the temperature increases above 60°C, 12% activity remains at 70°C after 4 h. At 10°C, the enzyme exhibits no loss of activity, even after 24 h
101
melting-temperature of the mutant enzymes P74C/C106S, P74C and C106S
103
wild type enzyme is thermally unfolded at 103.4°C
110
maximal activity at 95°C and retains 49% activity at 110°C
112
denaturing temperature
115
purified recombinant His-tagged enzyme, pH 6.0, half-life is 9.1 min
20 - 30
-
pH 8.0, 20 h, about 60%% loss of activity
25 - 55
-
purified recombinant enzyme, very stable at 25°C, loss of about 13.2% activity at 35°C after 2 h. The enzyme retains 10.4% activity at 45°C after 2 h, and is completely inactivated at 55°C after 30 min
27 - 30
-
purified enzyme, 60 min, completely stable
30
10 min, wild-type stable up to 30°C
30 - 50
-
150 h, 15% loss of activity
30 - 70
-
30 min to 2 h, stable
36
-
30 min, 50% loss of activity of cellulase 4.8, 25% loss of activity of cellulase 4.5
39 - 60
-
the purified enzyme is stable at 39-60°C and pH 4.0-6.0 for 60 min
4 - 45
the enzyme has an estimated low melting temperature of 45°C, about 50% activity remaining at 4°C, it is identified to be cold-adapted
43.9
melting temperature, mutant K94R/S365P
47
-
enzyme is stable up to 47°C and exhibits half-life of 138.6 min
47.3
melting temperature, mutant K94R
48.9
melting temperature, wild-type
49.1
melting temperature, mutant S365P
50 - 70
-
purified native enzyme, pH 5.0, the enzyme retains more than 50% activity after incubation at 65°C and 70°C for 180 min, no major loss in activity at 50°C
53.6
Tm of the recombinant deglycosylated wild-type enzyme
54.6
wild-type catalytic domain, melting temperature
63.7
N-glycosylation mutant residue D384, melting temperature
65.79
N-glycosylation mutant residue D45, melting temperature
65.94
wild-type, melting temperature
65.99
N-glycosylation mutant residue D270, melting temperature
66
-
melting temperature of enzyme GtGH45
68
-
melting temperature of mutant enzyme CtGH5-F194A
74.5
melting temperature, deglycosylated wild-type
76
-
Tm of enzyme MgCel6A
78.1
Tm of the recombinant deglycosylated wild-type enzyme
78.5
melting temperature, mutant N54C/P191C
80.9
-
melting temperature of enzyme MtGH45
81.4
denaturation temperature
84
melting temperature, mutant G4C/A72C/N54C/P191C/T243C/A375C
87
T1/2 of the recombinant deglycosylated wild-type enzyme
95 - 96
Tm-value for mutant enzymes C106A/C159A/C372A/C412A, C106A/C159A and C372A/C412A
100
half-life 40 min
100
-
enzyme is rapidly inactivated by boiling
100
60 min, 35% residual activity
100
Tm-value for wild-type enzyme
100
-
10 min, 70-80% loss of activity
100
-
5 min, 5% residual activity
100
-
5 min, aqueous buffer, 5% residual activity
100
5 min, 75% residual activity
100
5 min, aqueous buffer, 75% residual activity
100
-
10 min, 60% loss of activity
100
-
10 min, cellulase II-A retains 27% of the original activity, cellulase II-B retains 41% of the original activity
100
purified recombinant His-tagged enzyme, pH 6.0, half-life is 46 min
37
-
3 h, stable
37
-
purified enzyme, loss of 60% activity after 60 min
40
-
pH 8.0, 20 h, about 40% loss of activity
40
purified recombinant enzyme, completely stable to slightly activated after 48 h
40
-
10 min, stable up to
40
-
10 min, stable up to
40
-
1 h, about 15% loss of activity
40
-
purified enzyme, inactivation after 60 min
40
-
30 min, stable up to
40
-
stable up to 11 days
45
-
stable
45
-
2 h, cellulase II-B is stable over the pH-range 4.5-6.0, cellulase II-A is unstable, except at pH 5.5-6.0
50
-
purified recombinant mutant CtLic26A-Cel5, maximally stable
50
-
24 h, more than 90% loss of activity, endo-beta-1,4-glucanase EG45
50
-
half life for carboxymethylcellulase, filter paper cellulase, and beta-glucosidase is approximately 240 h
50
-
pH 8.0, 20 h, about 10% loss of activity
50
purified recombinant enzyme, 80% activity remaining after 48 h
50
-
10 min, 90% of the original activity is retained
50
-
60 min, about 20% loss of activity
50
-
CMCase, 1 day, no loss of activity, 46% activity remaning after 26 days, inactivation after 40 days
50
1 h, 70% residual activity
50
-
30 min, denatured at 50°C and above
50
-
carboxymethycellulase and avicelase activity, stable for 24 h
50
-
10 min, about 50% loss of activity
50
-
1 h, 50% loss of activity
50
-
purified enzyme, inactivation after 40 min
50
-
10 min, about 10% loss of activity
50
1 h, 80% residual activity
50
MG570051
half-life 59 min
50
-
30 min, CMCase I, stable below
50
-
1 h, more than 80% of the initial activity is retained
50
-
8% loss of activity after 3 days
50
t1/2: 173 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
50
t1/2: 693 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
50
15 h, wild-type enzyme and mutant enzymes Y206F, D58A and Y318A are stable, mutant enzyme D58N loses about 20% of its inital activity
50
Thermochaetoides thermophila
-
stable
50
-
48 h, 88% and 98% residual activity on filter paper and carboxymethyl cellulose, respectively
50
-
half-life of free enzyme is 3.0 h, half-life of the enzyme immobilized in calcium-alginate beads is 4.6 h
50
-
30 min, less than 10% loss of activity
50 - 60
melting temperature
50 - 60
-
CMCase, 100% activity after 1 day, 80% activity remaining after 40 days
54
-
Tm: 54.1°C
55
-
inactivation
55
Bacillus cellulyticus K-12
-
48 h, stable
55
Bacillus cellulyticus K-12
-
22% loss of activity after 72 h
55
-
30 min, stable up to
55
-
10 min, complete inactivation
55
-
pH 7.5, 15 min, stable up to
55
-
10 min, about 30% loss of activity with barley beta-glucan and about 60% loss of activity with carboxymethylcellulose
55
-
5 min, loss of activity
55
-
10 h, about 20% loss of activity
55
-
10 min, 80% loss of activity
57
-
Tm-value
57
T1/2 of the recombinant deglycosylated wild-type enzyme
60
-
enzyme form EGA, stable up to
60
-
48h, 50% loss of activity
60
10 min, mutant lacking the IgG-like domain stable up to 60°C
60
-
24 h, 15% loss of activity, endo-beta-1,4-glucanase EG27
60
stable for at least 10 min
60
-
pH 4.0, extremely sensitive above
60
-
10 min, completely stable below
60
-
pH 8.0, 20 h, about 15% loss of activity
60
purified recombinant enzyme, 50% activity remaining after 3 h, 20% after 6 h, and inactivation after 12 h
60
-
10 min, complete inactivation
60
-
60 min, more than 60% of the initial activity remains
60
-
CMCase, 97% activity remaining after 1 day, below 5% activity remaining after 40 days
60
30 min, complete loss of activity in absence of NaCl, no loss in presence of 2.5 M NaCl
60
-
4 h, 40% residual activity
60
-
30 min , 50% residual activity
60
purified recombinant enzyme, 60 min, stable
60
-
5 min, complete loss of activity
60
30 min, 90% loss of activity
60
8 h, no loss of activity
60
-
30% loss of activity overnight
60
purified recombinant enzyme, half-life is 48 h
60
-
120 min, little loss of activity
60
-
30 min, stable up to
60
-
10 min, about 50% loss of activity with barley beta-glucan and about 75% loss of activity with carboxymethylcellulose
60
10 min, 42% residual activity
60
-
10 min, complete inactivation of cellulase A, B and C
60
-
pH 5.0, 30 min, CMCase I, 50% loss of activity
60
-
30 min, more than 50% loss of activity of the catalytic domain and of the whole enzyme
60
t1/2: 16 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
60
t1/2: 347 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
60
15 h, wild-type enzyme is stable, mutant enzyme D58A loses about 20% of initial activity, mutant enzymes Y206F, D58N, D58N and Y318A lose about 10% of the inital activity
60
Thermochaetoides thermophila
-
1 h, stable
60
Thermochaetoides thermophila
-
15 min, no loss of activity
60
Thermochaetoides thermophila
-
t1/2: 18 min (without substrate), carboxymethyl cellulose partially protects the enzyme from heat inactivation
60
Thermochaetoides thermophila
1 h, stabel
60
Thermochaetoides thermophila
120 min, enzyme retains about 85% of its initial activity, xylanase ativity
60
Thermochaetoides thermophila
120 min, enzyme retains more than 80% of its initial activity, endoglucanase activity
60
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, 90% activity remaining after 120 min
60
-
48 h, 50% residual activity
60
-
half-life more than 96 h
60
-
thermal inactivation above
60
-
half-life of free enzyme is 1.2 h, half-life of the enzyme immobilized in calcium-alginate beads is 5.4 h
60
-
total loss of activity in less than 3 h
60 - 70
purified recombinant His-tagged enzyme, half-life of enzyme is 168 h at 60°C and 3 h at 70°C, respectively
60 - 70
recombinant enzyme NMgh45, completely stable for 2 h
65
-
denaturation above
65
-
enzyme form EGC, stable up to
65
-
1 h, 90% residual activity
65
2 h, extracellular enzyme, 90% activity remaining
65
-
avicelase activity, stable for 5 min
65
-
completely stable up to 65°C
65
15 h, wild-type enzyme loses about 10% of initial activity, mutant enzyme D58N and Y206F loses about 20% of maximal activity, mutant enzyme D58A loses about 90% of initial activity, mutant enzyme Y318A loses about 30% of initial activity
65
-
1 h, 90% residual activity
65
-
6 h, 80% residual activity
70
-
denaturation above
70
72 h, presence of 0.1% Tween 20, no loss of activity
70
-
10 min, 50% loss of activity
70
-
2 h, 30% loss of activity
70
20 min, loss of activity
70
-
10 min, 20% loss of activity
70
-
pH 8.0, 20 h, about 20% loss of activity
70
Bacillus cellulyticus K-12
-
30 min, 80% loss of activity
70
-
60 min, about 60% loss of activity
70
-
CMCase, 78% activity remaining after 1 day
70
purified enzyme, 48% activity remaining after 5 min, 30% after 60 min
70
2 h, 50% residual activtiy
70
-
3 h, 83% residual activity
70
-
CMCase, 89% activity after 1 day, complete loss of activity after 20 days
70
-
carboxymethylcellulase activity, 5 min, 95% residual activity
70
-
10 min, almost complete inactivation
70
-
30 min, 10% loss of activity
70
CBH6A and EgGH45, 90% activity for 10 min
70
1 h, almost all activity remaining
70
-
pH 5.0, 30 min, CMCase I, complete inactivation
70
10 min, less than 20% activity remaining
70
2 h, the wild-type enzyme retains 38% activity, the enzyme mutants retain 52% and 58% activity, respectively
70
t1/2: 15 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
70
t1/2: 231 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
70
wild-type enzyme loses about 50% of initial activity, mutant enzyme D58A loses about 20% of initial activity, mutant enymes D58A, Y206F and Y318A nearly completely lose activity
70
Thermochaetoides thermophila
-
half-life: 45 min
70
Thermochaetoides thermophila
-
half-life 45 min
70
Thermochaetoides thermophila
1 h, 79% residual activtiy
70
Thermochaetoides thermophila
60 min, enzyme retains 66.2% of its initial activity, xylanase ativity
70
Thermochaetoides thermophila
60 min, enzyme retains 74.3% of its initial activity, endoglucanase activity
70
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, 74.3% remaining after 60 min, half-life of endoxylanase activity is 110 min, 30% activity remaining after 120 min
70
-
4 h, 50% residual activity
75
-
about 20% loss of activity after 30 min, about 50% loss of activity after 2 h, 51000 Da subunit from the multicomponent cellulase complexes
75
72 h, presence of 0.1% Tween 20, 75% of initial activity
75
-
denaturation, presence of tris-(2-hydroxyethyl)-methylammonium methylsulfate
75
CelDR retains 70% of its maximum activity at 75°C after incubation for 30 min
75
-
avicelase activity, 20% residual activity
75
-
pH 5, half-life: 2-4 h
75
melting temperature, wild-type
75
-
half-life: endocellulases I (104 min), endocellulases II (93 min), endocellulases III (75 min), endocellulases IV (66 min)
75
purified recombinant enzyme, completely stable for 1 h, and 98% activity remaining after 2 h
75
-
less than 10% of the cellulolytic ativities remain after 1 h
75
purified recombinant His-tagged enzyme, pH 6.0, completely stable for 48 h
79
-
melting temperature of wild-type enzyme CtGH5
79
wild-type, 10 min, 50% loss of activity
79
wild-type, 10 min, 50% loss of activity
79
melting temperature, mutant T243C/A375C
80
-
15 min, 10% loss of activity
80
-
10 min, complete inactivation
80
-
pH 8.0, 20 h, about 40% loss of activity
80
-
40 min, about 80% loss of activity
80
-
CMCase, 10% activity remaining after 1 day
80
-
M44-11 mutant shows higher stability than others and retains more than 50% of its activity after incubation at 80°C for 1 h
80
-
30 min, 29% residual activity
80
purified recombinant His-tagged enzyme, at least 91.4% activity remains after 1 h
80
-
30 min, 50% loss of activity
80
-
CMCase, complete loss of activity after 21 days
80
-
24 h incubation, enzyme retains more than 60% activity
80
-
10 min, complete inactivation
80
60 min, 70% residual activity
80
-
30 min, 80% loss of activity
80
CBH6A and EgGH45, 80% activity for 10 min
80
10 min, 21% residual activity
80
1 h, 50% residual activity
80
melting temperature, mutant G4C/A72C
80
purified recombinant enzyme, completely stable for 1 h, and 90% activity remaining after 2 h
80
half-life: 8 h at pH 1.8, 160 min at pH 1. At neutral pH, the thermal inactivation rate is nearly two orders of magnitude higher than at pH 1.8
80
1 h, enzyme retains more than 50% of its activity
80
2 h, the wild-type enzyme retains no activity, the enzyme mutants retain 15% and 22% activity, respectively
80
t1/2: 12 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
80
t1/2: 63 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
80
Thermochaetoides thermophila
-
half-life: 24 min
80
Thermochaetoides thermophila
-
15 min, 71% residual activity
80
Thermochaetoides thermophila
-
half-life 24 min
80
Thermochaetoides thermophila
1 h, 66% residual activity
80
Thermochaetoides thermophila
60 min, enzyme retains 61.3% of its initial activity, endoglucanase activity
80
Thermochaetoides thermophila
60 min, enzyme retains about 50% of its initial activity, xylanase ativity
80
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, 61.3% activity remaining after 60 min, half-life of endoxylanase activity is 80 min, 18% activity remaining after 120 min
80
2.5 h, 80% residual activity
80
8 h, 80% residual activity, mutant E225H-K207G
80
8 h, 90% residual activity, mutant E225H-K207G-D37V
80
-
presence of 96%, plus 0.1% H2SO4, half-life 4.5 min
80
presence of 96%glycerol, plus 0.1% H2SO4, half-life 4.5 min
80
-
60 min, 70% of maximum activity
80
recombinant enzyme NMgh45, 90% activity remains after 2 h
83
chimeric construct C10, 10 min, 50% loss of activity
83
chimeric construct C10, 10 min, 50% loss of activity
85
purified recombinant enzyme, completely stable for 1 h, and 84% activity remaining after 2 h
85
half-life 8 h, both wild-type and mutant Y61G
90
-
half-life: 4 h
90
-
enzyme is able to sustain 50% of its activity when heated at 90°C for 5 h
90
-
20 min, about 90% loss of acfivity
90
enzyme retains approximately 50% of its maximum activity after incubating at 90°C for 1 h
90
-
24 h incubation, complete loss of activity
90
CBH6A and EgGH45, 47% activity for 10 min
90
pH 4.5, 100 min, 50% loss of activity
90
pH 4.5, 100 min, 50% residual activity
90
t1/2: 12 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
90
t1/2: 20 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
90
Thermochaetoides thermophila
-
half-life: 7 min
90
Thermochaetoides thermophila
-
half-life 7 min
90
Thermochaetoides thermophila
40 min, enzyme retains about 28% of its initial activity, endoglucanase activity
90
Thermochaetoides thermophila
60 min, enzyme retains about 30% of its initial activity, xylanase ativity
90
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, half-life of endoxylanase activity is 30 min, 20% activity remaining after 60 min, after 120 min
90
-
5 min, 87% residiual activity
90
-
5 min, aqueous buffer, 87% residual activity, acidified (0.1% (w/w) H2SO4) glycerol, 35% residual activity, acidified ethylene glycol, 36% residual activity
90
5 min, 87% residiual activity
90
5 min, aqueous buffer, 87% residual activity, acidified (0.1% (w/w) H2SO4) glycerol or glycerol, 80% residual activity, acidified ethylene glycol, 36% residual activity
90
recombinant enzyme NMgh45, 68% activity remains after 1 h, 40% after 2 h
90 - 100
-
CMCase, 60 min, complete inactivation
90 - 100
-
CMCase, 60 min, complete inactivation
95
-
5 min, inactivation
95
-
carboxymethylcellulase activity, 5 min, 45% residual activity
95
pH 1.8, rapid inactivation
95
half-life 40 min, both wild-type and mutant Y61G
97
3 h, 20% loss of activity
additional information
-
MgCl2 slightly enhances thermal stability
additional information
enzyme melting transition occurs at 72°C in presence of EDTA, Ca2+ does not affect the melting temperature
additional information
-
enzyme melting transition occurs at 72°C in presence of EDTA, Ca2+ does not affect the melting temperature
additional information
-
more stable to heat treatment at pH 8.0 than at pH 4.0
additional information
high thermostability (Topt: 79.8°C, half-life 48 h)
additional information
-
high thermostability (Topt: 79.8°C, half-life 48 h)
additional information
-
slight activation of cellulase B after 10 min at 40°C
additional information
-
free enzyme shows an activity of 75% of the initial activity after 30 min, and even an activity of 40% remained after 6 h, both measured at 70°C
additional information
hyperthermostable
additional information
the N-terminalbeta-sheet is critical for enzyme thermostability
additional information
-
the N-terminalbeta-sheet is critical for enzyme thermostability
additional information
mechanism of improved thermostability of hybrid mutant enzymes compared to parent wild-type enzymes
additional information
-
mechanism of improved thermostability of hybrid mutant enzymes compared to parent wild-type enzymes
additional information
mechanism of improved thermostability of hybrid mutant enzymes compared to parent wild-type enzymes
additional information
-
mechanism of improved thermostability of hybrid mutant enzymes compared to parent wild-type enzymes
additional information
-
low pH is the major factor that limits endoglucanase stability in glycerol or ethylene glycol at elevated temperatures
additional information
low pH is the major factor that limits endoglucanase stability in glycerol or ethylene glycol at elevated temperatures
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diagnostics
-
labeled Trichoderma reesei cellulase is useful as a marker for Acanthamoeba cyst wall cellulose in infected tissues
textile industry
-
enzymatic deinking experiments, the ink removal rate in samples treated with the catalytic module is only slightly higher (about 8%), than that of untreated controls, whereas that of the EG1-treated samples is 100% higher. Bio-stoning of denim with EG1-CM results in increases of 48% and 40% in weight loss and indigo dye removal, respectively compared with untreated controls. These increases are considerably lower than the corresponding values of 219% and 133% obtained when samples are treated with EG1
agriculture
in the treatment of agricultural waste at high temperature and low pH. Utilization in the biofuel industry after thermal pre-treatment in an acidic environment (e.g., steam explosion) of corncob, sugarcane bagasse and several types of agricultural waste to hydrolyze them down to fermentable sugars
agriculture
-
in the treatment of agricultural waste at high temperature and low pH. Utilization in the biofuel industry after thermal pre-treatment in an acidic environment (e.g., steam explosion) of corncob, sugarcane bagasse and several types of agricultural waste to hydrolyze them down to fermentable sugars
-
analysis
endo-beta-1,4-D-glucanase can be used as a marker to study root development in Arabidopsis
analysis
-
labeled Trichoderma reesei cellulase is useful as a marker for Acanthamoeba cyst wall cellulose in infected tissues
analysis
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. Hydrolysis by exo-acting enzymes such as beta-glucosidase and exo-beta-glucanase is prevented by the presence of the benzylidene group on the non-reducing end D-glucosyl residue. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture. The reaction is terminated and colour developed by the addition of a weak alkaline solution. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation
analysis
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. Hydrolysis by exo-acting enzymes such as beta-glucosidase and exo-beta-glucanase is prevented by the presence of the benzylidene group on the non-reducing end D-glucosyl residue. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture. The reaction is terminated and colour developed by the addition of a weak alkaline solution. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation
analysis
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. Hydrolysis by exo-acting enzymes such as beta-glucosidase and exo-beta-glucanase is prevented by the presence of the benzylidene group on the non-reducing end D-glucosyl residue. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture. The reaction is terminated and colour developed by the addition of a weak alkaline solution. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation
analysis
-
method for zymographic detection of specific cellulases in a complex (endocellulase, exocellulase, and cellobiase) from crude fermentation extracts, after a single electrophoretic separation. Cellulases are printed onto a membrane and, subsequently, substrate gel. Cellobiase isoforms are detected on the membrane using esculine as substrate, endocellulase isoforms on substrate gel with copolymerized carboxymethyl cellulose, while exocellulase isoforms are detected in electrophoresis gel with 4-methylumbelliferyl-beta-D-cellobioside
analysis
-
polymerization-based assay for determining the potency of cellulolytic enzyme formulations on pretreated biomass substrates by monitoring the autofluorescence of cellulose. The one-pot method is label-free, rapid, highly sensitive, and requires only a single pipetting step. Using model enzyme formulations derived from Trichoderma reesei, Trichoderma longibrachiatum, Talaromyces emersonii and recombinant bacterial minicellulosomes from Clostridium thermocellum, enzyme performance based on differences in thermostability, cellulose-binding domain targeting, and endo/exoglucanase synergy can be differentiated
analysis
-
screening for thermostable cellulase using 2% carboxymethyl cellulose and congo red as an indicator at temperatures 0°C, 37°C, 45°C and 50°C,respectively. Eight isolates were selected for further screening and show the abilities to secrete cellulases by forming distinct halo zones on selective agar plate. The maximum halo zones ranging from 32 mm to 35 mm are obtained after 72 hours incubation at 50°C
analysis
-
construction of a pipeline based on Leishmania tarentolae cell-free system to characterize 30 putative thermostable endo-1,4-beta-glucanases and xylanases identified in public genomic databases. The system uses high-throughput assays for glucanase and xylanase activities that rely on solubilisation of labelled particulate substrates performed in multiwell plates
analysis
-
construction of a pipeline based on Leishmania tarentolae cell-free system to characterize 30 putative thermostable endo-1,4-beta-glucanases and xylanases identified in public genomic databases. The system uses high-throughput assays for glucanase and xylanase activities that rely on solubilisation of labelled particulate substrates performed in multiwell plates
analysis
-
construction of a pipeline based on Leishmania tarentolae cell-free system to characterize 30 putative thermostable endo-1,4-beta-glucanases and xylanases identified in public genomic databases. The system uses high-throughput assays for glucanase and xylanase activities that rely on solubilisation of labelled particulate substrates performed in multiwell plates
analysis
rapid, selective, quantitative assay based on substrate 44-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside and reaction of product 4,6-O-(3-oxobutylidene)-beta-D-cellotriose with beta-glucosidase
analysis
rapid, selective, quantitative assay based on substrate 44-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside and reaction of product 4,6-O-(3-oxobutylidene)-beta-D-cellotriose with beta-glucosidase
analysis
rapid, selective, quantitative assay based on substrate 44-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-cellopentaoside and reaction of product 4,6-O-(3-oxobutylidene)-beta-D-cellotriose with beta-glucosidase
analysis
-
specific and sensitive assay of endo-1,4-beta-glucanase (cellulase). The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-beta-cellotrioside in the presence of thermostable beta-glucosidase. Hydrolysis by exo-acting enzymes such as beta-glucosidase and exo-beta-glucanase is prevented by the presence of the benzylidene group on the non-reducing end D-glucosyl residue. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-beta-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free D-glucose by the beta-glucosidase in the substrate mixture. The reaction is terminated and colour developed by the addition of a weak alkaline solution. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation
-
biofuel production
the enzyme is a candidate for the utilization of agro-industrial waste for fuel production
biofuel production
the enzyme is a tool for biomass conversion. The recombinant enzyme acts in high concentrations of ionic liquids and can therefore degrade alpha-cellulose or even complex cell wall preparations under those pretreatment conditions. The enzymatic conversion of lignocellulosic plant biomass into fermentable sugars is a crucial step in the production of biofuels
biofuel production
-
bioethanol fermentation using agricultural wastes
biofuel production
-
enzyme degrades carbohydrates of dried seaweed Ulva lactula. About 21 mg glucose/g of dry seaweed are obtained which can be further converted to bio-fuel
biofuel production
-
recycling of enzymes during cellulosic bioethanol production in a pilotscale stripper. When increasing the temperature (up to 65°C) or ethanol content (up to 7.5% w/v), the denaturation rate of the enzymes increases. Enzyme denaturation occurs slower when the experiments are performed in fiber beer compared to buffer only. At extreme conditions with high temperature (65°C) and ethanol content (7.5% w/v), polythylenglycol added to fiber beer has no enzyme stabilizing effect
biofuel production
-
potential of using the ionic liquids-tolerant extremophilic cellulases for hydrolysis of ionic liquids-pretreated lignocellulosic biomass, for biofuel production
biofuel production
-
potential of using the ionic liquids-tolerant extremophilic cellulases for hydrolysis of ionic liquids-pretreated lignocellulosic biomass, for biofuel production
biofuel production
-
enzymatic cell wall degradation of microalgae for biofuel production: of the Chlorella strains tested, only Chlorella emersonii CCAP211/11N shows sensitivity to cellulase. As these effects of cellulase are minor, cellulose does not appear to play a major role in cell wall integrity or permeability in most of the algal species and strains tested
biofuel production
-
its thermostability, resistance to heavy metal ions and specific activity make this enzyme an interesting candidate for industrial applications
biofuel production
the enzyme can be useful for production of bioethanol and biofuel
biofuel production
the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone
biofuel production
-
bioethanol fermentation using agricultural wastes
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biofuel production
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its thermostability, resistance to heavy metal ions and specific activity make this enzyme an interesting candidate for industrial applications
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biofuel production
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the enzyme is a tool for biomass conversion. The recombinant enzyme acts in high concentrations of ionic liquids and can therefore degrade alpha-cellulose or even complex cell wall preparations under those pretreatment conditions. The enzymatic conversion of lignocellulosic plant biomass into fermentable sugars is a crucial step in the production of biofuels
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biofuel production
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the enzyme can be useful for production of bioethanol and biofuel
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biofuel production
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the enzyme is a candidate for the utilization of agro-industrial waste for fuel production
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biofuel production
-
the enzyme can be useful for production of bioethanol and biofuel
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biofuel production
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enzyme degrades carbohydrates of dried seaweed Ulva lactula. About 21 mg glucose/g of dry seaweed are obtained which can be further converted to bio-fuel
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biofuel production
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potential of using the ionic liquids-tolerant extremophilic cellulases for hydrolysis of ionic liquids-pretreated lignocellulosic biomass, for biofuel production
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biotechnology
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Production of immobilized enzyme on Sepabeads EC-BU (hydrophobic interactions are the driving force for the adsorption of the enzyme to the carrier)
biotechnology
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considering its thermostable, alkali-stable, halostable and organic solvent-tolerant properties, the enzyme might be potentially useful for future applications in biotechnological processes
biotechnology
recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Large variations in properties such as the functional temperature range, stability, and specific activity on crystalline cellulose are found. Functional status and stability are predictable from simple linear models of the sequence-property data. Recombined protein fragments contribute additively to these properties in a given chimera
biotechnology
-
considering its thermostable, alkali-stable, halostable and organic solvent-tolerant properties, the enzyme might be potentially useful for future applications in biotechnological processes
-
biotechnology
-
recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Large variations in properties such as the functional temperature range, stability, and specific activity on crystalline cellulose are found. Functional status and stability are predictable from simple linear models of the sequence-property data. Recombined protein fragments contribute additively to these properties in a given chimera
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degradation
cellulase is an industrially important enzyme for biomass saccharification at high temperature. beta-Glucan can be completely degraded to glucose at high temperature with a combination of the hyperthermophile Pyrococcus furiosus endocellulase (EGPf) and beta-glucosidase (BGLPf). beta-Glucans are polysaccharides of D-glucose monomers formed by beta(1->3),(1->4) mixed-linkage bonds. They occur most commonly as cellulose in plants, in the bran of cereal grains, the cell wall of baker's yeast, and in certain fungi, mushrooms, and bacteria
degradation
-
a statistical optimization approach involving Plackett-Burman design and response surface methodology on submerged fermentation using cane molasses medium results in the production of 72410, 36420, 32420 and 5180 U/l of xylanase, endo-beta-1,4-glucanase, exo-beta-1,4-glucanase, and beta-glucosidase, respectively, i.e. more than fourfold improvements in production of xylanolytic and cellulolytic enzymes. Addition of microparticles engineers fungal morphology and enhances enzymes production. Maximum sugar yield of 578.12 and 421.79 mg/g substrate for waste tea cup and rice straw, respectively, are achieved after 24 h
degradation
addition of Eg5A to cellobiase (i.e. cellobiohydrolase and beta-glucosidase) results in a 53% increasing saccharification of NaOH-pretreated barley straw, and the glucose release is 47% higher than with cellobiase treatment alone
degradation
addition of isoform Eg5A to cellobiase (cellobiohydrolase and beta-glucosidase) results in a 53% increasing saccharification of NaOH-pretreated barley straw, whereas the glucose release is 47% higher than that cellobiase treatment alone
degradation
-
after hydrolysis and fermentation of wheat straw a significant amount of active enzymes can be recovered by recycling the liquid phase. In the early stage of the process, enzyme adsorbs to the substrate, then gradually returning to the solution as the saccharification proceeds. The hydrolysis yield and enzyme recycling efficiency in consecutive recycling rounds can be increased by using high enzyme loadings and moderate temperatures. The amount of enzymes in the liquid phase increases with its thermostability and hydrolytic efficiency
degradation
-
bioethanol production by Aspergillus fumigatus JCF at optimised growth conditions and Saccharomyces cerevisiae for simultaneous saccharification and fermentation. Using cotton seed as the substrate, maximum bioethanol concentration of 6.7 g/l can be achieved
degradation
cellulase complex containing cellulolytic enzymes,endoglucanase CelE, EC 3.2.1.4, and beta-glucosidase BglA, EC 3.2.1.21, to completely degrade cellulose to glucose. The cellulases are displayed on the cell surface of Corynebacterium glutamicum by using themechanosensitive channel to anchor enzymes in the cytoplasmic membrane. The displayed cellulases complexes have a synergic effect on the direct conversion of biomass to reducing sugars leading to 3.1- to 6.0fold increase compared to the conversion by the secreted cellulases complexes. The displayed cellulases complexes increase the residual activities of cCelEand cBglA at 70°C from 28.3% and 24.3% in the secreted form to 65.1% and 82.8%, respectively
degradation
-
during cultivation, consortium SV79 produces the maximum filter paper activity (FPase, 9.41 U/ml), carboxymethylcellulase activity (CMCase, 6.35 U/ml), and xylanase activity (4.28 U/ml) with sugarcane bagasse, spent mushroom substrate, and Sorbus anglica, respectively. The ethanol production using Miscanthus floridulus as substrate is up to 2.63 mM ethanol/g
degradation
-
effect of nickel-cobaltite (NiCo2O4) nanoparticles on production and thermostability of the cellulase enzyme system. Maximum production of endoglucanase (211 IU/gds), beta-glucosidase (301 IU/gds), and xylanase (803 IU/gds) is achieved after 72 h without nanoparticles, while in the presence of 1 mM of nanoparticles, endoglucanase, beta-glucosidase, and xylanase activity increase by about 49, 53, and 19.8%, respectively, after 48 h of incubation. Crude enzyme is thermally stable for 7 h at 80°C in presence of nanoparticles, as against 4 h at the same temperature for control samples
degradation
-
effects of microalgal biomass particle on the degree of enzymatic hydrolysis and bioethanol production by single enzyme hydrolysis (cellulase) and double enzyme hydrolysis (cellulase and cellobiase). The glucose yield from biomass in the smallest particle size range examined, i.e. 35 microm to 90 microm, is the highest, 134.73 mg glucose/g algae, while the yield from biomass in the larger particle size range from 295 microm to 425 microm is 75.45mg glucose/g algae. A similar trend is observed for bioethanol yield, with the highest yield of 0.47 g EtOH/g glucose obtained from biomass in the smallest particle size range
degradation
-
enzyme extracts obtained from growing Acrophialophora nainiana on cellulose, dirty-cotton residue, sugarcane bagasse and banana stem can be used in the hydrolysis of sugarcane bagasse, untreated, pre-treated by steam explosion and pretreated by acid-catalysed steam explosion. The carbohydrase activity profile of the enzyme preparations varies significantly with the used carbon source. The highest enzyme activities, especially total cellulase (0.0132 IU) and xylanase (0.0774 IU) activities, are obtained with banana stem as the carbon source. On sugarcane bagasse, total cellulase activity on filter paper and pectinase activities are predominant. The exocellulase/endocellulase activity ratio (FPAsol/FPAinsol) of the cellulases produced varies between 1 and 4 depending on the substrate. The highest endocellulase activity (FPAinsol) content is obtained when grown on sugarcane bagasse
degradation
hydrolysis of 2% carboxymethyl cellulose with purified enzyme at its optimum temperature and pH results in complete hydrolysis within 2 h yielding 18% cellotriose, 72% cellobiose and 10% glucose
degradation
-
immobilization of enzyme on functionalized magnetic silica nanospheres using glutaraldehyde. Immobilized cellulase exhibits better resistance to high temperature and pH inactivation in comparison to free cellulase. Use of cross-linking agent leads to a greater amount of immobilized cellulase and better operational stability. The amount of immobilized cellulase with the cross-linking agent is 92 mg/g support. The activity of the immobilized cellulase is still 85.5% of the initial activity after 10 continuous uses
degradation
mixtures of beta-xylosidase, xylanase, beta-glucosidase, and cellulase isolated from the metagenomic library of a long-term dry thermophilic methanogenic digester community retain high residual synergistic activities after incubation with cellulose, xylan, and steam-exploded corncob at 50°C for 72 h. About 55% dry weight of steam-exploded corncob is hydrolyzed to glucose and xylose by the synergistic action of the four enzymes at 50°C for 48 h
degradation
-
preparation of functionalized magnetic nanospheres by co-condensation of tetraethylorthosilicate with aminosilanes 3-(2-aminoethylaminopropyl)-triethoxysilane (AEAPTES), 3-(2-aminoethy-laminopropyl)-trimethoxysilane (AEAPTMES) and 3-aminopropyltriethoxysilane (APTES) and use as supports for immobilization of cellulase. The magnetic nanospheres with core-shell morphologies exhibit higher capacity for cellulase immobilization than unfunctionalized magnetic nanospheres. AEAPTMES with methoxy groups is favored to be hydrolyzed and grafted on unfunctionalized magnetic nanospheres. AEAPTMES functionalized magnetic nanospheres with the highest zeta-potential (29 mV) exhibit 87% activity recovery, and the maximum amount of immobilized cellulase is112 mg/g support at concentration of initial cellulase of 8 mg/ml. Immobilized cellulase on AEAPTMES functionalized magnetic nanospheres has higher temperature stability and broader pH stability than other immobilized cellulases and free cellulase
degradation
-
pretreatment method for lignocellulosic wheat straw to depolymerize lignin and expose the cellulose polymers to produce bioethanol. Wheat straw is pretreated with ligninolytic enzymes extract produced from Ganoderma lucidum under optimum solid state fermentation conditions. The pretreated biomass was further subjected to the enzymatic hydrolysis by crude unprocessed cellulases (beta-1,4-endoglucanase, 53.5 U/ml, beta-1,4-exoglucanase, 41.3 U/ml, beta-1,4-glucosidase, 46.8 U/ml, and xylanase 39 U/ml) produced by Trichoderma harzaianum. Under optimal conditions for enzymatic saccharification, 10% (w/v) of pretreated biomass is hydrolyzed completely and converted to 72.5 and 2.4 g/l of glucose and xylose, respectively
degradation
-
saccharification of pretreated dry potato peels, carrot peels, composite waste mixture, orange peels, onion peels, banana peels, pineapple peels by crude enzyme extract from Aspergillus niger NS-2 results in cellulose conversion efficiencies of 9298%
degradation
the purified enzyme decreases the viscosity of carboxymethyl cellulose when assessed at 70-85°C and is capable of releasing reducing sugars from acid-pretreated straw at 70 and 75°C
degradation
-
Trichoderma reesei NRRL-6156 filter paper exocellulase and endocellulase hydrolysis of sugarcane bagasse, results in 224.0 and 229 gram of total reducing sugar per kilogram of dry bagasse at 43.4°C and a concentration of enzymatic extract of 18.6% in water and ultrasound baths, respectively. The yields obtained are comparable to commercial enzymes
degradation
under simulated mashing conditions, addition of 60 U Egl5A reduces more viscosity (10.0 vs.7.6%) than 80 U of Ultraflo XL from Novozymes
degradation
under simulated mashing conditions, addition of Cel7A (99 microg) reduces the mash viscosity by 9.1% and filtration time by 24.6%
degradation
-
use of amine-functionalized cobalt ferrite (AF-CoFe2O4) magnetic nanoparticles for immobilization of cellulase. Particles show a mean diameter of about 8 nm and remain distinct with no significant change in size after binding with cellulase. The immobilized cellulase has higher thermal stability than free cellulase and shows good reusability after recovery
degradation
use of mutant T57N/E53D/S79P/T80E/V101I/S133R/N155E/G189S/F191V/T233V/G239E/V265T/D271Y/G293A7S309W/S318P and previously engineered highly active, thermostable variants of the fungal cellobiohydrolases Cel6A and Cel7A to hydrolyzes cellulose synergistically at an optimum temperature of 70°C over 60 h.The thermostable mixture produces three times as much total sugar as the best mixture of the wild type enzymes operating at their optimum temperature of 60°C
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
addition of recombinant Eg5A to cellobiase (cellobiohydrolase and beta-glucosidase) results in a 53% increase in saccharification of NaOH-pretreated barley straw, whereas the glucose release is 47% higher than with cellobiase treatment alone
degradation
Thermochaetoides thermophila
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cellulase enzyme filtrate from Chaetomium thermophile saccharifies 5% kallar grass straw to 69% reducing sugars (quantitatively) at 50°C. Glucose concentration in the hydrolysates from different fungi is in the decreasing order of Chaetomium thermophile > Trichoderma reesei > Sporotrichum thermophile > Aspergillus fumigatus > Torula thermophila > Humicola grisea > Malbranchea pulchella. At 60°C, thermostable enzymes hydrolyse kallar grass straw at a maximum rate for the initial 20 h
degradation
-
comparison of endoglucanases able to rapidly reduce the viscosity of 15% (w/w, dry matter) hydrothermally pretreated wheat straw. Based on temperature profiling studies, Thermoascus aurantiacus EGII/Cel5A is the most promising enzyme for biomass liquefaction
degradation
crude cellulase efficiently hydrolyzes office waste paper, algal pulp (Gracillaria verulosa), and biologically treated wheat straw at 60°C with sugar release of about 830 mg/ml, 285 mg/g, and 260 mg/g of the substrate, respectively
degradation
crude thermostable cellulases and xylanase hydrolyze phosphoric acid-swollen wheat straw, avicel and untreated xylan up to 74, 71 and 90 %, respectively
degradation
-
Freeze-dried enzyme of Trichoderma reesei, even at higher enzyme concentration results in 60% reducing sugars yield (quantitatively) at 50°C. Glucose concentration in the hydrolysates from different fungi is in the decreasing order of Chaetomium thermophile > Trichoderma reesei > Sporotrichum thermophile > Aspergillus fumigatus > Torula thermophila > Humicola grisea > Malbranchea pulchella. At 60°C, thermostable enzymes hydrolyse kallar grass straw at a maximum rate for the initial 20 h
degradation
-
hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase
degradation
oligosaccharides with degree of polymerization 2-10 are formed by hydrolysis of beta-glucan. The recombinant enzyme preparations are fast and effective in decreasing the reduced viscosity of wholegrain barley extract than some commercial enzyme preparations
degradation
-
scale-up systems for cellulase production and enzymatic hydrolysis of pretreated rice straw at highsolid loadings and by Aspergillus terreus. In a horizontal rotary drum reactor at 50°C with 25 % (w/v) solid loading and 9 FPU/g substrate enzyme load up to 20 % highly concentrated fermentable sugars are obtained at 40 h with an increased saccharification efficiency of 76 % compared to laboratory findings (69.2 %). Nearly 79-84% of the cellulases and more than 90% of the sugars are recovered from the saccharification mixture
degradation
-
use of lucerne fibre as a cellulase-recycling vehicle during bioconversion processes. Adsorption of cellulase complexes is minimal at the pH optimum, 5.0, for fibre conversion to soluble sugars. Lowering of incubation temperature to 3°C enhances adsorption of fungal cellulases. The adsorptive capacity can be improved about 30% by raising the pH above the hydrolysis optimum during the recycling phase
degradation
-
use of lucerne fibre as a cellulase-recycling vehicle during bioconversion processes. Adsorption of cellulase complexes is minimal at the pH optimum, 6.2, for fibre conversion to soluble sugars. Lowering of incubation temperature to 3°C enhances adsorption of fungal cellulases. The adsorptive capacity can be improved about 30% by raising the pH above the hydrolysis optimum during the recycling phase
degradation
use to release dye in neutral pH conditions from indigo-dyed cotton-containing fabric in biostoning applications
degradation
-
using enzymatic extract from M. thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively
degradation
MG570051
addition of Cel9K to a commercial enzyme set (Celluclast 1.5L + Novozym 188) increases the saccharification of the pretreated reed and rice straw powders by 30.4% and 15.9%, respectively
degradation
-
enzyme releases high amounts of reducing sugars from wheat bran and corn cobs, being a useful biocatalyst for producing bioethanol and fine chemicals from agroresidues
degradation
-
replacement of carbohydrate-binding module by modules from enzymes with different specificities leads to enhanced activity that is affected by carbohydrate-binding module binding specificity, e.g. on ball-milled cellulose or avicel. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls
degradation
under acidic conditions at 50°C, the enzyme is effective in digesting the green algae Ulva pertusa
degradation
-
cellulase complex containing cellulolytic enzymes,endoglucanase CelE, EC 3.2.1.4, and beta-glucosidase BglA, EC 3.2.1.21, to completely degrade cellulose to glucose. The cellulases are displayed on the cell surface of Corynebacterium glutamicum by using themechanosensitive channel to anchor enzymes in the cytoplasmic membrane. The displayed cellulases complexes have a synergic effect on the direct conversion of biomass to reducing sugars leading to 3.1- to 6.0fold increase compared to the conversion by the secreted cellulases complexes. The displayed cellulases complexes increase the residual activities of cCelEand cBglA at 70°C from 28.3% and 24.3% in the secreted form to 65.1% and 82.8%, respectively
-
degradation
-
under simulated mashing conditions, addition of Cel7A (99 microg) reduces the mash viscosity by 9.1% and filtration time by 24.6%
-
degradation
-
hydrolysis of 2% carboxymethyl cellulose with purified enzyme at its optimum temperature and pH results in complete hydrolysis within 2 h yielding 18% cellotriose, 72% cellobiose and 10% glucose
-
degradation
-
Trichoderma reesei NRRL-6156 filter paper exocellulase and endocellulase hydrolysis of sugarcane bagasse, results in 224.0 and 229 gram of total reducing sugar per kilogram of dry bagasse at 43.4°C and a concentration of enzymatic extract of 18.6% in water and ultrasound baths, respectively. The yields obtained are comparable to commercial enzymes
-
degradation
-
replacement of carbohydrate-binding module by modules from enzymes with different specificities leads to enhanced activity that is affected by carbohydrate-binding module binding specificity, e.g. on ball-milled cellulose or avicel. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls
-
degradation
-
using enzymatic extract from M. thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively
-
degradation
-
effect of nickel-cobaltite (NiCo2O4) nanoparticles on production and thermostability of the cellulase enzyme system. Maximum production of endoglucanase (211 IU/gds), beta-glucosidase (301 IU/gds), and xylanase (803 IU/gds) is achieved after 72 h without nanoparticles, while in the presence of 1 mM of nanoparticles, endoglucanase, beta-glucosidase, and xylanase activity increase by about 49, 53, and 19.8%, respectively, after 48 h of incubation. Crude enzyme is thermally stable for 7 h at 80°C in presence of nanoparticles, as against 4 h at the same temperature for control samples
-
degradation
-
use to release dye in neutral pH conditions from indigo-dyed cotton-containing fabric in biostoning applications
-
degradation
-
saccharification of pretreated dry potato peels, carrot peels, composite waste mixture, orange peels, onion peels, banana peels, pineapple peels by crude enzyme extract from Aspergillus niger NS-2 results in cellulose conversion efficiencies of 9298%
-
degradation
-
under simulated mashing conditions, addition of 60 U Egl5A reduces more viscosity (10.0 vs.7.6%) than 80 U of Ultraflo XL from Novozymes
-
degradation
-
Freeze-dried enzyme of Trichoderma reesei, even at higher enzyme concentration results in 60% reducing sugars yield (quantitatively) at 50°C. Glucose concentration in the hydrolysates from different fungi is in the decreasing order of Chaetomium thermophile > Trichoderma reesei > Sporotrichum thermophile > Aspergillus fumigatus > Torula thermophila > Humicola grisea > Malbranchea pulchella. At 60°C, thermostable enzymes hydrolyse kallar grass straw at a maximum rate for the initial 20 h
-
degradation
-
hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase
-
degradation
-
enzyme releases high amounts of reducing sugars from wheat bran and corn cobs, being a useful biocatalyst for producing bioethanol and fine chemicals from agroresidues
-
degradation
-
use of mutant T57N/E53D/S79P/T80E/V101I/S133R/N155E/G189S/F191V/T233V/G239E/V265T/D271Y/G293A7S309W/S318P and previously engineered highly active, thermostable variants of the fungal cellobiohydrolases Cel6A and Cel7A to hydrolyzes cellulose synergistically at an optimum temperature of 70°C over 60 h.The thermostable mixture produces three times as much total sugar as the best mixture of the wild type enzymes operating at their optimum temperature of 60°C
-
degradation
-
crude cellulase efficiently hydrolyzes office waste paper, algal pulp (Gracillaria verulosa), and biologically treated wheat straw at 60°C with sugar release of about 830 mg/ml, 285 mg/g, and 260 mg/g of the substrate, respectively
-
degradation
-
crude thermostable cellulases and xylanase hydrolyze phosphoric acid-swollen wheat straw, avicel and untreated xylan up to 74, 71 and 90 %, respectively
-
degradation
-
effects of microalgal biomass particle on the degree of enzymatic hydrolysis and bioethanol production by single enzyme hydrolysis (cellulase) and double enzyme hydrolysis (cellulase and cellobiase). The glucose yield from biomass in the smallest particle size range examined, i.e. 35 microm to 90 microm, is the highest, 134.73 mg glucose/g algae, while the yield from biomass in the larger particle size range from 295 microm to 425 microm is 75.45mg glucose/g algae. A similar trend is observed for bioethanol yield, with the highest yield of 0.47 g EtOH/g glucose obtained from biomass in the smallest particle size range
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degradation
-
after hydrolysis and fermentation of wheat straw a significant amount of active enzymes can be recovered by recycling the liquid phase. In the early stage of the process, enzyme adsorbs to the substrate, then gradually returning to the solution as the saccharification proceeds. The hydrolysis yield and enzyme recycling efficiency in consecutive recycling rounds can be increased by using high enzyme loadings and moderate temperatures. The amount of enzymes in the liquid phase increases with its thermostability and hydrolytic efficiency
-
degradation
-
use of amine-functionalized cobalt ferrite (AF-CoFe2O4) magnetic nanoparticles for immobilization of cellulase. Particles show a mean diameter of about 8 nm and remain distinct with no significant change in size after binding with cellulase. The immobilized cellulase has higher thermal stability than free cellulase and shows good reusability after recovery
-
degradation
-
bioethanol production by Aspergillus fumigatus JCF at optimised growth conditions and Saccharomyces cerevisiae for simultaneous saccharification and fermentation. Using cotton seed as the substrate, maximum bioethanol concentration of 6.7 g/l can be achieved
-
detergent
-
thermostability, pH-stability, good hydrolytic capability, and stability in the presence of detergents, surfactants, chelators and commercial proteases make this enzyme potentially useful in laundry detergents
detergent
-
used commercially in laundry detergents
detergent
-
strong resistance to anionic surfactants and oxidizing agents, might be a usefull enzyme in detergent industry
detergent
-
thermostability, pH-stability, good hydrolytic capability, and stability in the presence of detergents, surfactants, chelators and commercial proteases make this enzyme potentially useful in laundry detergents
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environmental protection
-
cellulase producing haloarchael cells may be potentially utilized for the treatment of hypersaline waste water to remove cellulose
environmental protection
-
cellulase producing haloarchael cells may be potentially utilized for the treatment of hypersaline waste water to remove cellulose
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food industry
-
extraction of pectins from apple pomace with monoactive preparation of endoxylanase and endcellulase. Pectin extracted with endocellulase has 1.5fold lower molecular mass but contains significantly more galacturonic acid (70.5%) of a high degree of methylation (66.3%). The simultaneous application of both enzymaticpreparations results in their cooperation, leading to a decrease of both the extraction efficiency and the molecular mass of pectin. This pectin displays the highest galacturonic acid (74.7%) and rhamnose contents
food industry
-
the capacity of Cel8A to cleave 1,3-1,4-beta-glucans is significantly affected by the presence of the barley-based feed for broilers. Exogenous 1,3-1,4-beta-glucanases (EC 3.2.1.73) but not 1,4-beta-glucanases are obligatory enzymes to improve the nutritive value of barley-based diets for broilers. Enzyme is completely resistant to proteolytic inactivation after a 30 min incubation with pancreatic proteases
industry
-
the purified enzyme performs well in biostoning of denim fabric at neutral pH
industry
due to its acidophilic (pH 3.5) and high temperature stability (up to 90°C), CSCMCase may be useful for industrial application such as animal feed industry and clarification of fruit juices
industry
-
enzyme possesses high power of defibrillation of textile and laundry. Polypeptide can be exploited for mass production and application in local industries
industry
potent enzyme for industrial bioprocesses, including the bio-polishing of cotton products, food processing and bioethanol production
industry
STCE1 may be appropriate for laundry use
industry
because of its ability to hydrolyze celluloses at high temperatures above 90°C, as well as its thermostability, the enzyme is expected to be an excellent tool for industrial hydrolysis of cellulose, particularly for biopolishing of cotton products
industry
textile and detergent industry, combination of CBH6A and EgGH45
industry
-
economical analysis of cellulase production by solid-state fermentation in a pilot plant integrated to both a first and a second generation ethanol processes. Growth of Myceliophthora thermophila I-1D3b at 45°C during 96 h on sugarcane bagasse and wheat bran. shows that the process is economically attractive, due to its easy integration to the main process, and its revenue is up to four fold greater than electricity cogeneration
industry
-
endoglucanases from family GH45 are applied in formulation of detergents and in industrial pulp and paper processes
industry
-
endoglucanases from family GH45 are applied in formulation of detergents and in industrial pulp and paper processes
industry
-
enzyme Bc22Cel is a potential and useful candidate for industrial applications, such as the bioconversion of sugarcane bagasse to its derivatives
industry
Thermochaetoides thermophila
the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
industry
the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone
industry
the thermophilic nature and biochemical properties of the enzyme indicate its potential suitability in industrial applications undertaken at high temperature, such as the production of second-generation bioethanol from lignocellulosic feedstocks and in the brewing industry
industry
Thermochaetoides thermophila IMI 039719
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the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
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industry
Thermochaetoides thermophila DSM 1495
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the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
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industry
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because of its ability to hydrolyze celluloses at high temperatures above 90°C, as well as its thermostability, the enzyme is expected to be an excellent tool for industrial hydrolysis of cellulose, particularly for biopolishing of cotton products
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industry
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the thermophilic nature and biochemical properties of the enzyme indicate its potential suitability in industrial applications undertaken at high temperature, such as the production of second-generation bioethanol from lignocellulosic feedstocks and in the brewing industry
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industry
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the thermophilic nature and biochemical properties of the enzyme indicate its potential suitability in industrial applications undertaken at high temperature, such as the production of second-generation bioethanol from lignocellulosic feedstocks and in the brewing industry
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industry
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enzyme possesses high power of defibrillation of textile and laundry. Polypeptide can be exploited for mass production and application in local industries
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industry
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the purified enzyme performs well in biostoning of denim fabric at neutral pH
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industry
Thermochaetoides thermophila CBS 144.50
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the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
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industry
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economical analysis of cellulase production by solid-state fermentation in a pilot plant integrated to both a first and a second generation ethanol processes. Growth of Myceliophthora thermophila I-1D3b at 45°C during 96 h on sugarcane bagasse and wheat bran. shows that the process is economically attractive, due to its easy integration to the main process, and its revenue is up to four fold greater than electricity cogeneration
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industry
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STCE1 may be appropriate for laundry use
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synthesis
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synthesis of glyceroyl beta-N-acetyllactosaminide and derivatives, that could be used as starting material for the synthesis of neoglycolipid and new kinds of detergents and as acceptors for glycosidase and glycosyltransferase
synthesis
when the enzyme is used in combination withbeta-glucosidase, cellulose is completely hydrolyzed to glucose at high temperature, suggesting great potential for EGPh in bioethanol industrial applications
synthesis
glucose production from cellulose material using beta-glucosidase from Pyrococcus furioses and endocellulase from Pyrococcus horikoshii. The combination reaction can produce only glucose without the other oligosaccharides from phosphoric acid swollen Avicel
synthesis
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production of enzyme in parallel-operated shake flasks and, alternatively, in parallel-operated stirred-tank bioreactors on a 10-m. scale. Reaction conditions with 53.3 g/l microcrystalline cellulose in the initial medium, no lactose feeding and 3.3 g/l and day intermittent ammonium sulfate addition are optimal. The optimum substrate supply on a liter-scale results in the production of 4.88 filter paper units of enzyme per ml with after 96 h
synthesis
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use of a cellulase blend to evaluate its application in a simultaneous saccharification and fermentation process for second generation ethanol production from sugar cane bagasse. After enzyme production in a bioreactor and tangential ultrafiltration in hollow fiber membranes, the cellulolytic preparation is stable for at least 300 h at both 37°C and 50°C. The ethanol production is carried out by sugar cane bagasse partially delignified cellulignin fed-batch simultaneous saccharification and fermantation process, using the onsite cellulase blend. The method applied results in 100 g/l ethanol concentration at the end of the process, which corresponds to a fermentation efficiency of 78% of the maximum obtainable theoretically. The experimental results lead to the ratio of 380 l of ethanolper ton of sugar cane bagasse partially delignified cellulignin
synthesis
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40% higher cellulase activity on filter paper in 72 h is observed with the addition of 1 mM of nickel-cobaltite (NiCo2O4) nanoparticles in the growth medium. Maximum production of endoglucanase (211 IU/gds), beta-glucosidase (301 IU/gds), and xylanase (803 IU/gds) is achieved after 72 h without nanoparticles, while in the presence of 1 mM of nanoparticles, endoglucanase, beta-glucosidase, and xylanase activity increase by about 49, 53, and 19.8%, respectively, after 48 h of incubation
synthesis
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a medium based on starch casein minerals containing carboxymethyl cellulose and beef extract supports enhanced cellulase production. Carboxymethyl cellulose, beef extract , NaCl, temperature and pH are significant for cellulase production. Optimization of cellulase production results in an enhancement of endoglucanase activity to 27 IU per ml
synthesis
expression of enzyme in Escherichia coli and Thermotoga sp. after fusion to the signal peptides of TM1840 (amyA) or TM0070 (xynB). Expressed in Escherichia coli and Thermotoga sp. renders the hosts with increased endo- and exoglucanase activities. In Escherichia coli, the recombinant enzymes are mainly bound to the bacterial cells, whereas in Thermotoga sp., about half of the enzyme activities are observed in the culture supernatants. However, the cellulase activities are lost in Thermotoga sp. after three consecutive transfers
synthesis
expression of enzyme in Escherichia coli and Thermotoga sp. after fusion to the signal peptides of TM1840 (amyA) or TM0070 (xynB). Expressed in Escherichia coli and Thermotoga sp. renders the hosts with increased endoglucanase activities. In Escherichia coli, the recombinant enzymes are mainly bound to the bacterial cells, whereas in Thermotoga sp., about half of the enzyme activities are observed in the culture supernatants. However, the cellulase activities are lost in Thermotoga sp. after three consecutive transfers
synthesis
heterologous expression in Bacillus subtilis combined with customized signal peptides for secretion from a random libraries with 173 different signal peptides originating from the Bacillus subtilis genome. The customized signal peptide does not affect enzyme performance when assayed on carboxymethyl cellulose, phosphoric acid swollen cellulose, and microcrystalline cellulose
synthesis
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in regulator cre1-silenced strain C88, the filter paper hydrolyzing activity and beta-1,4-endoglucanase activity are 3.76-, and 1.31fold higher, respectively, than those in the parental strain when the strains are cultured in inducing medium for 6 days. The activities of beta-1,4-exoglucanase and cellobiase are 2.64-, and 5.59fold higher, respectively, than those in the parental strain when the strains are cultured for 5 days
synthesis
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optimization of cultural conditions for enhanced cellulase production. Under solid-state fermentation, yields of carboxymethylcellulase are 463.9 U/g, filter paper cellulase 101.1 U/g and beta-glucosidase 99 U/g
synthesis
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alkali-pretreated roots of Taraxacum kok-saghyz (rubber dandelion), incubated with crude enzyme extracts from Thermomyces lanuginosus STm yield more natural rubber (90 mg/g dry root) than the protocols, Eskew process (24 mg/g) and commercial-enzyme-combination process (45 mg/g). The crude enzyme treatment at 91.6% rubber purity approaches the purity of the commercial-enzyme-combination process at 94.1% purity
synthesis
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scale-up systems for cellulase production and enzymatic hydrolysis of pretreated rice straw at highsolid loadings and by Aspergillus terreus. In a horizontal rotary drum reactor at 50°C with 25 % (w/v) solid loading and 9 FPU/g substrate enzyme load up to 20 % highly concentrated fermentable sugars are obtained at 40 h with an increased saccharification efficiency of 76 % compared to laboratory findings (69.2 %). Nearly 79-84% of the cellulases and more than 90% of the sugars are recovered from the saccharification mixture
synthesis
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under optimised conditions of growth on wheat bran, 420.8 and 22.73 units/g substrate of endo-beta-1,4-glucanase and filter paper cellulase are produced, respectively. Both endo-beta-1,4-glucanase and filter paper activity production show significant dependence on ammonium sulfate concentration and pH
synthesis
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enhanced production of enzyme in Escherichia coli. High-cell-density and optimal CenC expression are obtained in ZYBM9 medium induced either with 0.5 mM IPTG/150 mM lactose, after 6 h induction at 37°C. Before induction, bacterial cells are given heat shock (42°C) for 1 h when culture density (OD600 nm) reached at 0.6. Intracellular enzyme activity is enhanced by 6.67- and 3.20fold in ZYBM9 (yeast extract 0.5% (w/v), NaCl 0.5% (w/v), tryptone 1.0% (w/v), NH4Cl 0.1% (w/v), KH2PO4 0.3% (w/v), Na2HPO4 0.6% (w/v), MgSO4.7H2O 1 mM, and Glucose 0.4% (w/v)) and 3×ZYBM9 medium, respectively, under optimal conditions
synthesis
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the cold active butanol-tolerant endoglucanase is valuable for biobutanol production by a simultaneous saccharification and fermentation process
synthesis
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heterologous expression in Bacillus subtilis combined with customized signal peptides for secretion from a random libraries with 173 different signal peptides originating from the Bacillus subtilis genome. The customized signal peptide does not affect enzyme performance when assayed on carboxymethyl cellulose, phosphoric acid swollen cellulose, and microcrystalline cellulose
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synthesis
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in regulator cre1-silenced strain C88, the filter paper hydrolyzing activity and beta-1,4-endoglucanase activity are 3.76-, and 1.31fold higher, respectively, than those in the parental strain when the strains are cultured in inducing medium for 6 days. The activities of beta-1,4-exoglucanase and cellobiase are 2.64-, and 5.59fold higher, respectively, than those in the parental strain when the strains are cultured for 5 days
-
synthesis
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when the enzyme is used in combination withbeta-glucosidase, cellulose is completely hydrolyzed to glucose at high temperature, suggesting great potential for EGPh in bioethanol industrial applications
-
synthesis
-
glucose production from cellulose material using beta-glucosidase from Pyrococcus furioses and endocellulase from Pyrococcus horikoshii. The combination reaction can produce only glucose without the other oligosaccharides from phosphoric acid swollen Avicel
-
synthesis
-
alkali-pretreated roots of Taraxacum kok-saghyz (rubber dandelion), incubated with crude enzyme extracts from Thermomyces lanuginosus STm yield more natural rubber (90 mg/g dry root) than the protocols, Eskew process (24 mg/g) and commercial-enzyme-combination process (45 mg/g). The crude enzyme treatment at 91.6% rubber purity approaches the purity of the commercial-enzyme-combination process at 94.1% purity
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synthesis
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under optimised conditions of growth on wheat bran, 420.8 and 22.73 units/g substrate of endo-beta-1,4-glucanase and filter paper cellulase are produced, respectively. Both endo-beta-1,4-glucanase and filter paper activity production show significant dependence on ammonium sulfate concentration and pH
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synthesis
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40% higher cellulase activity on filter paper in 72 h is observed with the addition of 1 mM of nickel-cobaltite (NiCo2O4) nanoparticles in the growth medium. Maximum production of endoglucanase (211 IU/gds), beta-glucosidase (301 IU/gds), and xylanase (803 IU/gds) is achieved after 72 h without nanoparticles, while in the presence of 1 mM of nanoparticles, endoglucanase, beta-glucosidase, and xylanase activity increase by about 49, 53, and 19.8%, respectively, after 48 h of incubation
-
synthesis
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optimization of cultural conditions for enhanced cellulase production. Under solid-state fermentation, yields of carboxymethylcellulase are 463.9 U/g, filter paper cellulase 101.1 U/g and beta-glucosidase 99 U/g
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synthesis
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enhanced production of enzyme in Escherichia coli. High-cell-density and optimal CenC expression are obtained in ZYBM9 medium induced either with 0.5 mM IPTG/150 mM lactose, after 6 h induction at 37°C. Before induction, bacterial cells are given heat shock (42°C) for 1 h when culture density (OD600 nm) reached at 0.6. Intracellular enzyme activity is enhanced by 6.67- and 3.20fold in ZYBM9 (yeast extract 0.5% (w/v), NaCl 0.5% (w/v), tryptone 1.0% (w/v), NH4Cl 0.1% (w/v), KH2PO4 0.3% (w/v), Na2HPO4 0.6% (w/v), MgSO4.7H2O 1 mM, and Glucose 0.4% (w/v)) and 3×ZYBM9 medium, respectively, under optimal conditions
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synthesis
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use of a cellulase blend to evaluate its application in a simultaneous saccharification and fermentation process for second generation ethanol production from sugar cane bagasse. After enzyme production in a bioreactor and tangential ultrafiltration in hollow fiber membranes, the cellulolytic preparation is stable for at least 300 h at both 37°C and 50°C. The ethanol production is carried out by sugar cane bagasse partially delignified cellulignin fed-batch simultaneous saccharification and fermantation process, using the onsite cellulase blend. The method applied results in 100 g/l ethanol concentration at the end of the process, which corresponds to a fermentation efficiency of 78% of the maximum obtainable theoretically. The experimental results lead to the ratio of 380 l of ethanolper ton of sugar cane bagasse partially delignified cellulignin
-
synthesis
-
a medium based on starch casein minerals containing carboxymethyl cellulose and beef extract supports enhanced cellulase production. Carboxymethyl cellulose, beef extract , NaCl, temperature and pH are significant for cellulase production. Optimization of cellulase production results in an enhancement of endoglucanase activity to 27 IU per ml
-
synthesis
-
production of enzyme in parallel-operated shake flasks and, alternatively, in parallel-operated stirred-tank bioreactors on a 10-m. scale. Reaction conditions with 53.3 g/l microcrystalline cellulose in the initial medium, no lactose feeding and 3.3 g/l and day intermittent ammonium sulfate addition are optimal. The optimum substrate supply on a liter-scale results in the production of 4.88 filter paper units of enzyme per ml with after 96 h
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