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(1-3)-beta-D-glucan + H2O
laminaritriose + laminaritetraose
(1-3:1-4)-beta-D-glucan + H2O
?
2 laminaripentaose + H2O
octasaccharide + ?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminariheptaose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose, low activity
-
?
alkali soluble 1,3-beta-glucan + H2O
reducing sugar + ?
-
produced by solubilised 1,3-beta-glucan synthase complex of A. fumigatus
-
?
alkaline-treated paramylon + H2O
?
-
78.6% of the activity with laminarin
-
-
?
alpha-laminaribiosyl fluoride + H2O
?
-
-
-
-
?
azurine-crosslinked beta-1,3-glucan + H2O
?
-
AZCL-pachyman
-
?
azurine-crosslinked beta-1,3:1,4-glucan + H2O
?
-
AZCL-barley-beta-glucan, 100fold less active than on AZCL-pachyman
-
?
barley beta-glucan + H2O
?
barley glucan + H2O
?
-
8% activity compared to laminarin
-
-
?
beta-1,3-1,4-glucan + H2O
?
substrate from Hordeum vulgare, substrate of EC 3.2.1.6, endo-1,3(4)-beta-glucanase
-
-
?
beta-1,3-glucan + H2O
laminaribiose + D-glucose
carboxy-methylated pachyman + H2O
?
carboxymethyl cellulose + H2O
?
-
49.56% activity compared to laminarin
-
-
?
carboxymethyl curdlan + H2O
?
carboxymethyl curdlan-Remazol Brilliant Blue + H2O
?
-
-
-
-
?
carboxymethyl pachyman + H2O
?
carboxymethyl-cellulose + H2O
?
-
carboxymethyl-cellulose is only hydrolyzed by YlCrh1Sp
-
-
?
carboxymethyl-curdlan + H2O
?
-
-
-
?
carboxymethyl-pachyman + H2O
?
carboxymethylated curdlan + H2O
?
-
-
-
?
carboxymethylated pachyman + H2O
?
-
-
-
?
carboxymethylated pachyman + H2O
D-glucose + ?
carboxymethylated pachyman + H2O
oligoglucosides
-
86% of activity compared to laminarin from Laminaria digitata
-
-
?
carboxymethylcellulose + H2O
?
cell wall glucan + H2O
reducing sugar + ?
cellobiose + H2O
2 D-glucose
-
0.61% activity compared to laminarin
-
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
-
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotriose + H2O
cellobiose + D-glucose
-
-
-
-
?
cellulose + H2O
?
-
80.55% activity compared to laminarin
-
-
?
curdlan + H2O
D-glucose + laminaritriose + laminaribiose
-
-
-
-
?
curdlan + H2O
glucobiose + glucotriose
curdlan + H2O
laminaribiose + laminaritriose
curdlan + H2O
laminarioligosaccharides + laminaribiose
curdlan + H2O
laminaritriose + laminaribiose
gentiobiose + H2O
?
-
0.61% activity compared to laminarin
-
-
?
Glc-beta-(1->4)-Glc-beta-(1->3)-Glc-beta-(1->4)-Glc + H2O
D-glucose + Glc-beta-(1->4)-Glc-beta-(1->3)-Glc
insoluble yeast glucan + H2O
?
-
-
-
-
?
laminaran from Laminaria cichorioides + H2O
D-glucose + ?
Laminaria digitata laminarin + H2O
laminarioligosaccharides
laminariheptaose + H2O
laminaripentaose + laminaribiose
laminarihexaose + H2O
laminaritetraose + laminaribiose
laminarihexose + H2O
laminaritriose + laminaritetraose
active with the wild-type enzyme, but also the active site mutant E259A, that shows residual activity in the substrate complex crystal and cleaves the substrate in two different ways, generating trisaccharides and tetrasaccharides, mass spectrometry
laminaritriose shows higher binding affinity and fully occupies the -1, -2 and -3 sites of the active-site cleft, even at a low molar excess of the substrate. At elevated substrate concentration laminaritetrose also occupies the active site, spanning the opposite sites +1, +2, +3 and +4 of the cleft
-
?
laminarin + H2O
D-glucose + ?
laminarin + H2O
D-glucose + laminaribiose
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
laminarin + H2O
D-glucose + laminaribiose + ?
-
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose
laminarin + H2O
D-glucose + laminarioligosaccharides
laminarin + H2O
laminaribiose + beta-D-glucose
laminarin + H2O
laminaribiose + laminaritriose
laminarin + H2O
laminaribiose + laminaritriose + laminaritetraose
laminarin + H2O
laminaritriose
preferred substrate
main product
-
?
laminarin + H2O
laminaritriose + ?
laminarin + H2O
laminaritrisaccharides + laminaritetrasaccharides
laminarin + H2O
laminoarioligosaccharides
-
-
-
?
laminarin from Eisenia bicyclis + H2O
oligoglucosides
-
9% of activity compared to laminarin from Laminaria digitata
-
-
?
laminarin from Laminaria digitata + H2O
oligoglucosides
-
-
mixture with different chain length
-
?
laminarioligosaccharide + H2O
D-glucose + laminaribiose + laminaritriose
CaLam digests laminarin and laminarioligosaccharides except laminaribiose as an endo-beta-1,3-glucanase, releasing glucose, laminaribiose and laminaritriose as the major products
-
-
?
laminarioligosaccharide + H2O
laminaribiose + beta-D-glucose
laminaripentaose + H2O
D-glucose + laminaritriose + laminaribiose
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
laminaripentaose + H2O
laminaritetraose + ?
laminaripentaose + H2O
laminaritriose + laminaribiose
-
-
-
-
?
laminaritetraose + H2O
2 laminaribiose
-
-
-
?
laminaritetraose + H2O
D-glucose + ?
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
laminaritetraose + H2O
laminaritriose + ?
laminaritriose + H2O
D-glucose + ?
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
laminaritriose + H2O
D-glucose + laminaribiose
lentinan + H2O
?
4.4% of the activity with laminarin
-
-
?
lichenan + H2O
D-glucose + ?
lichenin from Cetraria islandica + H2O
oligoglucosides
-
6% of activity compared to laminarin from Laminaria digitata
-
-
?
mycolaminarin + H2O
reducing sugar
-
highest activity
no glucose release, approximately four glycosidic linkages hydrolyzed per molecule mycolaminarin, predominant product are tetrasaccharides
?
O-carboxymethyl-(1,3:1,6)-beta-D-glucan + H2O
?
O-carboxymethyl-pachyman + H2O
?
oat glucan + H2O
?
-
15% activity compared to laminarin
-
-
?
pachyman + H2O
D-glucose + ?
pendulan + H2O
reducing sugar + ?
-
acts in random fashion, reaction product with high molecular weight, major role in decreasing the molecular weight of pendulan during fermentation
-
?
periodate-oxidized laminaran + H2O
?
Littorina kurila
-
95% of the rate with laminaran
-
-
?
periodate-oxidized laminaran + H2O
D-glucose + ?
periodate-oxidized laminarin + H2O
?
polysaccharide + H2O
ethanol-soluble sugar + ?
-
crude fraction from unripe bananas, not active in polysaccharide fraction from ripe bananas, possible involvement in ripening and/or softening process
-
?
reduced laminarihexaose + H2O
?
-
-
-
-
?
reduced laminarin + H2O
laminarioligosaccharides
reduced laminarin + H2O
laminaritriose + laminaritetraose + laminari-oligosaccharides
reduced laminarioligosaccharide + H2O
?
-
19 glucose units
-
-
?
reduced laminarioligosaccharides + H2O
laminaribiose + laminaritriose + laminaritetraose + laminaripentaose
-
velocity of catalytic reaction increases with the number of 1,3-beta-glucosidic bonds, preferentially cleaves between the glucose residues at positions 2 and 3 from the reducing end
-
?
scleroglucan + H2O
?
-
low activity
-
?
short-chain pachyman + H2O
?
-
low affinity
-
?
sophorose + H2O
?
-
0.11% activity compared to laminarin
-
-
?
yeast beta-D-glucan + H2O
laminaritriose + laminari-oligosaccharides
-
-
-
?
zymosan + H2O
?
beta-(1->3)-glucose, substrate from Saccharomyces cerevisiae, 9.11% activity compared to curdlan
-
-
?
additional information
?
-
(1-3)-beta-D-glucan + H2O
laminaritriose + laminaritetraose
-
if derived from marine organisms, other(1-3)-beta-D-glucans are not substrate
main products
-
?
(1-3)-beta-D-glucan + H2O
laminaritriose + laminaritetraose
-
if derived from marine organisms, other(1-3)-beta-D-glucans are not substrate
main products
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
Flavobacterium dormitator
-
lichenan
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
-
lichenan
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
-
release of cellobiose as main product
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
-
from cereals, limited action, due to action at few consecutive beta-1,3-linked glucose residues
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
-
very low activity
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
-
lichenan
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
-
lichenan
-
?
2 laminaripentaose + H2O
octasaccharide + ?
transglycosylation activity, product is a linear beta-1,3-octasaccharide containing an intrachain beta-1,6 linkage
-
-
?
2 laminaripentaose + H2O
octasaccharide + ?
transglycosylation activity, product is a linear beta-1,3-octasaccharide containing an intrachain beta-1,6 linkage
-
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
Flavobacterium dormitator
-
releases laminaribiose and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
Flavobacterium dormitator
-
laminaritriose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritriose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
-
releases laminaribiose and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritriose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
-
smallest substrate, products are smaller oligosaccharides and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritriose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritriose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
low activity
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
end-products are laminaritriose, laminaribiose and glucose, exhibits weak glucosyltransferase activity
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
release of laminaritriose and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
low activity
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
end-product laminaribiose, no glucose release
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
products are smaller oligosaccharides and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
low activity
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
end-products laminaritriose and laminaribiose, no glucose release
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminarihexaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
main product laminaritriose, small amounts laminaritriose and laminaribiose, no glucose release
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminarihexaose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
Flavobacterium dormitator
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
2% of activity compared to laminaran from Laminaria cichorioides
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
7% of activity compared to laminaran from Laminaria cichorioides
-
-
?
avicel + H2O
?
-
-
-
?
avicel + H2O
?
i.e. microcrystalline cellulose
-
-
?
avicel + H2O
?
i.e. microcrystalline cellulose
-
-
?
avicel + H2O
?
-
85.92% activity compared to laminarin
-
-
?
avicel + H2O
?
microcrystalline cellulose
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
40.18% activity compared to laminarin
-
-
?
barley beta-glucan + H2O
?
-
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
16.20% activity compared to curdlan
-
-
?
barley beta-glucan + H2O
?
16.20% activity compared to curdlan
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
highest activity
-
-
?
barley beta-glucan + H2O
?
-
highest activity
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
main linkage type beta-1,3-1,4(Glc), about 10% of the specific activity compared to laminarin
-
-
?
barley beta-glucan + H2O
?
-
-
-
-
?
beta-1,3-glucan + H2O
?
-
sources: Pediococcus parvalus and yeast
-
-
?
beta-1,3-glucan + H2O
?
-
sources: Pediococcus parvalus and yeast
-
-
?
beta-1,3-glucan + H2O
?
-
25% of the activity with curdlan
-
-
?
beta-1,3-glucan + H2O
?
-
25% of the activity with curdlan
-
-
?
beta-1,3-glucan + H2O
laminaribiose + D-glucose
-
-
-
?
beta-1,3-glucan + H2O
laminaribiose + D-glucose
-
-
-
?
beta-D-glucan + H2O
?
Flavobacterium dormitator
-
-
-
-
?
beta-D-glucan + H2O
?
-
-
-
?
beta-D-glucan + H2O
?
-
-
-
?
beta-glucan + H2O
?
-
from yeast
-
?
beta-glucan + H2O
?
-
beta-glucanases I and II differ in substrate affinity according to the degree of its polymerization, complete degradation of yeast glucan is determined by synergistic activities of more than one beta-glucanase
-
?
beta-glucan + H2O
?
-
from yeast
-
?
beta-glucan + H2O
?
-
beta-glucanases I and II differ in substrate affinity according to the degree of its polymerization, complete degradation of yeast glucan is determined by synergistic activities of more than one beta-glucanase
-
?
beta-glucan + H2O
?
-
from barley
-
?
beta-glucan + H2O
?
-
from yeast cell wall
-
?
beta-glucan + H2O
?
Flavobacterium dormitator
-
from yeast
-
?
beta-glucan + H2O
?
-
from barley
-
?
beta-glucan + H2O
?
-
beta-1,3- and beta-1,4-linkages
-
?
beta-glucan + H2O
?
-
major product cellobiose
-
?
beta-glucan + H2O
?
Fungi imperfecti
-
from yeast
-
?
beta-glucan + H2O
?
Fungi imperfecti
-
beta-1,3-glucanase of the random type, producing more higher oligosaccharides
-
?
beta-glucan + H2O
?
-
low activity
-
?
beta-glucan + H2O
?
-
from yeast
-
?
beta-glucan + H2O
?
-
from cell wall polysaccharide extracts of fruits or from barley, activites and substrate specificities of enzymes from different cultivars, overview
-
-
?
beta-glucan + H2O
?
-
from yeast
-
?
beta-glucan + H2O
?
-
from oat
-
?
beta-glucan + H2O
?
-
from yeast
-
-
?
beta-glucan + H2O
?
-
low activity
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
low activity
-
?
beta-glucan + H2O
?
-
from yeast
-
?
beta-glucan + H2O
?
-
from yeast
-
?
beta-glucan + H2O
?
-
rapid reduction up to 60% on the turbidity of substrate suspension, slow and very little release of glucose and reducing sugars
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
31.2% activity
-
?
beta-glucan + H2O
?
-
from yeast
-
?
beta-glucan + H2O
?
Barley beta-glucan, 1,3-1,4-beta-glucose monomers, high activity
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
macro- and micro-assay method development and evaluation, overview
-
-
?
beta-glucan + H2O
?
-
from yeast
-
?
beta-glucan + H2O
?
-
beta-1,3- and beta-1,4-linkages
-
?
beta-glucan + H2O
?
-
-
-
-
?
beta-glucan + H2O
?
-
macro- and micro-assay method development and evaluation, overview
-
-
?
beta-glucan + H2O
?
-
from yeast
-
?
callose + H2O
?
-
-
-
-
?
carboxy-methylated pachyman + H2O
?
-
-
-
-
?
carboxy-methylated pachyman + H2O
?
-
-
-
-
?
carboxymethyl curdlan + H2O
?
13.7% of the activity with laminarin
-
-
?
carboxymethyl curdlan + H2O
?
-
-
-
?
carboxymethyl pachyman + H2O
?
-
135% of the activity with laminarin
-
-
?
carboxymethyl pachyman + H2O
?
-
135% of the activity with laminarin
-
-
?
carboxymethyl pachyman + H2O
?
9.1% of the activity with laminarin
-
-
?
carboxymethyl-pachyman + H2O
?
-
-
-
?
carboxymethyl-pachyman + H2O
?
-
-
-
-
?
carboxymethyl-pachyman + H2O
?
1.7% activity compared to laminarin
-
-
?
carboxymethylated pachyman + H2O
D-glucose + ?
Eulota maakii
-
7% of activity compared to laminaran from Laminaria cichorioides
-
-
?
carboxymethylated pachyman + H2O
D-glucose + ?
-
14% of activity compared to laminaran from Laminaria cichorioides
-
-
?
carboxymethylated pachyman + H2O
D-glucose + ?
-
24% of activity compared to laminaran from Laminaria cichorioides
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from Fusarium oxysporum f. sp. apii, possible inducible antimicrobial defense system in plants
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from yeast
-
?
cell wall glucan + H2O
reducing sugar + ?
-
putative role during cell wall morphogenesis
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from fungi
-
?
cell wall glucan + H2O
reducing sugar + ?
Flavobacterium dormitator
-
living yeast cells
-
?
cell wall glucan + H2O
reducing sugar + ?
Fungi imperfecti
-
living yeast cells
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from Phytophthora megasperma, carbohydrate release to elicit glyceollin accumulation in cotyledons
-
?
cell wall glucan + H2O
reducing sugar + ?
-
-
-
?
cell wall glucan + H2O
reducing sugar + ?
-
living yeast cells
-
?
cell wall glucan + H2O
reducing sugar + ?
-
cell wall autolysis
-
?
cell wall glucan + H2O
reducing sugar + ?
-
involved in modification and limited degradation of the cell wall during cell life cycle
-
?
cell wall glucan + H2O
reducing sugar + ?
-
cell wall autolysis
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from different fungi, containing beta-1,3-, beta-1,4 and/or beta-1,6-linkages
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from yeast and different fungi, slight activity, involvement in mycoparasitism
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from yeast
-
?
chitin + H2O
?
-
-
-
?
curdlan + H2O
?
-
-
-
-
?
curdlan + H2O
?
-
-
-
-
?
curdlan + H2O
?
-
insoluble reduced 1,3-beta-glucan
-
?
curdlan + H2O
?
9.1% of the activity with laminarin
-
-
?
curdlan + H2O
?
-
from Alcaligenes faecalis
-
?
curdlan + H2O
?
-
insoluble reduced 1,3-beta-glucan
-
?
curdlan + H2O
?
-
-
-
-
?
curdlan + H2O
?
100% activity. When curdlan is used as the substrate, hydrolysis products mainly range from glucose to tetrasaccharide
-
-
?
curdlan + H2O
?
100% activity. When curdlan is used as the substrate, hydrolysis products mainly range from glucose to tetrasaccharide
-
-
?
curdlan + H2O
?
-
54.6% activity compared to laminarin
-
-
?
curdlan + H2O
glucobiose + glucotriose
degradation
-
-
?
curdlan + H2O
glucobiose + glucotriose
beta-(1->3)-(glucose), substrate from Agrobacterium sp., recombinant CcGluE hydrolyses curdlan powder effectively. The hydrolytic products of curdlan are glucan oligosaccharides with degrees of polymerisation of 2-13, and the main products are glucobiose and glucotriose, overview
-
-
?
curdlan + H2O
glucobiose + glucotriose
degradation
-
-
?
curdlan + H2O
laminaribiose + laminaritriose
100% activity
-
-
?
curdlan + H2O
laminaribiose + laminaritriose
100% activity
-
-
?
curdlan + H2O
laminaribiose + laminaritriose
-
-
-
?
curdlan + H2O
laminaribiose + laminaritriose
-
-
-
?
curdlan + H2O
laminarioligosaccharides + laminaribiose
-
the enzyme hydrolyzes selectively curdlan containing only beta-1,3 linkages
hydrolysis of curdlan powder results in the accumulation of laminaribiose
-
?
curdlan + H2O
laminarioligosaccharides + laminaribiose
-
the enzyme hydrolyzes selectively curdlan containing only beta-1,3 linkages
hydrolysis of curdlan powder results in the accumulation of laminaribiose
-
?
curdlan + H2O
laminaritriose + laminaribiose
-
water-insoluble curdlan, best substrate
main products, plus minor amounts of D-glucose and laminaritetraose
-
?
curdlan + H2O
laminaritriose + laminaribiose
-
water-insoluble curdlan, best substrate
main products, plus minor amounts of D-glucose and laminaritetraose
-
?
Glc-beta-(1->4)-Glc-beta-(1->3)-Glc-beta-(1->4)-Glc + H2O
D-glucose + Glc-beta-(1->4)-Glc-beta-(1->3)-Glc
-
containing one beta-1,4-linkage separated by one beta-1,3-linkage, i.e. G4G3G, which is not further degraded
-
?
Glc-beta-(1->4)-Glc-beta-(1->3)-Glc-beta-(1->4)-Glc + H2O
D-glucose + Glc-beta-(1->4)-Glc-beta-(1->3)-Glc
-
containing one beta-1,4-linkage separated by one beta-1,3-linkage, i.e. G4G3G, which is not further degraded
-
?
laminaran + H2O
?
-
-
-
?
laminaran + H2O
?
Littorina kurila
-
-
-
-
?
laminaran from Laminaria cichorioides + H2O
D-glucose + ?
Eulota maakii
-
-
glucose content in products about 90%
-
?
laminaran from Laminaria cichorioides + H2O
D-glucose + ?
-
-
glucose content in products about 40%
-
?
laminaran from Laminaria cichorioides + H2O
D-glucose + ?
-
-
glucose content in products about 33%, retention of the glycoside bond configuration
-
?
Laminaria digitata laminarin + H2O
laminarioligosaccharides
-
contains a small amount of beta-1,6 linkages compared with curdlan
-
-
?
Laminaria digitata laminarin + H2O
laminarioligosaccharides
-
contains a small amount of beta-1,6 linkages compared with curdlan
-
-
?
laminaribiose + H2O
?
wild-type enzyme performs glucosidase activity on laminarioligosaccharides, while the mutant performs transglycosylation
-
-
?
laminaribiose + H2O
?
wild-type enzyme performs glucosidase activity on laminarioligosaccharides, while the mutant performs transglycosylation
-
-
?
laminaribiose + H2O
?
-
39.24% activity compared to laminarin
-
-
?
laminariheptaose + H2O
?
-
-
-
-
?
laminariheptaose + H2O
?
-
-
-
-
?
laminariheptaose + H2O
?
-
-
-
-
?
laminariheptaose + H2O
laminaripentaose + laminaribiose
-
-
-
-
?
laminariheptaose + H2O
laminaripentaose + laminaribiose
-
-
-
-
?
laminarihexaose + H2O
?
-
-
-
-
?
laminarihexaose + H2O
?
-
-
-
?
laminarihexaose + H2O
?
-
-
-
?
laminarihexaose + H2O
?
-
-
-
?
laminarihexaose + H2O
?
-
-
-
?
laminarihexaose + H2O
?
Flavobacterium dormitator
-
-
-
-
?
laminarihexaose + H2O
laminaritetraose + laminaribiose
-
-
-
-
?
laminarihexaose + H2O
laminaritetraose + laminaribiose
-
-
-
-
?
laminarin + H2O
?
13% of activity compared to barley beta-glucan
-
-
?
laminarin + H2O
?
13% of activity compared to barley beta-glucan
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
best substrate, the enzyme shows an endo-type cleavage mode and hydrolyzes laminarin into glucoses, disaccharides, trioligosaccharides, and tetraoligosaccharides
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
beta-(1->3)-glucose, 44.47% activity compared to curdlan
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
beta-(1->3)-glucose, 44.47% activity compared to curdlan
-
-
?
laminarin + H2O
?
lowest activity
-
-
?
laminarin + H2O
?
-
lowest activity
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
100% activity
-
-
?
laminarin + H2O
?
100% activity
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
47.6% activity compared to curdlan
-
-
?
laminarin + H2O
?
47.6% activity compared to curdlan
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
best substrate
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
72.2% activity compared to curdlan. When laminarin is used as the substrate, major products are a series of beta-1,3-oligosaccharides with degree of polymerization from 1 to 5
-
-
?
laminarin + H2O
?
72.2% activity compared to curdlan. When laminarin is used as the substrate, major products are a series of beta-1,3-oligosaccharides with degree of polymerization from 1 to 5
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
main linkage type beta-1,3-(Glc). The enzyme cleaves laminarin randomly, yielding glucose, laminaribiose, and higher laminari-oligosaccharides
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
1,3-beta-glucose monomers, best substrate
-
-
?
laminarin + H2O
?
-
best substrate, 100% activity
-
-
?
laminarin + H2O
?
substrate from Laminaria digitata
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
the wild-type enzyme displays a bent topology adapted to the binding of helical-shaped laminarin
-
-
?
laminarin + H2O
?
-
-
-
?
laminarin + H2O
?
the wild-type enzyme displays a bent topology adapted to the binding of helical-shaped laminarin
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
best substrate, specific for for 1,3-beta-glucans in which 1,6-beta-linkages are present
-
?
laminarin + H2O
D-glucose + ?
-
100% activity
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
soluble reduced 1,3-beta-glucan, release of reducing 1,3-beta-oligosaccharides of variable size, presence of a single 1,6-beta branched glucose every three glucose units of a linear 1,3-beta-glucan chain prevents hydrolysis
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
strong substrate affinity
-
?
laminarin + H2O
D-glucose + ?
-
specifically hydrolyzes (1-3)-beta-glycosidic linkages, predominant products are laminaribiose and laminaritriose, minor amounts of glucose and higher oligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
major products are glucose, laminaribiose, laminaritriose, laminaritetraose and higher liminarioligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
highly specific to hydrolyse beta-1,3-glycosidic bonds
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
-
?
laminarin + H2O
D-glucose + ?
-
soluble laminarin, no glucose release
-
?
laminarin + H2O
D-glucose + ?
Flavobacterium dormitator
-
major products are glucose, laminaribiose, laminaritriose, laminaritetraose and higher liminarioligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
release of laminarisaccharides with polymerization degree from 1-7
-
?
laminarin + H2O
D-glucose + ?
Fungi imperfecti
-
-
-
?
laminarin + H2O
D-glucose + ?
-
lower activity than on mycolaminarin
-
?
laminarin + H2O
D-glucose + ?
-
devoid of debranching activity, depolymerizes the unbranched portions of the beta-(1-3), beta-(1-6)-glucan, down to laminaritriose, retaining the anomeric configuration
-
?
laminarin + H2O
D-glucose + ?
-
hydrolysis at highest rates by isoform GI, lower hydrolysis by isoform GII, enzyme requires a long run of contiguous beta-1,3-D-glucosidic linkages, where glucosyl units neither substituted nor branched
-
?
laminarin + H2O
D-glucose + ?
-
functional opportunities to inhibit the advance of pathogenic fungi
-
?
laminarin + H2O
D-glucose + ?
-
major products are glucose, laminaribiose, laminaritriose, laminaritetraose and higher liminarioligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
highest rates from Laminaria digitata, major products are laminaribiose and laminaritriose for isoforms GII and GIII, GI yields predominantly (1-3)-beta-D-oligoglucosides greater than 4 units
-
?
laminarin + H2O
D-glucose + ?
-
end-products are laminarihexaose to laminaritriose, some glucose and little gentiobiose for lytic beta-(1-3)-glucanase I
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
release of laminaritetraose, laminaritriose, laminaribiose and glucose
-
?
laminarin + H2O
D-glucose + ?
-
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
-
?
laminarin + H2O
D-glucose + ?
-
from Laminaria digitata, lower rates are from Laminaria hyperborea and Eisenia bicyclis, best substrates are unbranched (1-3)-beta-D-glucans
-
?
laminarin + H2O
D-glucose + ?
-
end-products are laminaritriose, laminaribiose and glucose
-
?
laminarin + H2O
D-glucose + ?
-
accumulation of the enzyme after inoculation with fungi, involvement in pathogenesis in relation to active plant defense
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
action of enzyme requires oligomers with glucose units more than 9
-
?
laminarin + H2O
D-glucose + ?
-
different product patterns for glucanases I, IIIB, IV and V
-
?
laminarin + H2O
D-glucose + ?
-
major products are laminaribiose and laminaritriose
-
?
laminarin + H2O
D-glucose + ?
-
product distribution consistent of 20% laminaribiose, 30% laminaritriose and 50% higher oligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
specifically hydrolyzes (1-3)-beta-glycosidic linkages, predominant products are laminaribiose and laminaritriose, minor amounts of glucose and higher oligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
specifically hydrolyzes beta-1,3-bonds, final products are glucose, laminaribiose and laminaritetraose
-
?
laminarin + H2O
D-glucose + ?
-
preferred substrate
-
?
laminarin + H2O
D-glucose + ?
-
accumulation of the enzyme after inoculation with fungi, involvement in pathogenesis in relation to active plant defense
-
?
laminarin + H2O
D-glucose + ?
-
very active against substrates containing beta-1,3-linkages, mainly disaccharides and oligosaccharides produced, involvement in mycoparasitism
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
?
laminarin + H2O
D-glucose + ?
-
specifically hydrolyzes beta-1,3-bonds, final products are glucose, laminaribiose and laminaritetraose
-
?
laminarin + H2O
D-glucose + ?
-
only active against glucans containing beta-1,3-linkages
-
?
laminarin + H2O
D-glucose + ?
-
-
-
-
?
laminarin + H2O
D-glucose + ?
-
-
-
-
?
laminarin + H2O
D-glucose + ?
-
highly specific to hydrolyse beta-1,3-glycosidic bonds
-
?
laminarin + H2O
D-glucose + ?
-
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose
CaLam digests laminarin and laminarioligosaccharides except laminaribiose as an endo-beta-1,3-glucanase, releasing glucose, laminaribiose and laminaritriose as the major products
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose
-
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose
-
major products, enzyme most frequently attacks the bond between the 3rd and 4th residue from the non-reducing end
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose
-
major products, enzyme most frequently attacks the bond between the 3rd and 4th residue from the non-reducing end
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
-
-
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
-
-
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
-
-
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
-
-
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
endolytic depolymerization of glucans composed of beta-1,3-linked main chains
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
-
-
if the degree of cleavage of laminarin under exhaustive hydrolysis reaches 74%, the major products are glucose and di-, tri-, and tetrasaccharides
-
?
laminarin + H2O
laminaribiose + beta-D-glucose
-
-
-
-
?
laminarin + H2O
laminaribiose + beta-D-glucose
-
-
-
?
laminarin + H2O
laminaribiose + laminaritriose
-
5% of the activity with curdlan
-
-
?
laminarin + H2O
laminaribiose + laminaritriose
-
5% of the activity with curdlan
-
-
?
laminarin + H2O
laminaribiose + laminaritriose + laminaritetraose
-
-
main reaction products
-
?
laminarin + H2O
laminaribiose + laminaritriose + laminaritetraose
-
-
main reaction products
-
?
laminarin + H2O
laminaribiose + laminaritriose + laminaritetraose
-
-
main reaction products
-
?
laminarin + H2O
laminaritriose + ?
-
the mutant enzyme W203F fused to 1,3-beta-D-glucanase catalytic domain shows a 3.6fold increase in specific activity against laminarin as compared with the 1,3-beta-D-glucanase catalytic domain alone with laminaritriose as the major product
major product
-
?
laminarin + H2O
laminaritriose + ?
-
the mutant enzyme W203F fused to 1,3-beta-D-glucanase catalytic domain shows a 3.6fold increase in specific activity against laminarin as compared with the 1,3-beta-D-glucanase catalytic domain alone with laminaritriose as the major product
major product
-
?
laminarin + H2O
laminaritrisaccharides + laminaritetrasaccharides
laminarin from Saccharina cichorioides with molecular weight of 3.5 kDa
-
-
?
laminarin + H2O
laminaritrisaccharides + laminaritetrasaccharides
laminarin from Saccharina cichorioides with molecular weight of 3.5 kDa
-
-
?
laminarioligosaccharide + H2O
laminaribiose + beta-D-glucose
-
e.g. laminaritetraose
-
-
?
laminarioligosaccharide + H2O
laminaribiose + beta-D-glucose
-
-
-
?
laminarioligosaccharide + H2O
laminaribiose + beta-D-glucose
substrate specificities and products, overview
-
-
?
laminaripentaose + H2O
?
-
-
-
-
?
laminaripentaose + H2O
?
-
-
-
-
?
laminaripentaose + H2O
?
-
-
-
-
?
laminaripentaose + H2O
?
-
-
-
?
laminaripentaose + H2O
?
-
-
-
?
laminaripentaose + H2O
laminaritetraose + ?
efficient hydrolytic activity
-
-
?
laminaripentaose + H2O
laminaritetraose + ?
efficient hydrolytic activity
-
-
?
laminaritetraose + H2O
?
-
-
-
-
?
laminaritetraose + H2O
?
-
-
-
-
?
laminaritetraose + H2O
?
-
smallest substrate accepted
-
-
?
laminaritetraose + H2O
laminaritriose + ?
efficient hydrolytic activity
-
-
?
laminaritetraose + H2O
laminaritriose + ?
efficient hydrolytic activity
-
-
?
laminaritriose + H2O
?
wild-type enzyme performs glucosidase activity on laminarioligosaccharides, while the mutant performs transglycosylation
-
-
?
laminaritriose + H2O
?
wild-type enzyme performs glucosidase activity on laminarioligosaccharides, while the mutant performs transglycosylation
-
-
?
laminaritriose + H2O
D-glucose + laminaribiose
-
-
-
?
laminaritriose + H2O
D-glucose + laminaribiose
-
-
-
?
laminaritriose + H2O
D-glucose + laminaribiose
the smallest oligosaccharide that can be degraded by the enzyme
-
-
?
laminaritriose + H2O
D-glucose + laminaribiose
the smallest oligosaccharide that can be degraded by the enzyme
-
-
?
lichenan + H2O
?
90% of activity compared to barley beta-glucan
-
-
?
lichenan + H2O
?
90% of activity compared to barley beta-glucan
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
1.1% activity compared to laminarin
-
-
?
lichenan + H2O
?
1.1% activity compared to laminarin
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
main linkage type beta-1,3-1,4(Glc), about 10% of the specific activity compared to laminarin
-
-
?
lichenan + H2O
?
1,3-1,4-beta-glucose monomers, high activity
-
-
?
lichenan + H2O
?
substrate from Cetraria islandica
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
lichenan is only hydrolyzed by YlCrh1Sp
-
-
?
lichenan + H2O
D-glucose + ?
-
-
-
?
lichenan + H2O
D-glucose + ?
Eulota maakii
-
16% of activity compared to laminaran from Laminaria cichorioides
-
-
?
lichenan + H2O
D-glucose + ?
-
20% of activity compared to laminaran from Laminaria cichorioides
-
-
?
lichenan + H2O
D-glucose + ?
-
22% of activity compared to laminaran from Laminaria cichorioides
-
-
?
O-carboxymethyl-(1,3:1,6)-beta-D-glucan + H2O
?
-
from yeast, low activity
-
?
O-carboxymethyl-(1,3:1,6)-beta-D-glucan + H2O
?
-
from yeast, low activity
-
?
O-carboxymethyl-pachyman + H2O
?
-
release of laminarisaccharides ranging in polymerization degree from 1-7
-
?
O-carboxymethyl-pachyman + H2O
?
-
-
-
?
O-carboxymethyl-pachyman + H2O
?
-
faster hydrolysis by isoform GII than by isoform GI, isoform GII may play a role in response to fungal infection
-
?
O-carboxymethyl-pachyman + H2O
?
-
-
-
?
O-carboxymethyl-pachyman + H2O
?
-
rate of hydrolysis decreases as degree of substitutions increases, requirement for three unsubstituted beta-1,3-glycosyl residues
-
?
O-carboxymethyl-pachyman + H2O
?
-
unbranched (1-3)-beta-glucan from Poria cocos
-
?
O-carboxymethyl-pachyman + H2O
?
-
preferred substrate
-
?
pachyman + H2O
?
-
78.86% ctivity compared to laminarin
-
-
?
pachyman + H2O
?
Flavobacterium dormitator
-
-
-
?
pachyman + H2O
?
-
release of laminarisaccharides in polymerization degree form 1-7
-
?
pachyman + H2O
?
Fungi imperfecti
-
-
-
?
pachyman + H2O
?
most favored substrate, 223% activity compared to curdlan
-
-
?
pachyman + H2O
?
most favored substrate, 223% activity compared to curdlan
-
-
?
pachyman + H2O
?
14.9% of the activity with laminarin
-
-
?
pachyman + H2O
?
-
-
-
-
?
pachyman + H2O
?
-
-
-
-
?
pachyman + H2O
?
-
insoluble pachyman, more affinity than on soluble, short-chain pachyman, forms L-1 and L-2 release predominantly pentaose, form L-4 yields a mixture from biose to heptaose
-
?
pachyman + H2O
?
-
low activity
-
?
pachyman + H2O
?
substrate from Poria cocos
-
-
?
pachyman + H2O
?
-
-
-
-
?
pachyman + H2O
?
-
-
-
-
?
pachyman + H2O
?
-
5% of the activity with curdlan
-
-
?
pachyman + H2O
?
-
5% of the activity with curdlan
-
-
?
pachyman + H2O
D-glucose + ?
-
10% of activity compared to laminaran from Laminaria cichorioides
-
-
?
pachyman + H2O
D-glucose + ?
-
13% of activity compared to laminaran from Laminaria cichorioides
-
-
?
paramylon + H2O
?
-
23.4% of the activity with laminarin
the enzyme effectively produces soluble beta-1,3-glucans from alkaline-treated Euglena freeze-dried powder containing paramylon
-
?
paramylon + H2O
?
-
-
-
-
?
paramylon + H2O
?
-
action of endo-beta-1,3-glucanase on the microwave-pretreated paramylon produces soluble beta-1,3-glucans with degrees of polymerisation (DP) ranging from 2-59
-
-
?
periodate-oxidized laminaran + H2O
D-glucose + ?
Eulota maakii
-
0.5% of activity compared to laminaran from Laminaria cichorioides
-
-
?
periodate-oxidized laminaran + H2O
D-glucose + ?
-
90% of activity compared to laminaran from Laminaria cichorioides
-
-
?
periodate-oxidized laminaran + H2O
D-glucose + ?
-
85% of activity compared to laminaran from Laminaria cichorioides
-
-
?
periodate-oxidized laminarin + H2O
?
-
-
-
?
periodate-oxidized laminarin + H2O
?
-
-
-
-
?
periodate-oxidized laminarin + H2O
?
Flavobacterium dormitator
-
-
-
?
periodate-oxidized laminarin + H2O
?
-
-
-
?
periodate-oxidized laminarin + H2O
?
98% activity compared to laminarin
-
-
?
periodate-oxidized laminarin + H2O
?
98% activity compared to laminarin
-
-
?
periodate-oxidized laminarin + H2O
?
-
-
-
?
periodate-oxidized laminarin + H2O
?
-
-
-
?
periodate-oxidized laminarin + H2O
?
-
100% of the activity with laminarin
-
-
?
periodate-oxidized laminarin + H2O
?
-
-
-
?
periodate-oxidized laminarin + H2O
?
-
-
-
?
periodate-oxidized laminarin + H2O
?
-
-
-
?
periodate-oxidized laminarin + H2O
?
-
-
-
?
pustulan + H2O
?
-
beta-1,6-glucan, low activity
-
?
pustulan + H2O
?
-
4% activity compared to laminarin
-
-
?
pustulan + H2O
?
-
enzyme can also cleave beta-1,6 glucans
-
-
?
pustulan + H2O
?
-
beta-1,6-glucan, low activity
-
?
pustulan + H2O
?
-
beta-1,6-glucan, low activity
-
?
pustulan + H2O
?
-
pustulan is only hydrolyzed by YlCrh1Sp
-
-
?
reduced laminarin + H2O
laminarioligosaccharides
-
-
-
?
reduced laminarin + H2O
laminarioligosaccharides
-
-
-
?
reduced laminarin + H2O
laminaritriose + laminaritetraose + laminari-oligosaccharides
high hydrolytic activity
-
-
?
reduced laminarin + H2O
laminaritriose + laminaritetraose + laminari-oligosaccharides
high hydrolytic activity
-
-
?
schizophyllan + H2O
?
-
from Schizophyllum commune, low activity
-
?
schizophyllan + H2O
?
-
low activity
-
?
schizophyllan + H2O
?
-
-
-
-
?
schizophyllan + H2O
?
-
from Schizophyllum commune, low activity
-
?
schizophyllan + H2O
?
-
-
-
-
?
translam + H2O
?
Littorina kurila
-
86% of the rate with laminaran
-
-
?
translam + H2O
?
-
32.1% of the activity with laminarin
-
-
?
zymosan A + H2O
?
-
-
-
?
zymosan A + H2O
?
-
-
-
-
?
zymosan A + H2O
?
-
-
-
?
zymosan A + H2O
?
-
-
-
?
additional information
?
-
-
no activity towards chitosan, lichenan, carboxymethylcellulose, amylose, and p-nitrophenyl beta-D-glucopyranoside
-
-
?
additional information
?
-
-
the enzyme exerts relatively high specific activity toward the glucans comprising beta-1,3-glycosidic bond, such as laminarin, pachyman, and barley beta-glucan, with relative activity of 100%, 78.86%, and 40.18%, respectively. Low activity with zymosan A, carboxymethylcellulose-Na, and agarose
-
-
?
additional information
?
-
-
AkLam36 specific for beta-1,3-glucosyl linkages. AkLam36 is an endolytic enzyme degrading laminarin and laminarioligosaccharides to laminaritriose, laminaribiose, and D-glucose. AkLam36 shows higher activity toward beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin than highly branched beta-1,3-glucans such as Eisenia bicyclis laminarin
-
-
?
additional information
?
-
-
enzyme preferentially acts on soluble beta-1,3-glucans. Additional transferase activity for oligosaccharides of a low degree of polymerization
-
-
?
additional information
?
-
-
enzyme is involved in the autolytic cell wall degradation resulting from carbon starvation of the fungus and liberates reducing sugars from cell debris
-
-
?
additional information
?
-
-
enzyme hydrolyzes soluble and insoluble (1-3)-beta-D-glucan chains
-
-
?
additional information
?
-
-
no substrate: pustulan, p-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
-
no substrate: laminaribiose or laminaritriose, carboxymethyl cellulose, chitin, and pustulan
-
-
?
additional information
?
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, and the highest catalytic activity for curdlan. The enzyme exerts beta-(1->3)-glucan-degrading activity
-
-
?
additional information
?
-
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, and the highest catalytic activity for curdlan. The enzyme exerts beta-(1->3)-glucan-degrading activity
-
-
?
additional information
?
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, e.g. chitosan from crab shell and water-soluble starch from Ipomoea batatas, and the highest catalytic activity for curdlan. Degradation mode analysis indicates that CcGluE is more likely to hydrolyse glucopentaose and reveals that CcGluE is an endoglucanase. Curdlan is insoluble because of its special structure, which greatly limits the efficiency of the enzyme degradation of curdlan, but a homogenising pre-treatment method with curdlan, improves the degradation efficiency of CcGluE for curdlan powder by 7.1fold, overview. No activity with inulin, microcrystalline cellulose, carboxymethylcellulose, gel-chitin, and alpha-chitin
-
-
?
additional information
?
-
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, e.g. chitosan from crab shell and water-soluble starch from Ipomoea batatas, and the highest catalytic activity for curdlan. Degradation mode analysis indicates that CcGluE is more likely to hydrolyse glucopentaose and reveals that CcGluE is an endoglucanase. Curdlan is insoluble because of its special structure, which greatly limits the efficiency of the enzyme degradation of curdlan, but a homogenising pre-treatment method with curdlan, improves the degradation efficiency of CcGluE for curdlan powder by 7.1fold, overview. No activity with inulin, microcrystalline cellulose, carboxymethylcellulose, gel-chitin, and alpha-chitin
-
-
?
additional information
?
-
-
no substrate: laminaribiose or laminaritriose, carboxymethyl cellulose, chitin, and pustulan
-
-
?
additional information
?
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, and the highest catalytic activity for curdlan. The enzyme exerts beta-(1->3)-glucan-degrading activity
-
-
?
additional information
?
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, e.g. chitosan from crab shell and water-soluble starch from Ipomoea batatas, and the highest catalytic activity for curdlan. Degradation mode analysis indicates that CcGluE is more likely to hydrolyse glucopentaose and reveals that CcGluE is an endoglucanase. Curdlan is insoluble because of its special structure, which greatly limits the efficiency of the enzyme degradation of curdlan, but a homogenising pre-treatment method with curdlan, improves the degradation efficiency of CcGluE for curdlan powder by 7.1fold, overview. No activity with inulin, microcrystalline cellulose, carboxymethylcellulose, gel-chitin, and alpha-chitin
-
-
?
additional information
?
-
no substrates: laminaribiose, pustulan, carboxymethyl cellulose
-
-
?
additional information
?
-
the enzyme does not act on substrates containing only beta-1,4-glycosidic bondas (like carboxymethyl cellulose) or beta-1,6-glycosidic bonds (like pustulan)
-
-
?
additional information
?
-
-
the enzyme does not act on substrates containing only beta-1,4-glycosidic bondas (like carboxymethyl cellulose) or beta-1,6-glycosidic bonds (like pustulan)
-
-
?
additional information
?
-
-
the enzyme does not act on substrates containing only beta-1,4-glycosidic bondas (like carboxymethyl cellulose) or beta-1,6-glycosidic bonds (like pustulan)
-
-
?
additional information
?
-
no substrates: laminaribiose, pustulan, carboxymethyl cellulose
-
-
?
additional information
?
-
-
enzyme cleaves cell wall debris of yeast Pichia fermentans, Zygosaccharomyces bailii, Saccharomycodes ludwigii, Dekkera bruxellensis. No substrate: xylan, pustulan, carboxymethyl cellulose, dextran
-
-
?
additional information
?
-
-
enzyme cleaves cell wall debris of yeast Pichia fermentans, Zygosaccharomyces bailii, Saccharomycodes ludwigii, Dekkera bruxellensis. No substrate: xylan, pustulan, carboxymethyl cellulose, dextran
-
-
?
additional information
?
-
-
the enzyme is inducible with a complex plant beta-glucan laminarin from which it releases simple saccharides when supplied to leaves as a substrate
-
-
?
additional information
?
-
-
the enzyme is inducible with a complex plant beta-glucan laminarin from which it releases simple saccharides when supplied to leaves as a substrate
-
-
?
additional information
?
-
-
enzyme additionally catalyzes a transglycosylation reaction by which reaction products with a higher molecular weight than the supplied substrates are initially generated. Ultimately the substrates are degraded into glucose, laminaribiose and laminaritriose
-
-
?
additional information
?
-
Eulota maakii
-
no substrate: pachyman, p-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
-
enzyme catalyzes transfer of the glyconic part of a substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside. Low activity on yeast glucan, no substrates: pachyman and aubasidan, pustulan, pullulan, amylopectin, and carboxymethylcellulose
-
-
?
additional information
?
-
enzyme catalyzes transfer of the glyconic part of a substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside. Low activity on yeast glucan, no substrates: pachyman and aubasidan, pustulan, pullulan, amylopectin, and carboxymethylcellulose
-
-
?
additional information
?
-
-
the enzyme catalyzes transfer of glyconic part of substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside
-
-
?
additional information
?
-
the enzyme catalyzes transfer of glyconic part of substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside
-
-
?
additional information
?
-
-
the enzyme has no ability to degrade pachiman, aubasidan, pustulan, pullulan, amylopectin, and carboxymethyl-cellulose
-
-
?
additional information
?
-
the enzyme has no ability to degrade pachiman, aubasidan, pustulan, pullulan, amylopectin, and carboxymethyl-cellulose
-
-
?
additional information
?
-
-
the enzyme catalyzes transfer of glyconic part of substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside
-
-
?
additional information
?
-
the enzyme catalyzes transfer of glyconic part of substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside
-
-
?
additional information
?
-
-
the enzyme has no ability to degrade pachiman, aubasidan, pustulan, pullulan, amylopectin, and carboxymethyl-cellulose
-
-
?
additional information
?
-
the enzyme has no ability to degrade pachiman, aubasidan, pustulan, pullulan, amylopectin, and carboxymethyl-cellulose
-
-
?
additional information
?
-
-
enzyme catalyzes transfer of the glyconic part of a substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside. Low activity on yeast glucan, no substrates: pachyman and aubasidan, pustulan, pullulan, amylopectin, and carboxymethylcellulose
-
-
?
additional information
?
-
enzyme catalyzes transfer of the glyconic part of a substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside. Low activity on yeast glucan, no substrates: pachyman and aubasidan, pustulan, pullulan, amylopectin, and carboxymethylcellulose
-
-
?
additional information
?
-
-
laminarinase mainly hydrolyses beta?1,3-glycosidic bonds, with negligible activity towards beta-1,4-glycosidic bonds
-
-
?
additional information
?
-
-
laminarinase mainly hydrolyses beta?1,3-glycosidic bonds, with negligible activity towards beta-1,4-glycosidic bonds
-
-
?
additional information
?
-
HdLam33 possesses transglycosylation activity splitting glycoside linkage in a retaining manner, overview. It also shows activity of EC 3.2.1.6, endo-1,3(4)-beta-glucanase
-
-
?
additional information
?
-
-
HdLam33 possesses transglycosylation activity splitting glycoside linkage in a retaining manner, overview. It also shows activity of EC 3.2.1.6, endo-1,3(4)-beta-glucanase
-
-
?
additional information
?
-
-
hydrothermal microwave pretreatment of substrate paramylon at 170 °C for 2 min is established to facilitate the enzymatic production of soluble bioactive beta-1,3-glucans from the recalcitrant substrate paramylon, structure comparisons of paramylon granules with and without heat treatment, overview. Virtual absence of enzymatic hydrolysis of paramylon pretreated at the lower incubation temperatures may be explained by steric hindrance of the enzymes
-
-
?
additional information
?
-
no activity with xylan, colloidal chitin, carboxymethylcellulose, polygalacturonic acid, and pectin
-
-
?
additional information
?
-
no activity with xylan, colloidal chitin, carboxymethylcellulose, polygalacturonic acid, and pectin
-
-
?
additional information
?
-
no substrate: beta-1,3-1,4-glucans such as barley glucan or lichenan, or beta-1,6 glucans such as pustulan
-
-
?
additional information
?
-
Littorina kurila
-
narrow substrate specificity, hydrolyzes only the (1-3)-beta-D-glucosidic bonds in the mixed (1-3),(1-6)- and (1-3),(1-4)-beta-D-glucans down to glucose and glucooligosaccharides. Enzyme acts with retention of the anomeric configuration and additionally catalyzes transglycosylation reactions
-
-
?
additional information
?
-
-
no substrate: starch, cellulose, chitin, chitosan
-
-
?
additional information
?
-
OsGlu1 may act in the defense response to pathogen attack
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-
?
additional information
?
-
OsGlu1 may act in the defense response to pathogen attack
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-
?
additional information
?
-
-
OsGlu1 may act in the defense response to pathogen attack
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?
additional information
?
-
-
no substrate: cellulose, xylan, amylose
-
-
?
additional information
?
-
the catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
-
-
?
additional information
?
-
the catalytic module specifically hydrolyzes beta-1,3- and beta-1,3-1,4-glucan. The catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
-
-
?
additional information
?
-
-
poor substrates: yeast glucan, pachyman, amylopectin, carboxymethy cellulose, and pustulan
-
-
?
additional information
?
-
-
no substrate: starch, cellulose, chitin, chitosan
-
-
?
additional information
?
-
endo-1,3-beta-D-glucanases catalyze the hydrolysis of internal beta-(1,3)-O-glycosidic bonds
-
-
?
additional information
?
-
the enzyme does not display activity towards agarose, pachyman, Zymosan A, barley beta-glucan, and (carboxymethyl)cellulose
-
-
?
additional information
?
-
the enzyme does not display activity towards agarose, pachyman, Zymosan A, barley beta-glucan, and (carboxymethyl)cellulose
-
-
?
additional information
?
-
-
besides endo-activity, enzyme has some exo-activity, and catalyzes hydrolysis of mixed-linked oligosaccharides with both beta-1,3 and beta-1,4 specificities
-
-
?
additional information
?
-
no activity with cellulose, xylan and chitin
-
-
?
additional information
?
-
-
no activity with cellulose, xylan and chitin
-
-
?
additional information
?
-
-
enzyme does not hydrolyze beta-1,4 linkages present in cellooligosaccharides such as cellobiose, cellotriose, cellotetraose and cellopentaose
-
-
?
additional information
?
-
-
the enzyme hardly cleaves the beta-1,3 linkage in laminaribiose
-
-
?
additional information
?
-
the enzyme hardly cleaves the beta-1,3 linkage in laminaribiose
-
-
?
additional information
?
-
-
the enzyme hardly cleaves the beta-1,3 linkage in laminaribiose
-
-
?
additional information
?
-
the enzyme hardly cleaves the beta-1,3 linkage in laminaribiose
-
-
?
additional information
?
-
-
laminaribiose and laminaritriose are no substrates, laminaritetraose is very inefficiently cleaved
-
-
?
additional information
?
-
-
role as a regulator for the acid trehalase activity by association in the enzyme aggregate
-
-
?
additional information
?
-
-
laminaribiose and laminaritriose are no substrates, laminaritetraose is very inefficiently cleaved
-
-
?
additional information
?
-
-
laminaribiose and laminaritriose are no substrates, laminaritetraose is very inefficiently cleaved
-
-
?
additional information
?
-
plant endo-1,3-beta-glucanases hydrolyze (1,3)-beta-glucans, with very limited activity towards mixed (1,3,1,4)-beta-glucans and branched (1,3,1,6)-beta-glucans
-
-
?
additional information
?
-
-
plant endo-1,3-beta-glucanases hydrolyze (1,3)-beta-glucans, with very limited activity towards mixed (1,3,1,4)-beta-glucans and branched (1,3,1,6)-beta-glucans
-
-
?
additional information
?
-
Enzyme shows low processivity of 0.4. No substrate: yeast beta-1,3-1,6-glucan or other polysaccharides. enzyme is unable to lyse Saccharomyces cerevisiae cells
-
-
?
additional information
?
-
no substrates : cellulose, xylan, amylose, starch, beta-cyclodextrin
-
-
?
additional information
?
-
-
no substrates : cellulose, xylan, amylose, starch, beta-cyclodextrin
-
-
?
additional information
?
-
BglS27 preferentially catalyzes the hydrolysis of glucans with a beta-1,3-linkage using an endolytic mode of action
-
-
?
additional information
?
-
no activity with oat spelt xylan and carboxymethyl cellulose
-
-
?
additional information
?
-
-
Eisenia bicyclis laminarin, with a higher amount of beta-1,6-linkages, is no substrate for the enzyme. Trisaccharide is inevitably released from the hydrolysis of laminarioligosaccharides with 5 to 7 degrees of polymerization. Although the enzyme cleaves off disaccharide from tetrasaccharide, the reaction rate is lower than those of laminaripentaose to laminariheptaose. The results indicate that the active site of Mo endo-beta-1,3-glucanase can efficiently recognize glucosyl residue chain of greater than laminaripentaose and hydrolyzes the beta-1,3 linkage between the 3rd and 4th glucosyl residue
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-
?
additional information
?
-
-
Eisenia bicyclis laminarin, with a higher amount of beta-1,6-linkages, is no substrate for the enzyme. Trisaccharide is inevitably released from the hydrolysis of laminarioligosaccharides with 5 to 7 degrees of polymerization. Although the enzyme cleaves off disaccharide from tetrasaccharide, the reaction rate is lower than those of laminaripentaose to laminariheptaose. The results indicate that the active site of Mo endo-beta-1,3-glucanase can efficiently recognize glucosyl residue chain of greater than laminaripentaose and hydrolyzes the beta-1,3 linkage between the 3rd and 4th glucosyl residue
-
-
?
additional information
?
-
the enzyme is an endoglucanase that hydrolyzes beta-1,3-glucans as laminarin and yeast beta-1,3-1,6-glucan, but is inactive toward other polysaccharides, e.g. unbranched beta-1,3-glucans or mixed beta-1,3-1,4-glucan from cereals, or disaccharides
-
-
?
additional information
?
-
-
the enzyme is an endoglucanase that hydrolyzes beta-1,3-glucans as laminarin and yeast beta-1,3-1,6-glucan, but is inactive toward other polysaccharides, e.g. unbranched beta-1,3-glucans or mixed beta-1,3-1,4-glucan from cereals, or disaccharides
-
-
?
additional information
?
-
-
substrate specificities of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
substrate specificities of wild-type and mutant enzymes, overview
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-
?
additional information
?
-
specific cleavage of internal beta-1,3-bonds. No substrate: avicel, carboxymethyl cellulose and cellopentaose, xylan, arabinan and manan containing polysaccharides
-
-
?
additional information
?
-
-
specific cleavage of internal beta-1,3-bonds. No substrate: avicel, carboxymethyl cellulose and cellopentaose, xylan, arabinan and manan containing polysaccharides
-
-
?
additional information
?
-
specific cleavage of internal beta-1,3-bonds. No substrate: avicel, carboxymethyl cellulose and cellopentaose, xylan, arabinan and manan containing polysaccharides
-
-
?
additional information
?
-
-
specifically cleaves beta-1,3-linkages in polysaccharides
-
-
?
additional information
?
-
-
specifically cleaves beta-1,3-linkages in polysaccharides
-
-
?
additional information
?
-
-
YlCrh2Sp does not hydrolyze carboxymethyl-cellulose, pustulan, and lichenan
-
-
?
additional information
?
-
the enzyme specifically cleaves beta-1,4-linkages next to beta-1,3-linkages and is active on linear 1,3-beta-D-glucans with 3-6 monomers and on a glucan tetrasaccharide containing two beta-1,4-linkages separated by one beta-1,3-linkage. The activity towards beta-1,4-linkages is much lower than towards beta-1,3-linkages. Enzyme-substrate complex structure analysis using wild-type and mutant enzymes with glucan oligomers, binding structure and substrate recognition, overview
-
-
?
additional information
?
-
-
the enzyme specifically cleaves beta-1,4-linkages next to beta-1,3-linkages and is active on linear 1,3-beta-D-glucans with 3-6 monomers and on a glucan tetrasaccharide containing two beta-1,4-linkages separated by one beta-1,3-linkage. The activity towards beta-1,4-linkages is much lower than towards beta-1,3-linkages. Enzyme-substrate complex structure analysis using wild-type and mutant enzymes with glucan oligomers, binding structure and substrate recognition, overview
-
-
?
additional information
?
-
the enzyme specifically cleaves beta-1,4-linkages next to beta-1,3-linkages and is active on linear 1,3-beta-D-glucans with 3-6 monomers and on a glucan tetrasaccharide containing two beta-1,4-linkages separated by one beta-1,3-linkage. The activity towards beta-1,4-linkages is much lower than towards beta-1,3-linkages. Enzyme-substrate complex structure analysis using wild-type and mutant enzymes with glucan oligomers, binding structure and substrate recognition, overview
-
-
?
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Arthritis, Rheumatoid
Role of Glutamine-Glutamate/GABA cycle and potential target GLUD2 in alleviation of rheumatoid arthritis by Tripterygium hypoglaucum (levl.) Hutch based on metabolomics and molecular pharmacology.
Asthma, Occupational
Report of occupational asthma due to phytase and beta-glucanase.
Asthma, Occupational
Response to a case of occupational asthma due to the enzymes phytase and beta-glucanase.
Ataxia
D-Serine regulates cerebellar LTD and motor coordination through the ?2 glutamate receptor.
Ataxia
Epilepsy with myoclonic atonic seizures and chronic cerebellar symptoms associated with antibodies against glutamate receptors N2B and D2 in serum and cerebrospinal fluid.
Ataxia
The low binding affinity of D-serine at the ionotropic glutamate receptor GluD2 can be attributed to the hinge region.
Ataxia
The N-terminal domain of GluD2 (GluRdelta2) recruits presynaptic terminals and regulates synaptogenesis in the cerebellum in vivo.
Atypical Squamous Cells of the Cervix
{beta}-glucanase Eng2 is required for ascus wall endolysis after sporulation in the fission yeast Schizosaccharomyces pombe.
Autoimmune Diseases
Role of Glutamine-Glutamate/GABA cycle and potential target GLUD2 in alleviation of rheumatoid arthritis by Tripterygium hypoglaucum (levl.) Hutch based on metabolomics and molecular pharmacology.
Bradycardia
Involvement of GluD2 in Fear-Conditioned Bradycardia in Mice.
Coccidiosis
Effects of exogenous ?-glucanase on ileal digesta soluble ?-glucan molecular weight, digestive tract characteristics, and performance of coccidiosis vaccinated broiler chickens fed hulless barley-based diets with and without medication.
Glioblastoma
Mitochondrial enzyme GLUD2 plays a critical role in glioblastoma progression.
Glioma
Hominoid-specific enzyme GLUD2 promotes growth of IDH1R132H glioma.
Glioma
Mitochondrial enzyme GLUD2 plays a critical role in glioblastoma progression.
glucan endo-1,3-beta-d-glucosidase deficiency
Physiological compensation in antisense transformants: specific induction of an "ersatz" glucan endo-1,3-beta-glucosidase in plants infected with necrotizing viruses.
Hypersensitivity
Ksg1, a homologue of the phosphoinositide-dependent protein kinase 1, controls cell wall integrity in Schizosaccharomyces pombe.
Hypersensitivity
Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit.
Hypersensitivity
Occupational allergy in a researcher due to Ole e 9, an allergenic 1,3-beta-glucanase from olive pollen.
Hypersensitivity
Prophylactic intranasal treatment with fragments of 1,3-beta-glucanase olive pollen allergen prevents airway inflammation in a murine model of type I allergy.
Hypersensitivity
The C-terminal segment of the 1,3-beta-glucanase Ole e 9 from olive (Olea europaea) pollen is an independent domain with allergenic activity: expression in Pichia pastoris and characterization.
Infections
A novel tissue-specific plantain beta-1,3-glucanase gene that is regulated in response to infection by Fusarium oxysporum fsp. cubense.
Infections
An alpha-glucan elicitor from the cell wall of a biocontrol binucleate Rhizoctonia isolate.
Infections
Analysis of regulatory elements involved in stress-induced and organ-specific expression of tobacco acidic and basic beta-1,3-glucanase genes.
Infections
Coordinated expression of defense-related genes by TMV infection or salicylic acid treatment in tobacco.
Infections
Differential in vitro DNA binding activity to a promoter element of the gn1 beta-1,3-glucanase gene in hypersensitively reacting tobacco plants.
Infections
Differential induction and accumulation of beta-1,3-glucanase and chitinase isoforms in soybean hypocotyls and leaves after compatible and incompatible infection with Phytophthora megasperma f.sp. glycinea.
Infections
Differential Regulation of beta-1,3-Glucanase Messenger RNAs in Response to Pathogen Infection.
Infections
Disease development and beta-1,3-glucanase expression following leaf rust infection in resistant and susceptible near-isogenic wheat seedlings.
Infections
Effects of Cellulytic Enzymes on Phytophthora cinnamomi.
Infections
Effects of cellulytic enzymes on Phytophthora cinnamomi.
Infections
Ethylene: Symptom, Not Signal for the Induction of Chitinase and beta-1,3-Glucanase in Pea Pods by Pathogens and Elicitors.
Infections
Extracellular beta-1,3-Glucanases in Stem Rust-Affected and Abiotically Stressed Wheat Leaves : Immunocytochemical Localization of the Enzyme and Detection of Multiple Forms in Gels by Activity Staining with Dye-Labeled Laminarin.
Infections
Genes encoding acidic and basic class III beta-1,3-glucanases are expressed in tomato plants upon viroid infection.
Infections
Genes involved in adult plant resistance to stripe rust in wheat cultivar Xingzi 9104
Infections
Greenhouse and field testing of transgenic wheat plants stably expressing genes for thaumatin-like protein, chitinase and glucanase against Fusarium graminearum.
Infections
Identification and partial characterization of beta-1,3-glucanase from virus-infected cucumber cotyledons.
Infections
Immunogold localization of an extracellular beta-1,3-glucanase of the ergot fungus Claviceps purpurea during infection of rye.
Infections
Induction and differential expression of beta-1,3-glucanase mRNAs in tolerant and susceptible Hevea clones in response to infection by Phytophthora meadii.
Infections
Induction by pathogen, salt and drought of a basic class II chitinase mRNA and its in situ localization in pepper (Capsicum annuum).
Infections
Induction of beta-1,3-glucanase in barley in response to infection by fungal pathogens.
Infections
Induction of beta-1,3-glucanase in seedlings of pearl millet in response to infection by Sclerospora graminicola.
Infections
Induction of different chitinase and beta-1,3-glucanase isoenzymes in sunflower (Helianthus annuus L.) seedlings in response to infection by Plasmopara halstedii.
Infections
Induction of resistance in host against the infection of leaf blight pathogen (Alternaria palandui) in onion (Allium cepa var aggregatum).
Infections
Isoform patterns of chitinase and beta-1,3-glucanase in maturing corn kernels (Zea mays L.) associated with Aspergillus flavus milk stage infection.
Infections
Molecular cloning of a soybean class III beta-1,3-glucanase gene that is regulated both developmentally and in response to pathogen infection.
Infections
Molecular size and net charge of pathogenesis-related enzymes from barley (Hordeum vulgare L., v. Karat) infected with Drechslera teres f. teres (Sacch.) Shoem.
Infections
Optimization of RQRT-pCR protocols to measure beta-1,3-glucanase mRNA levels in infected tissues of rubber tree (Hevea brasiliensis).
Infections
Overexpression of defense response genes in transgenic wheat enhances resistance to Fusarium head blight.
Infections
Pepper gene encoding a basic beta-1,3-glucanase is differentially expressed in pepper tissues upon pathogen infection and ethephon or methyl jasmonate treatment.
Infections
Physiological compensation in antisense transformants: specific induction of an "ersatz" glucan endo-1,3-beta-glucosidase in plants infected with necrotizing viruses.
Infections
Potato virus Y induced changes in the gene expression of potato (Solanum tuberosum L.).
Infections
Primary structure and expression of mRNAs encoding basic chitinase and 1,3-beta-glucanase in potato.
Infections
Scientifically advanced solutions for chestnut ink disease.
Infections
The function of vacuolar beta-1,3-glucanase investigated by antisense transformation. Susceptibility of transgenic Nicotiana sylvestris plants to Cercospora nicotianae infection.
Infections
Tissue-specific and pathogen-induced regulation of a Nicotiana plumbaginifolia beta-1,3-glucanase gene.
Infections
Transgenic potato plants expressing soybean beta-1,3-endoglucanase gene exhibit an increased resistance to Phytophthora infestans.
Infections
[The relationship between activities of chitinase and beta-1,3-glucanase and resistance to rhizomania in sugar beet]
Infectious Mononucleosis
Glutamate dehydrogenase activity in lymphocytes of B-cell chronic lymphocytic leukaemia patients.
Infertility, Male
Mechanism of male sterility in Petunia: The relationship between pH, callase activity in the anthers, and the breakdown of the microsporogenesis.
Infertility, Male
Premature dissolution of the microsporocyte callose wall causes male sterility in transgenic tobacco.
Infertility, Male
Tapetum-specific expression of the gene for an endo-beta-1,3-glucanase causes male sterility in transgenic tobacco.
Infertility, Male
Timing of callase activity and cytoplasmic male sterility in Petunia.
Intussusception
A seroreactive 120-kilodalton beta-1,3-glucanase of Coccidioides immitis which may participate in spherule morphogenesis.
Leukemia, Lymphoid
Glutamate dehydrogenase activity in lymphocytes of B-cell chronic lymphocytic leukaemia patients.
Lung Injury
Beta-glucan attenuates inflammatory cytokine release and prevents acute lung injury in an experimental model of sepsis.
Mite Infestations
Study of defense-related gene expression in grapevine infested by Colomerus vitis (Acari: Eriophyidae).
Mycoses
A study of some biochemical and histopathological responses of wet-stored recalcitrant seeds of Avicennia marina infected by Fusarium moniliforme.
Mycoses
Ethylene: Symptom, Not Signal for the Induction of Chitinase and beta-1,3-Glucanase in Pea Pods by Pathogens and Elicitors.
Mycoses
The function of vacuolar beta-1,3-glucanase investigated by antisense transformation. Susceptibility of transgenic Nicotiana sylvestris plants to Cercospora nicotianae infection.
Nematode Infections
Alfalfa (Medicago sativa L.) resistance to the root-lesion nematode, Pratylenchus penetrans: defense-response gene mRNA and isoflavonoid phytoalexin levels in roots.
Neoplasms
Hominoid-specific enzyme GLUD2 promotes growth of IDH1R132H glioma.
Neoplasms
Mitochondrial enzyme GLUD2 plays a critical role in glioblastoma progression.
Nervous System Diseases
Glucose transporter type 1 deficiency syndrome associated with autoantibodies to glutamate receptors.
Neuroblastoma
Glutamate receptor ?2 serum antibodies in pediatric opsoclonus myoclonus ataxia syndrome.
Neurodegenerative Diseases
The human GLUD2 glutamate dehydrogenase and its regulation in health and disease.
Opsoclonus-Myoclonus Syndrome
Absence of GluD2 Antibodies in Patients With Opsoclonus-Myoclonus Syndrome.
Parkinson Disease
Deregulation of glutamate dehydrogenase in human neurologic disorders.
Parkinson Disease
Functional validation of a human GLUD2 variant in a murine model of Parkinson's disease.
Parkinson Disease
Gain-of-function variant in GLUD2 glutamate dehydrogenase modifies Parkinson's disease onset.
Parkinson Disease
The human GLUD2 glutamate dehydrogenase and its regulation in health and disease.
Plant Diseases
[Advances on the plant disease resistant beta-glucanase gene]
Pruritus
Salvinorin A analogues PR-37 and PR-38 attenuate compound 48/80-induced itch responses in mice.
Rhinitis, Allergic, Seasonal
Allergenic contribution of the IgE-reactive domains of the 1,3-beta-glucanase Ole e 9: diagnostic value in olive pollen allergy.
Seizures
Epilepsy with myoclonic atonic seizures and chronic cerebellar symptoms associated with antibodies against glutamate receptors N2B and D2 in serum and cerebrospinal fluid.
Starvation
Expression of a cloned beta-glucanase gene from Bacillus amyloliquefaciens in an Escherichia coli relA strain after plasmid amplification.
Starvation
Regulation of beta-1,3-glucanase by carbon starvation in the mycoparasite Trichoderma harzianum.
Tuberculosis
Crystal structural basis for Rv0315, an immunostimulatory antigen and inactive beta-1,3-glucanase of Mycobacterium tuberculosis.
Tuberculosis
Rv0315, a novel immunostimulatory antigen of Mycobacterium tuberculosis, activates dendritic cells and drives Th1 immune responses.
Virus Diseases
Biological function of ;pathogenesis-related' proteins: four PR proteins of tobacco have 1,3-beta-glucanase activity.
Virus Diseases
Expression of stress-response proteins upon whitefly-mediated inoculation of Tomato yellow leaf curl virus in susceptible and resistant tomato plants.
Virus Diseases
Local expression of enzymatically active class I beta-1, 3-glucanase enhances symptoms of TMV infection in tobacco.
Virus Diseases
Movement of plant viruses is delayed in a beta-1,3-glucanase-deficient mutant showing a reduced plasmodesmatal size exclusion limit and enhanced callose deposition.
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I157L
-
site-directed mutagenesis of the active site residue
N52D
-
site-directed mutagenesis of the active site residue
V158A
-
site-directed mutagenesis of the active site residue
K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
E119A/Ldel
-
variant of catalytic domain with deletion of the Gly/Ser-rich linker, Ser244-Thr256, no expression of protein
E119G
site-directed mutagenesis, glucosidase inactive catalytic residue mutant, the mutant shows transglycosylation activity toward laminarioligosaccharides. The hydrolytic as well as transglycosylation activities of E119G decrease with the decrease in temperature, but the ratio of transglycosylation products increases. The enzymatic activity of E119G toward laminaritriose in the presence of glucose is abolished, while the addition of laminaribiose evidently increases the transglycosylation products such as laminaritetraose and laminaripentaose
M123del
-
variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
T149A/A344V
increased activity
T149A/G145D/A344V
increased activity
E119A/Ldel
-
variant of catalytic domain with deletion of the Gly/Ser-rich linker, Ser244-Thr256, no expression of protein
-
E119G
-
site-directed mutagenesis, glucosidase inactive catalytic residue mutant, the mutant shows transglycosylation activity toward laminarioligosaccharides. The hydrolytic as well as transglycosylation activities of E119G decrease with the decrease in temperature, but the ratio of transglycosylation products increases. The enzymatic activity of E119G toward laminaritriose in the presence of glucose is abolished, while the addition of laminaribiose evidently increases the transglycosylation products such as laminaritetraose and laminaripentaose
-
M123del
-
variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
-
E231A
-
no enzymic activity with laminarin, in presence of sodium formate, recovery of 75% of activitiy compared to wild type, with substrate alpha-laminaribiosyl fluoride, polymerization to insoluble, crystalline (1,3)-beta-D-glucans
E231G
-
no enzymic activity with laminarin, in presence of sodium formate, recovery of 75% of activitiy compared to wild type, with substrate alpha-laminaribiosyl fluoride, polymerization to insoluble, crystalline (1,3)-beta-D-glucans
E231S
-
no enzymic activity with laminarin, with substrate alpha-laminaribiosyl fluoride, polymerization to insoluble, crystalline (1,3)-beta-D-glucans
W1679A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
W1688A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
W1729A
site-directed mutagenesis, mutation in the F5/8C module or DS domain, the mutant domain forms inclusion bodies upon expression in Escherichia coli
Y1714A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
Y1768A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
W1679A
-
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
-
W1688A
-
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
-
W1729A
-
site-directed mutagenesis, mutation in the F5/8C module or DS domain, the mutant domain forms inclusion bodies upon expression in Escherichia coli
-
Y1714A
-
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
-
Y1768A
-
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
-
D287A
-
decreased activity
delI72-G75
deletion mutant, lacking residues 72-75, hydrolyses the mixed-linkage beta-1,3-1,4-glucan lichenan at 40°C and 70°C 10times more efficiently than the wiild-type protein. At 80°C, the specific activity of the D-loop mutant is reduced significantly relative to that of the wild-type with both laminarin and lichenan
delMet174
the specific activities of the mutant LamA, on both laminarin and lichenan, is about 10fold lower than the respective wild-type value. The methionine deletion leads to an enzyme with 13.1% of wild-type Vmax and a slightly higher Km on laminarin as a substrate. With lichenan as substrate, the mutant LamA has 7.9% of the wild-type Vmax and the same Km value
E170A
-
severely reduced hydrolytic activity, active as a glycosynthase catalysing condensation of alpha-laminaribiosyl fluoride to different acceptors
E53A
-
decreased activity
E53A/D287A
-
decreased activity
S296C
the immobilized S296C variant shows extreme pH stability and can be repeatedly used at 60°C without significant activity loss of activity
D526A
-
enzymatic activity is similar to that of the wild type protein
D545A
-
enzymatic activity is similar to that of the wild type protein
D526A
-
enzymatic activity is similar to that of the wild type protein
-
C6A
significant decrease in activity towards carboxymethyl-curdlan and laminarin, strong increase in activity towards lichenan
E259A
site-directed mutagenesis, substitution of the nucleophilic residue, the active site mutant retains residual endoglucanase activity
D422A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D422E
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D424A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D424H
-
site-directed mutagenesis, the mutation alters the substrate specificity by increasing the rate of cleavage of mixed-linkage beta-glucan and carboxymethylcellulose 60fold and 16fold, respectively, compared to the wild-type enzyme
D424H/S501A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E499A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E499D
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E503A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E503D
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
F425A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
F425Y
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
H423A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
H426A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
N421A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
S500A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
S501A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
S502A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
W404A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
W444A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
Y427A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D422A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
-
D424A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
-
D424H
-
site-directed mutagenesis, the mutation alters the substrate specificity by increasing the rate of cleavage of mixed-linkage beta-glucan and carboxymethylcellulose 60fold and 16fold, respectively, compared to the wild-type enzyme
-
E499A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
-
W404A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
-
K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
-
the mutant shows 63% increased catalytic activity and stability compared to the wild type enzyme. Half-life values at 60°C and 70°C are 152 and 99 min, respectively
K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
the mutant shows increased catalytic activity and stability compared to the wild type enzyme
K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
-
the mutant shows 63% increased catalytic activity and stability compared to the wild type enzyme. Half-life values at 60°C and 70°C are 152 and 99 min, respectively
-
K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
-
the mutant shows increased catalytic activity and stability compared to the wild type enzyme
-
E119A
inactive
E119A
-
variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
E119A
-
variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
-
W118A
-
the mutant almost abolishes its activity
W118A
-
the mutant almost abolishes its activity
-
H245A
inactive
E158A
mutation switches the activity from mainly transglycosylation to beta-1,3-glucanase. Hydrolytic activity toward reduced laminarin is 348.5fold higher than the wild type
E158A
-
mutation switches the activity from mainly transglycosylation to beta-1,3-glucanase. Hydrolytic activity toward reduced laminarin is 348.5fold higher than the wild type
-
E269S
site-directed mutagenesis, nucleophile replacement, inactive mutant
E269S
-
site-directed mutagenesis, nucleophile replacement, inactive mutant
-
additional information
-
mutant docking study, overview
additional information
-
enzyme disruption mutant, no further effects on growth rate of mutant strains, but results in formation of chains of cells. Enzyme gene is able to complement eng1 mutants in Saccharomyces cerevisiae
additional information
the recombinant N-terminal domain has high hydrolytic activity on laminarin. The C-terminal domain of Fra e 9, a cysteine-rich compact structure, is able to bind laminarin
additional information
-
plants resistant to infection by Orobanche crenata, enzyme is differently expressed in cells near the penetration point
additional information
-
deletion mutant lacking resiudes 72-75 hydrolyzes the mixed-linkgae beta-(1-3)-(1-4)-glucan lichenan 10times more efficiently than wild-type
additional information
deletion mutant lacking resiudes 72-75 hydrolyzes the mixed-linkgae beta-(1-3)-(1-4)-glucan lichenan 10times more efficiently than wild-type
additional information
-
an enzyme deletion strain shows decreased activity of acid trehalase
additional information
-
a point mutation, that destroys the catalytic activity of the protein, results in a phenotype similar to that of the mutant strain with gene eng2 placed under the control of a repressible promoter. Exogenous addition of purified Eng2 releases the ascospores from asci generated by the eng2+-deficient mutant
additional information
C-terminally truncated enzyme without carbohydrate-binding module, about 40% reduction of activity
additional information
-
C-terminally truncated enzyme without carbohydrate-binding module, about 40% reduction of activity
additional information
-
engineering of dual-functional hybrid glucanases from a truncated and mutated 1,3-1,4-beta-D-glucanase gene TFsW203F from Fibrobacter succinogenes, and a 1,3-beta-D-glucanase gene TmLam from hyperthermophilic Thermotoga maritima used as target enzymes, by ligating substrate-binding domains (TmB1 and TmB2) and the catalytic domain (TmLamCD) of TmLam to the N- or C-terminus of TFsW203F to create four hybrid enzymes, TmB1-TFsW203F, TFsW203F-TmB2, TmB1-TFsW203F-TmB2 and TFsW203F-TmLamCD, creation of desirable hybrid enzymes with economic benefits for industrial applications. Improved thermal tolerance of the hybrid enzyme TFsW203FTmLamCD, fluorescence and circular dichroism spectrometric analyses, overview. Kinetic properties of mutant hybrid glucanases
additional information
-
engineering of dual-functional hybrid glucanases from a truncated and mutated 1,3-1,4-beta-D-glucanase gene TFsW203F from Fibrobacter succinogenes, and a 1,3-beta-D-glucanase gene TmLam from hyperthermophilic Thermotoga maritima used as target enzymes, by ligating substrate-binding domains (TmB1 and TmB2) and the catalytic domain (TmLamCD) of TmLam to the N- or C-terminus of TFsW203F to create four hybrid enzymes, TmB1-TFsW203F, TFsW203F-TmB2, TmB1-TFsW203F-TmB2 and TFsW203F-TmLamCD, creation of desirable hybrid enzymes with economic benefits for industrial applications. Improved thermal tolerance of the hybrid enzyme TFsW203FTmLamCD, fluorescence and circular dichroism spectrometric analyses, overview. Kinetic properties of mutant hybrid glucanases
-
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