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1'-beta-D-fructofuranosyl alpha-acarbose
D-fructose + acarbose
alpha-D-glucopyranosyl fluoride + ?
?
luteolin + sucrose
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
sucrose
D-fructose + dextran
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
sucrose + 1,5-anhydro-D-fructose
alpha-D-glucopyranosyl-(1,6)-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose
sucrose + 2-chloroethanol
2-chloroethyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + 3-methyl-1-butanol
D-fructose + 3-methylbutyl alpha-D-glucoside
sucrose + 4-chlorobutanol
4-chlorobutyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + 6-chlorohexanol
6-chlorohexyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + acceptor
?
-
-
-
-
?
sucrose + alpha-butylglucopyranoside
alpha-D-glucopyranosyl-(1,6)-O-butyl-alpha-D-glucopyranoside + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-butyl-alpha-D-glucopyranoside
-
-
-
-
?
sucrose + alpha-D-glucopyranoside
?
sucrose + butan-1-ol
butyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + caffeic acid
D-fructose + caffeic acid-3-O-alpha-D-glucopyranoside
sucrose + cellobiose
D-fructose + ?
sucrose + chlorogenic acid
D-fructose + chlorogenic acid-4'-O-alpha-D-glucopyranoside
sucrose + D-glucose
D-fructose + isomalto-oligosaccharide + isomaltose + leucrose
sucrose + D-glucose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
sucrose + dextran
D-fructose + ?
sucrose + dextran
D-fructose + elongated dextran
sucrose + ethanol
D-fructose + ethyl alpha-D-glucoside
sucrose + ethanol
ethyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + gentobiose
?
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + hydroquinone
D-fructose + 4-hydroxyphenyl-alpha-D-glucopyranoside
sucrose + isomaltohexaose
?
sucrose + isomaltose
D-fructose + isomaltotriose
sucrose + isomaltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
sucrose + L-ascorbic acid
D-fructose + L-ascorbic acid 2-glucoside
sucrose + lactulose
D-fructose + lactulosucrose
sucrose + maltose
?
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + maltose
D-fructose + ?
sucrose + maltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
sucrose + methanol
D-fructose + methyl alpha-D-glucoside
sucrose + methanol
methyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + N-(tert-butoxycarbonyl)-L-serine methyl ester
N-tert-butoxycarbonyl-3-O-alpha-D-glucopyranosyl-L-serine methyl ester + D-fructose
-
-
-
-
?
sucrose + n-propanol
D-fructose + propyl alpha-D-glucoside
sucrose + N-tert-butoxycarbonyl-D-serine methyl ester
N-tert-butoxycarbonyl-3-O-alpha-D-glycopyranosyl-D-serine methyl ester + D-fructose
-
-
-
-
?
sucrose + propan-1-ol
propyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + raffinose
D-fructose + ?
sucrose + salicin
?
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + stachyose tetrahydrate
D-fructose + ?
sucrose + stevioside
13-O-beta-sophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-(beta-(1->6) glucosyl)-beta-glucosylsophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-beta-sophorosyl-19-O-beta-isomaltotriosyl-steviol
sucrose + tert-butanol
D-fructose + tert-butyl alpha-D-glucoside
-
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
additional information
?
-
1'-beta-D-fructofuranosyl alpha-acarbose
D-fructose + acarbose
-
-
-
-
?
1'-beta-D-fructofuranosyl alpha-acarbose
D-fructose + acarbose
-
-
-
-
?
alpha-D-glucopyranosyl fluoride + ?
?
-
-
-
-
?
alpha-D-glucopyranosyl fluoride + ?
?
-
-
-
-
?
luteolin + sucrose
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
-
44% conversion
luteolin-3'-O-alpha-D-glucopyranoside is the major product
-
?
luteolin + sucrose
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
-
44% conversion
luteolin-3'-O-alpha-D-glucopyranoside is the major product
-
?
luteolin + sucrose
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
-
44% conversion
luteolin-3'-O-alpha-D-glucopyranoside is the major product
-
?
myricetin + sucrose
?
-
49% conversion
-
-
?
myricetin + sucrose
?
-
49% conversion
-
-
?
myricetin + sucrose
?
-
49% conversion
-
-
?
sucrose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose
D-fructose + ?
dextransucrase capable of producing a dextran polysaccharide with four types of linkages, including 69% (alpha1->6), 24% (alpha1->3), 6% (alpha1->4), and 1% (alpha1->2)
-
-
?
sucrose
D-fructose + ?
dextransucrase capable of producing a dextran polysaccharide with four types of linkages, including 69% (alpha1->6), 24% (alpha1->3), 6% (alpha1->4), and 1% (alpha1->2)
-
-
?
sucrose
D-fructose + dextran
-
free and immobilized enzyme produces 5.7 mg/ml and 2.6 mg/ml of dextran in 2 l bench scale fermenter under optimum reaction conditions
-
-
?
sucrose
D-fructose + dextran
-
-
-
-
?
sucrose
D-fructose + dextran
-
-
-
-
?
sucrose
D-fructose + dextran
-
-
-
-
?
sucrose
D-fructose + dextran
dextran that is produced by wild-type enzyme has 95% alpha(1->6) linkages in the main chains and 5% alpha(1->3) branch linkage. the dextran synthesized by mutant P473S/P856S shows almost no obvious change with comparison of the wild-type enzyme
-
-
?
sucrose
D-fructose + dextran
-
the produced dextran has a molecular size of 800-1000 kDa
-
-
?
sucrose
D-fructose + dextran
dextran that is produced by wild-type enzyme has 95% alpha(1->6) linkages in the main chains and 5% alpha(1->3) branch linkage. the dextran synthesized by mutant P473S/P856S shows almost no obvious change with comparison of the wild-type enzyme
-
-
?
sucrose
D-fructose + dextran
-
-
-
-
?
sucrose
D-fructose + dextran
-
the produced dextran has a molecular size of 800-1000 kDa
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
high amounts of enzyme catalyze the hydrolysis of the D-glucose residues from the ends of the dextran chains, giving a decrease in the amount of dextran
-
r
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
native enzyme produces mainly 6-linked glucopyranosylresidues, while Escherichia coli recombinant enzyme produces a glucan consisting of 70% 6-linked glucopyranosyl residues and 15% 3,6-glucopyranosyl residues. Mutant enzyme T350K and S455K produce a glucan with 85% 6-linked glucopyranosyl residues. The mutant T350K/S455K produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
with increasing concentrations of sucrose, from 0.1 to 4.0 M, the amount of high-molecular weight dextran decreases with a concomitant increase in low-molecular weight dextran. At 0.1 M sucrose, pH 5.5, and 28°C, 99.8% of the dextran had a MW of more than 1000000 Da and at 4.0 M sucrose, 69.9% have a MW below 100000 Da and 30.1% have a MW of more than 1000000 Da, giving a bimodal distribution. The degree of branching increased from 5% for 0.1 M sucrose to 16.6% for 4.0 M sucrose. The temperature has very little effect on the size of the dextran, which is above 1000000 Da, but it has a significant effect on the degree of branching, which is 4.8% at 4 °C and increases to 14.7% at 45°C. Both the molecular weight and the degree of branching are not significantly affected by different pH values between 4.5 and 6.0
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
dextransucrase preferentially produces an isomaltooligosaccharide series, whose concentration is always low because of the high ability of these products to be elongated and form high molecular weight dextran. In dextransucrase, the A repeats define anchoring zones for the growing chains, favoring their elongation. Based on these results, a semi-processive mechanism involving only one active site and an elongation by the non-reducing end is proposed
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
high amounts of enzyme catalyze the hydrolysis of the D-glucose residues from the ends of the dextran chains, giving a decrease in the amount of dextran
-
r
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
with increasing concentrations of sucrose, from 0.1 to 4.0 M, the amount of high-molecular weight dextran decreases with a concomitant increase in low-molecular weight dextran. At 0.1 M sucrose, pH 5.5, and 28°C, 99.8% of the dextran had a MW of more than 1000000 Da and at 4.0 M sucrose, 69.9% have a MW below 100000 Da and 30.1% have a MW of more than 1000000 Da, giving a bimodal distribution. The degree of branching increased from 5% for 0.1 M sucrose to 16.6% for 4.0 M sucrose. The temperature has very little effect on the size of the dextran, which is above 1000000 Da, but it has a significant effect on the degree of branching, which is 4.8% at 4 °C and increases to 14.7% at 45°C. Both the molecular weight and the degree of branching are not significantly affected by different pH values between 4.5 and 6.0
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
native enzyme produces mainly 6-linked glucopyranosylresidues, while Escherichia coli recombinant enzyme produces a glucan consisting of 70% 6-linked glucopyranosyl residues and 15% 3,6-glucopyranosyl residues. Mutant enzyme T350K and S455K produce a glucan with 85% 6-linked glucopyranosyl residues. The mutant T350K/S455K produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
dextransucrase preferentially produces an isomaltooligosaccharide series, whose concentration is always low because of the high ability of these products to be elongated and form high molecular weight dextran. In dextransucrase, the A repeats define anchoring zones for the growing chains, favoring their elongation. Based on these results, a semi-processive mechanism involving only one active site and an elongation by the non-reducing end is proposed
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
participates in glucan synthesis
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
participates in glucan synthesis
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + 1,5-anhydro-D-fructose
alpha-D-glucopyranosyl-(1,6)-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose
-
the amount of 1,5-anhydro-D-fructo-glucooligosaccharides produced and the average DP increases by using a high sucrose/1,5-anhydro-D-fructose molar ratio and high total sugar concentration
-
-
?
sucrose + 1,5-anhydro-D-fructose
alpha-D-glucopyranosyl-(1,6)-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose
-
the amount of 1,5-anhydro-D-fructo-glucooligosaccharides produced and the average DP increases by using a high sucrose/1,5-anhydro-D-fructose molar ratio and high total sugar concentration
-
-
?
sucrose + 3-methyl-1-butanol
D-fructose + 3-methylbutyl alpha-D-glucoside
-
-
-
-
?
sucrose + 3-methyl-1-butanol
D-fructose + 3-methylbutyl alpha-D-glucoside
-
-
-
-
?
sucrose + alpha-D-glucopyranoside
?
-
three homologous series (S1S3) of methyl alpha-D-glucooligosaccharides. Series S2 and S3 are characterized by the presence of alpha(1,2) linkages, in combination with alpha(1,6) bonds. Two parameters, sucrose to acceptor concentration ratio (S/A) and the total sugar concentration (TSC) determine the yield of methyl alpha-D-glucooligosaccharides. The maximum concentration achieved of the first acceptor product, methyl alpha-D-isomaltoside, is 65 mM using a S/A 1:4 and a TSC of 336 g/l. When increasing temperature, a shift of selectivity towards compounds containing alpha(1,2) bonds is observed. The formation of leucrose as a side process reaches values of 32 g/l at high sucrose concentrations
-
-
?
sucrose + alpha-D-glucopyranoside
?
-
three homologous series (S1S3) of methyl alpha-D-glucooligosaccharides. Series S2 and S3 are characterized by the presence of alpha(1,2) linkages, in combination with alpha(1,6) bonds. Two parameters, sucrose to acceptor concentration ratio (S/A) and the total sugar concentration (TSC) determine the yield of methyl alpha-D-glucooligosaccharides. The maximum concentration achieved of the first acceptor product, methyl alpha-D-isomaltoside, is 65 mM using a S/A 1:4 and a TSC of 336 g/l. When increasing temperature, a shift of selectivity towards compounds containing alpha(1,2) bonds is observed. The formation of leucrose as a side process reaches values of 32 g/l at high sucrose concentrations
-
-
?
sucrose + caffeic acid
D-fructose + caffeic acid-3-O-alpha-D-glucopyranoside
-
-
-
-
?
sucrose + caffeic acid
D-fructose + caffeic acid-3-O-alpha-D-glucopyranoside
-
-
-
-
?
sucrose + cellobiose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + cellobiose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + chlorogenic acid
D-fructose + chlorogenic acid-4'-O-alpha-D-glucopyranoside
-
production yield of chlorogenic acid-4'-O-alpha-D-glucopyranoside is 44.0% or 141 mM as determined by response surface methodology
-
-
?
sucrose + chlorogenic acid
D-fructose + chlorogenic acid-4'-O-alpha-D-glucopyranoside
-
production yield of chlorogenic acid-4'-O-alpha-D-glucopyranoside is 44.0% or 141 mM as determined by response surface methodology
-
-
?
sucrose + D-glucose
D-fructose + isomalto-oligosaccharide + isomaltose + leucrose
-
isomalto-oligosaccharides from DP3 to DP5 along with isomaltose 44 (DP2) and leucrose (DP2) are synthesized
-
-
?
sucrose + D-glucose
D-fructose + isomalto-oligosaccharide + isomaltose + leucrose
-
isomalto-oligosaccharides from DP3 to DP5 along with isomaltose 44 (DP2) and leucrose (DP2) are synthesized
-
-
?
sucrose + D-glucose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are leucrose, isomaltose, glucosyl leucroside, isomaltotriose, isomaltosyl leucroside, and isomaltotetrose
-
?
sucrose + D-glucose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are leucrose, isomaltose, glucosyl leucroside, isomaltotriose, isomaltosyl leucroside, and isomaltotetrose
-
?
sucrose + dextran
?
-
glucose transfer reaction, determination of the dextransucrase minimal motif involved in dextran binding, strong interaction with dextran is localized between amino acids N1397 and A1527 of the C-terminal domain, GBD-7, and consists of six YG repeats, overview. The motif containing enzyme shows very high affinity for isomaltohexaose and longer dextrans and is involved in polymer formation, overview
-
-
?
sucrose + dextran
?
-
glucose transfer reaction, determination of the dextransucrase minimal motif involved in dextran binding, strong interaction with dextran is localized between amino acids N1397 and A1527 of the C-terminal domain, GBD-7, and consists of six YG repeats, overview. The motif containing enzyme shows very high affinity for isomaltohexaose and longer dextrans and is involved in polymer formation, overview
-
-
?
sucrose + dextran
?
-
dextransucrase exhibits both hydrolytic and transferase activities. It catalyses the transfer of glucosyl residues from sucrose to dextran to form complex polysaccharides
-
-
?
sucrose + dextran
?
-
dextransucrase exhibits both hydrolytic and transferase activities. It catalyses the transfer of glucosyl residues from sucrose to dextran to form complex polysaccharides
-
-
?
sucrose + dextran
D-fructose + ?
-
glucose transfer, a step in production of isomaltose, overview
-
-
?
sucrose + dextran
D-fructose + ?
-
glucose transfer
-
-
?
sucrose + dextran
D-fructose + ?
-
glucose transfer, a step in production of isomaltose, overview
-
-
?
sucrose + dextran
D-fructose + ?
-
glucose transfer
-
-
?
sucrose + dextran
D-fructose + ?
-
glucose transfer reaction
-
-
?
sucrose + dextran
D-fructose + elongated dextran
-
-
-
?
sucrose + dextran
D-fructose + elongated dextran
-
-
-
?
sucrose + ethanol
D-fructose + ethyl alpha-D-glucoside
-
-
-
-
?
sucrose + ethanol
D-fructose + ethyl alpha-D-glucoside
-
-
-
-
?
sucrose + hydroquinone
D-fructose + 4-hydroxyphenyl-alpha-D-glucopyranoside
-
optimum condition for 4-hydroxyphenyl-alpha-D-glucopyranoside synthesis is 450 mM hydroquinone, 215 mM sucrose, and 0.55 U/ml dextransucrase
NMR product identification, the product shows antioxidant nitrite- and diphenylpicryl-hydrazyl scavenging activity, to a higher extent than beta-arbutin
-
?
sucrose + hydroquinone
D-fructose + 4-hydroxyphenyl-alpha-D-glucopyranoside
-
optimum condition for 4-hydroxyphenyl-alpha-D-glucopyranoside synthesis is 450 mM hydroquinone, 215 mM sucrose, and 0.55 U/ml dextransucrase
NMR product identification, the product shows antioxidant nitrite- and diphenylpicryl-hydrazyl scavenging activity, to a higher extent than beta-arbutin
-
?
sucrose + isomaltohexaose
?
-
glucose transfer reaction, determination of the dextransucrase minimal motif involved in dextran binding, strong interaction with dextran is localized between amino acids N1397 and A1527 of the C-terminal domain, GBD-7, and consists of six YG repeats, overview. The motif containing enzyme shows very high affinity for isomaltohexaose and longer dextrans and is involved in polymer formation, overview
-
-
?
sucrose + isomaltohexaose
?
-
glucose transfer reaction, determination of the dextransucrase minimal motif involved in dextran binding, strong interaction with dextran is localized between amino acids N1397 and A1527 of the C-terminal domain, GBD-7, and consists of six YG repeats, overview. The motif containing enzyme shows very high affinity for isomaltohexaose and longer dextrans and is involved in polymer formation, overview
-
-
?
sucrose + isomaltose
D-fructose + isomaltotriose
-
-
-
-
?
sucrose + isomaltose
D-fructose + isomaltotriose
-
-
-
-
?
sucrose + isomaltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are leucroside, glucosyl leucroside, isomaltotriose, and isomaltotetraose
-
?
sucrose + isomaltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are leucroside, glucosyl leucroside, isomaltotriose, and isomaltotetraose
-
?
sucrose + L-ascorbic acid
D-fructose + L-ascorbic acid 2-glucoside
recombinant glucansucrase
the glycosylated product has the potential as an antioxidant in industrial applications
-
?
sucrose + L-ascorbic acid
D-fructose + L-ascorbic acid 2-glucoside
recombinant glucansucrase
the glycosylated product has the potential as an antioxidant in industrial applications
-
?
sucrose + lactulose
D-fructose + lactulosucrose
-
-
i.e. beta-D-Gal-(1->4)-beta-D-Fru-(2->1)-alpha-D-Glu, structure determination by NMR, overview
-
?
sucrose + lactulose
D-fructose + lactulosucrose
-
-
i.e. beta-D-Gal-(1->4)-beta-D-Fru-(2->1)-alpha-D-Glu, structure determination by NMR, overview
-
?
sucrose + maltose
D-fructose + ?
-
-
-
?
sucrose + maltose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + maltose
D-fructose + ?
-
-
-
?
sucrose + maltose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + maltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are panose, alpha-isomaltosyl-1,6-alpha-D-glucopyranosyl-1,4-D-glucopyranose, and alpha-isomaltotriosyl-1,6-alpha-D-glucopyranosyl-1,4-D-glucopyranose
-
?
sucrose + maltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are panose, alpha-isomaltosyl-1,6-alpha-D-glucopyranosyl-1,4-D-glucopyranose, and alpha-isomaltotriosyl-1,6-alpha-D-glucopyranosyl-1,4-D-glucopyranose
-
?
sucrose + maltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
glucooligosaccarides are produced through the acceptor reaction with maltose, a homologous series of isomaltooligosac-charides with reducing end maltose units
-
?
sucrose + methanol
D-fructose + methyl alpha-D-glucoside
-
-
-
-
?
sucrose + methanol
D-fructose + methyl alpha-D-glucoside
-
-
-
-
?
sucrose + n-propanol
D-fructose + propyl alpha-D-glucoside
-
-
-
-
?
sucrose + n-propanol
D-fructose + propyl alpha-D-glucoside
-
-
-
-
?
sucrose + raffinose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + raffinose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + stachyose tetrahydrate
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + stachyose tetrahydrate
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + stevioside
13-O-beta-sophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-(beta-(1->6) glucosyl)-beta-glucosylsophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-beta-sophorosyl-19-O-beta-isomaltotriosyl-steviol
-
-
-
-
?
sucrose + stevioside
13-O-beta-sophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-(beta-(1->6) glucosyl)-beta-glucosylsophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-beta-sophorosyl-19-O-beta-isomaltotriosyl-steviol
-
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
a highly processive mechanism of dextran biosynthesis, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
the enzyme performs dextran synthesis from sucrose, but D-glucose and sucrose are no initiator primers. Both D-glucose and dextran are covalently attached to B-512FMC dextransucrase at the active site during polymerization. The D-glucose moieties of sucrose are added to the reducing ends of the covalently linked growing dextran chains. Asp551, Glu589, and Asp 622 at the active sites of glucansucrases participate in the polymerization of dextran and related glucans from a single active site by the addition of the D-glucose moiety of sucrose to the reducing ends of the covalently linked glucan chains in a two catalytic-site, insertion mechanism overview. In the early stages of the reaction the products are D-glucose, D-fructose, leucrose, and isomaltodextrins in low, exponentially decreasing amounts from DP 2-5, with minuscule amounts of DP 6-12, but exponentially decreasing amounts of isomaltodextrins, down to minuscule amounts of DP 20-25, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
a highly processive mechanism of dextran biosynthesis, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
the enzyme performs dextran synthesis from sucrose, but D-glucose and sucrose are no initiator primers. Both D-glucose and dextran are covalently attached to B-512FMC dextransucrase at the active site during polymerization. The D-glucose moieties of sucrose are added to the reducing ends of the covalently linked growing dextran chains. Asp551, Glu589, and Asp 622 at the active sites of glucansucrases participate in the polymerization of dextran and related glucans from a single active site by the addition of the D-glucose moiety of sucrose to the reducing ends of the covalently linked glucan chains in a two catalytic-site, insertion mechanism overview. In the early stages of the reaction the products are D-glucose, D-fructose, leucrose, and isomaltodextrins in low, exponentially decreasing amounts from DP 2-5, with minuscule amounts of DP 6-12, but exponentially decreasing amounts of isomaltodextrins, down to minuscule amounts of DP 20-25, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
In the presence of maltose, the most abundant reaction product is panose, i.e. MP1 or alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,4)-D-glucopyranose, with 35.3%, detailed NMR product identification and structure analysis, overview
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
substrate is dextran
product analysis by thin layer chromatography
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
substrate is dextran
product analysis by thin layer chromatography
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
DSase-catalyzed dextran elongation
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
sucrose is the preferred donor substrate
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
sucrose is the preferred donor substrate
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
JX679020
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
JX679020
best at 5% sucrose in 20 mM sodium acetate buffer
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
JX679020
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
JX679020
best at 5% sucrose in 20 mM sodium acetate buffer
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
production of dextran
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
production of dextran, optimal at 5% w/v sucrose
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
production of dextran
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
production of dextran, optimal at 5% w/v sucrose
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
substrate is dextran
product determination by NMR spectroscopy
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
substrate is dextran
the produced dextran confirmes the presence of main chain alpha-(1->6) linkages with only 3.0% of alpha-(1->3) branching, of which some are elongated
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
dextran
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
substrate is dextran
product determination by NMR spectroscopy
-
?
additional information
?
-
-
glucose transfer from sucrose, synthesis of panose
-
-
?
additional information
?
-
the recombinant enzyme successfully produces a series of isomaltooligosaccharides from sucrose and maltose, on the basis of its transglycosylation activity
-
-
?
additional information
?
-
DexT catalyzes the polymerization of sucrose to dextran via a transglucosyl reaction
-
-
?
additional information
?
-
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching
-
-
?
additional information
?
-
-
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching
-
-
?
additional information
?
-
-
dextransucrase promotes the sucrose cleavage polymerizing the glucose into dextran chain and releasing the fructose moiety
-
-
?
additional information
?
-
structural analysis, by HPAEC-PAD, HPSEC, and 13C-NMR, of the polymer and oligodextrans produced by the B/110-1-2 dextransucrases, overview
-
-
?
additional information
?
-
-
structural analysis, by HPAEC-PAD, HPSEC, and 13C-NMR, of the polymer and oligodextrans produced by the B/110-1-2 dextransucrases, overview
-
-
?
additional information
?
-
the recombinant enzyme catalyzes oligosaccharides synthesis from sucrose as donor and maltose acceptor
-
-
?
additional information
?
-
-
the recombinant enzyme catalyzes oligosaccharides synthesis from sucrose as donor and maltose acceptor
-
-
?
additional information
?
-
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching
-
-
?
additional information
?
-
-
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching
-
-
?
additional information
?
-
the recombinant enzyme catalyzes oligosaccharides synthesis from sucrose as donor and maltose acceptor
-
-
?
additional information
?
-
-
the recombinant enzyme catalyzes oligosaccharides synthesis from sucrose as donor and maltose acceptor
-
-
?
additional information
?
-
structural analysis, by HPAEC-PAD, HPSEC, and 13C-NMR, of the polymer and oligodextrans produced by the B/110-1-2 dextransucrases, overview
-
-
?
additional information
?
-
the recombinant enzyme successfully produces a series of isomaltooligosaccharides from sucrose and maltose, on the basis of its transglycosylation activity
-
-
?
additional information
?
-
-
the recombinant enzyme successfully produces a series of isomaltooligosaccharides from sucrose and maltose, on the basis of its transglycosylation activity
-
-
?
additional information
?
-
DexT catalyzes the polymerization of sucrose to dextran via a transglucosyl reaction
-
-
?
additional information
?
-
-
DexT catalyzes the polymerization of sucrose to dextran via a transglucosyl reaction
-
-
?
additional information
?
-
-
dextransucrase promotes the sucrose cleavage polymerizing the glucose into dextran chain and releasing the fructose moiety
-
-
?
additional information
?
-
-
a lysine residue is present at the active site and is essential for the activity
-
-
?
additional information
?
-
-
the enzyme also catalyzes hydrolysis of D-glucose from the non-reducing ends of dextran chains and transfer of D-glucose from the non-reducing ends of dextran chains to maltose with low efficiency
-
-
?
additional information
?
-
-
the enzyme possesses enhanced levels of sucrose hydrolyzing activity
-
-
?
additional information
?
-
the enzyme catalyzes the formation of both alpha-1,6 and alpha1,2-glycosidic linkages. The catalytic domain CD1 is specific for the synthesis of alpha-1,6 glucosidic bonds and CD2 only catalyzes the formation of alpha-1,2 linkage
-
-
?
additional information
?
-
-
induced by growth on sucrose
-
-
?
additional information
?
-
-
activity assay by measurement of release of reducing sugar from sucrose by the 3,5-dinitrosalicylic acid method
-
-
?
additional information
?
-
glucose transfer from sucrose to dextran of about 68 kDa by the recombinant enzyme expressed in Escherichia coli
-
-
?
additional information
?
-
-
glucose transfer from sucrose to dextran of about 68 kDa by the recombinant enzyme expressed in Escherichia coli
-
-
?
additional information
?
-
-
glucose transfer from sucrose to dextrans leading to polymerization with release of D-fructose, the enzyme contains an active site His residue as well as an essential lysine residue
-
-
?
additional information
?
-
-
glucose transfer from sucrose, synthesis of panose
-
-
?
additional information
?
-
-
keta-sucrose, produced by pyranose 2-oxidase, is polymerized to keto-dextran by the dextrasucrase
-
-
?
additional information
?
-
-
synthesis of a series of cellobio-oligosaccharides from cellobiose by dextransucrase performed transglycosylation, method optimization, overview
-
-
?
additional information
?
-
-
the dextransucrase DSRBCB4 synthesizes only alpha-1,6-linked dextran, the recombinantly expressed DSRBCB4 synthesizes oligosaccharides in the presence of maltose or isomaltose as an acceptor, the products including alpha-1,6-linked glucosyl residues in addition to the maltosyl or isomaltosyl residue, conserved amino acid residues in the catalytic core, D530, E568, and D641, that are critical for enzyme activity, NMR product analysis, overview
-
-
?
additional information
?
-
-
the enzyme synthesizes isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, overview
-
-
?
additional information
?
-
-
wild-type and mutant enzymes from strain Lm M286 produce a resistant glucan, based on endo-dextranase and amyloglucosidase hydrolysis. The extracellular enzymes from strain Lm M286 catalyse acceptor reactions and transfer the glucose unit from sucrose to maltose to produce glucooligosaccharides , synthesisis of a dextran-type polysaccharide, overview
-
-
?
additional information
?
-
-
dextransucrase can possibly transfer acarbose to various types of dextransucrase acceptors
-
-
?
additional information
?
-
engineered recombinant mutant enzyme DXSR, a fusion of dextransucrase and dextranase, produces linear isomalto-oligosaccharides with DP2-DP10 using sucrose as a sole substrate. DXSR gives 30fold higher production of isomalto-oligosaccharides than that of an equal activity mixture of the two enzymes such as dextranase and dextransucrase
-
-
?
additional information
?
-
-
measurement of liberation of D-fructose from sucrose
-
-
?
additional information
?
-
-
no activity with 2-propanol, MALDI-TOF-mass spectrometry and NMR, structures and HMBC correlations, product analysis
-
-
?
additional information
?
-
-
DSase can quickly proceed to elongation because the decomposition rate of the ESdex complex is very small
-
-
?
additional information
?
-
dextran product analysis by treatment with Penicillium dextranase and by thin layer chromatography, and by NMR spectroscopy
-
-
?
additional information
?
-
-
dextran product analysis by treatment with Penicillium dextranase and by thin layer chromatography, and by NMR spectroscopy
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
-
synergistic catalytic manner of recombinant dextransucrase and Hypocrea lixii dextranase in production of isomalto-oligosaccharides, produced by sucrose conversion and dextran hydrolysis, molecular weight change of dextrans, overview. High sucrose concentrations in the dextransucrase and dextranase system lead to accumulation of oligodextrans with molecular weights below 15 kDa. Combined usage of recombinant dextransucrase and Hypocrea lixii dextranase produces isomalto-oligosaccharides with a degree of polymerization of 2-10
-
-
?
additional information
?
-
-
the enzyme also catalyzes the hydrolysis of sucrose to give D-glucose and D-fructose. Leucrose (alpha-D-Glu-(1->5)-D-Fru) formation is attributed to the minor capacity of free D-fructose to act as acceptor in the dextransucrase-catalyzed reactions, formation of leucrose by action of dextransucrase is favored at high fructose concentration. Once the availability of sucrose is very limited, lactulosucrose can then act as donor substrate
-
-
?
additional information
?
-
glucose transfer from sucrose to dextran of about 68 kDa by the recombinant enzyme expressed in Escherichia coli
-
-
?
additional information
?
-
-
glucose transfer from sucrose to dextran of about 68 kDa by the recombinant enzyme expressed in Escherichia coli
-
-
?
additional information
?
-
-
no activity with 2-propanol, MALDI-TOF-mass spectrometry and NMR, structures and HMBC correlations, product analysis
-
-
?
additional information
?
-
-
the dextransucrase DSRBCB4 synthesizes only alpha-1,6-linked dextran, the recombinantly expressed DSRBCB4 synthesizes oligosaccharides in the presence of maltose or isomaltose as an acceptor, the products including alpha-1,6-linked glucosyl residues in addition to the maltosyl or isomaltosyl residue, conserved amino acid residues in the catalytic core, D530, E568, and D641, that are critical for enzyme activity, NMR product analysis, overview
-
-
?
additional information
?
-
dextran product analysis by treatment with Penicillium dextranase and by thin layer chromatography, and by NMR spectroscopy
-
-
?
additional information
?
-
-
dextran product analysis by treatment with Penicillium dextranase and by thin layer chromatography, and by NMR spectroscopy
-
-
?
additional information
?
-
engineered recombinant mutant enzyme DXSR, a fusion of dextransucrase and dextranase, produces linear isomalto-oligosaccharides with DP2-DP10 using sucrose as a sole substrate. DXSR gives 30fold higher production of isomalto-oligosaccharides than that of an equal activity mixture of the two enzymes such as dextranase and dextransucrase
-
-
?
additional information
?
-
-
dextransucrase can possibly transfer acarbose to various types of dextransucrase acceptors
-
-
?
additional information
?
-
-
glucose transfer from sucrose to dextrans leading to polymerization with release of D-fructose, the enzyme contains an active site His residue as well as an essential lysine residue
-
-
?
additional information
?
-
-
the enzyme synthesizes isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, overview
-
-
?
additional information
?
-
-
the enzyme also catalyzes hydrolysis of D-glucose from the non-reducing ends of dextran chains and transfer of D-glucose from the non-reducing ends of dextran chains to maltose with low efficiency
-
-
?
additional information
?
-
-
synthesis of a series of cellobio-oligosaccharides from cellobiose by dextransucrase performed transglycosylation, method optimization, overview
-
-
?
additional information
?
-
-
the enzyme also catalyzes the hydrolysis of sucrose to give D-glucose and D-fructose. Leucrose (alpha-D-Glu-(1->5)-D-Fru) formation is attributed to the minor capacity of free D-fructose to act as acceptor in the dextransucrase-catalyzed reactions, formation of leucrose by action of dextransucrase is favored at high fructose concentration. Once the availability of sucrose is very limited, lactulosucrose can then act as donor substrate
-
-
?
additional information
?
-
-
wild-type and mutant enzymes from strain Lm M286 produce a resistant glucan, based on endo-dextranase and amyloglucosidase hydrolysis. The extracellular enzymes from strain Lm M286 catalyse acceptor reactions and transfer the glucose unit from sucrose to maltose to produce glucooligosaccharides , synthesisis of a dextran-type polysaccharide, overview
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
the enzyme catalyzes the formation of both alpha-1,6 and alpha1,2-glycosidic linkages. The catalytic domain CD1 is specific for the synthesis of alpha-1,6 glucosidic bonds and CD2 only catalyzes the formation of alpha-1,2 linkage
-
-
?
additional information
?
-
-
the enzyme catalyzes the formation of both alpha-1,6 and alpha1,2-glycosidic linkages. The catalytic domain CD1 is specific for the synthesis of alpha-1,6 glucosidic bonds and CD2 only catalyzes the formation of alpha-1,2 linkage
-
-
?
additional information
?
-
-
the enzyme possesses enhanced levels of sucrose hydrolyzing activity
-
-
?
additional information
?
-
-
a lysine residue is present at the active site and is essential for the activity
-
-
?
additional information
?
-
-
triple mutation N1134S/N1135E/S1136V converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme. Mutant enzyme P1026V/I1029V/N1134S/N1135E/S1136V synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
-
-
?
additional information
?
-
-
triple mutation N1134S/N1135E/S1136V converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme. Mutant enzyme P1026V/I1029V/N1134S/N1135E/S1136V synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
-
-
?
additional information
?
-
JX679020
no activity with raffinose
-
-
?
additional information
?
-
-
no activity with raffinose
-
-
?
additional information
?
-
-
optimization of conditions for dextransucrase activity assay
-
-
?
additional information
?
-
JX679020
no activity with raffinose
-
-
?
additional information
?
-
-
no activity with raffinose
-
-
?
additional information
?
-
-
purified dextransucrase possesses an invertase-like activity
-
-
?
additional information
?
-
-
the enzyme shows hydrolytic and glucosyl transferase activities with sucrose
-
-
?
additional information
?
-
-
purified dextransucrase possesses an invertase-like activity
-
-
?
additional information
?
-
-
the enzyme shows hydrolytic and glucosyl transferase activities with sucrose
-
-
?
additional information
?
-
the recombinant DSRWC synthesizes oligosaccharides in the presence of maltose or isomaltose as an acceptor and the synthesized products include alpha-1,6-linked glucosyl residues in addition to the maltosyl or isomaltosyl residue. rDSRWC synthesizes water-soluble polymers using sucrose as substrate, and rDSRBWC synthesizes dextran and leucrose [alpha-D-glucopyranosyl-(1,5)-beta-D-fructofuranose]
-
-
?
additional information
?
-
-
the recombinant DSRWC synthesizes oligosaccharides in the presence of maltose or isomaltose as an acceptor and the synthesized products include alpha-1,6-linked glucosyl residues in addition to the maltosyl or isomaltosyl residue. rDSRWC synthesizes water-soluble polymers using sucrose as substrate, and rDSRBWC synthesizes dextran and leucrose [alpha-D-glucopyranosyl-(1,5)-beta-D-fructofuranose]
-
-
?
additional information
?
-
Cab3 dextransucrase WcCab3-DSR is used for in vitro synthesis of dextran and glucooligosaccharides, product analysis by NMR and and mass spectrometry. Glucooligosaccarides are produced through the acceptor reaction with maltose
-
-
?
additional information
?
-
-
Cab3 dextransucrase WcCab3-DSR is used for in vitro synthesis of dextran and glucooligosaccharides, product analysis by NMR and and mass spectrometry. Glucooligosaccarides are produced through the acceptor reaction with maltose
-
-
?
additional information
?
-
optimization of enzymatic dextran production in wheat bran, overview
-
-
?
additional information
?
-
-
optimization of enzymatic dextran production in wheat bran, overview
-
-
?
additional information
?
-
optimization of enzymatic dextran production in wheat bran, overview
-
-
?
additional information
?
-
-
optimization of enzymatic dextran production in wheat bran, overview
-
-
?
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A670V
the mutation increases the percentage of alpha(1->3) linkages (9% at most) and decreases the percentage of alpha(1->6) linkages in the product
D460A/H463S/T464L
site-directed mutagenesis
D460M/H463Y/T464M/S512C
site-directed mutagenesis
D511N
-
mutant protein shows no dextran formation
D513N
-
mutant enzyme shows reduced dextran formation
D530N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D533A
-
mutant enzyme with 2.3% of wild-type activity
D533N
-
complete suppression of dextran synthesis activity
D536A
-
mutant enzyme with 40.8% of wild-type activity
D536N
-
complete suppression of dextran synthesis activity
D551N
-
mutant protein shows no dextran formation
D590A
the mutation introduces a decrease the percentage of alpha(1->3) linkage in the product
D641N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E568Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E664K
the mutation introduces additional alpha(1->3) glycosidic linkages and also some additional alpha(1->2) glycosidic linkages, the mutation decreases the percentage of alpha(1->6) linkages in the product
F196S
-
site-directed mutagenesis, the mutant DRN1 shows a higher expression level in Escherichia coli and increased activity compared to DSRB742
H161R
-
mutant protein retains a very low dextran synthesis activity
H463R/T464D/S512T
site-directed mutagenesis
H463R/T464V/S512T
site-directed mutagenesis
H643A
-
complete suppression of dextran synthesis activity
H643N
-
complete suppression of dextran synthesis activity
K378T
mutant enzyme shows 75% increase in activity
K378T/K725T
mutant enzyme shows 90% decrease in activity
K378T/K725T/K955T
mutant enzyme shows no enzymatic activity
K378T/K955T
mutant enzyme shows 60% increase in activity
K395T
-
site-directed mutagenesis, the mutant DRN3 shows a higher expression level in Escherichia coli and increased activity compared to DSRB742
K725T
mutant enzyme shows 85% decrease in activity
K725T/K955T
mutant enzyme shows 80% decrease in activity
K955T
activity of the mutant enzyme is similar to activity of wild-type enzyme
N555Y
the mutation increases the percentage of alpha(1->3) linkages (9% at most) and decreases the percentage of alpha(1->6) linkages in the product
P473S
mutant enzyme shows 40% increase in activity
P473S/P678S
mutant enzyme shows 75% increase in activity
P473S/P678S/P856S
mutant enzyme shows no enzymatic activity
P473S/P856S
the mutant enzyme shows a significant increase in thermal inactivation with a 7.4fold increase in half-life at 35°C and a 2fold increase in catalytic efficiency compared with the wild-type. Highest enzymatic activity mutant. Mutant enzyme P478S/P856S is slightly more stable than wild-type enzyme
P678S
mutant enzyme shows 15% increase in activity
P678S/P856S
mutant enzyme shows 95% increase in activity
P856S
mutant enzyme shows 50% increase in activity
P980T
-
site-directed mutagenesis, the mutant DRN4 shows a lower expression level in Escherichia coli compared to DSRB742
Q1029K
the mutation has no significant effect on the linkage specificity
Q666R
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreases the percentage of alpha(1->6) linkages in the product
S455K
-
produces a glucan with 85% 6-linked glucopyranosyl residues
S663N
the mutation increases the percentage of alpha(1->3) linkages (9% at most) and decreases the percentage of alpha(1->6) linkages in the product
T350K
-
produces a glucan with 85% 6-linked glucopyranosyl residues
V553A
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreased the production of alpha(1->3) linkage polysaccharides
V556I
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreased the production of alpha(1->3) linkage polysaccharides
V665A
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreases the percentage of alpha(1->6) linkages in the product
W591G
the mutation introduces a decrease the percentage of alpha(1->3) linkage in the product
Y346N
-
site-directed mutagenesis, the mutant DRN2 shows a lower expression level in Escherichia coli compared to DSRB742
D590A
-
the mutation introduces a decrease the percentage of alpha(1->3) linkage in the product
-
K378T
-
mutant enzyme shows 75% increase in activity
-
K725T
-
mutant enzyme shows 85% decrease in activity
-
N555Y
-
the mutation increases the percentage of alpha(1->3) linkages (9% at most) and decreases the percentage of alpha(1->6) linkages in the product
-
P473S
-
mutant enzyme shows 40% increase in activity
-
P678S
-
mutant enzyme shows 15% increase in activity
-
P856S
-
mutant enzyme shows 50% increase in activity
-
V553A
-
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreased the production of alpha(1->3) linkage polysaccharides
-
V556I
-
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreased the production of alpha(1->3) linkage polysaccharides
-
D530N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
D641N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
E568Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
D533A
-
mutant enzyme with 2.3% of wild-type activity
-
D533N
-
complete suppression of dextran synthesis activity
-
D536A
-
mutant enzyme with 40.8% of wild-type activity
-
D536N
-
complete suppression of dextran synthesis activity
-
H643A
-
complete suppression of dextran synthesis activity
-
D511N
-
mutant protein shows no dextran formation
-
D513N
-
mutant enzyme shows reduced dextran formation
-
D551N
-
mutant protein shows no dextran formation
-
H161R
-
mutant protein retains a very low dextran synthesis activity
-
D306X
-
random mutagenesis
-
F353T
-
random mutagenesis
-
F353W
-
random mutagenesis
-
F353X
-
random mutagenesis
-
S455K
-
produces a glucan with 85% 6-linked glucopyranosyl residues
-
T350K
-
produces a glucan with 85% 6-linked glucopyranosyl residues
-
N1134S/N1135E/S1136V
-
mutation converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme
P1026V/I1029V/N1134S/N1135E/S1136V
-
mutant enzyme synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
N1134S/N1135E/S1136V
-
mutation converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme
-
P1026V/I1029V/N1134S/N1135E/S1136V
-
mutant enzyme synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
-
N1134S
-
the mutation in GTFA results in a drastically changed specificity but no major changes in polymer versus oligosaccharide formation
R624G
-
the R624G mutations near the transition state stabilizer is involved in the phenotype which exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages
R624G/V630I
-
the mutant exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages, both mutations near the transition state stabilizer, R624G and V630I, are contributing to this alteration
R624G/V630I/D717A
-
the mutant exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages, both mutations near the transition state stabilizer, R624G and V630I, are contributing to this alteration
S628D
-
saturation mutagenesis, the mutation guides the reaction toward the synthesis of short chain oligosaccharides with a drastically increased yield of 47% isomaltose or 64% leucrose
S628R
-
saturation mutagenesis, the mutation guides the reaction toward the synthesis of short chain oligosaccharides with a drastically increased yield of 47% isomaltose or 64% leucrose
V630I
-
the V630I mutations near the transition state stabilizer is involved in the phenotype which exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages
T350K/S455K
-
mutant enzyme exhibits a 10fold increase in glucosyltransferase activity over those of the parental DSRS-His6 and its T350K and S455K mutants
T350K/S455K
-
produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
T350K/S455K
-
mutant enzyme exhibits a 10fold increase in glucosyltransferase activity over those of the parental DSRS-His6 and its T350K and S455K mutants
-
T350K/S455K
-
produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
-
additional information
construction of a truncated active variant DSR-F-DELTASPDELTAGBD of 1251 amino acids, with a molecular mass of 145544 Da, the mutant lacks the sequence encoding signal peptide and a portion of the C-terminal domain, i.e. the glucan binding domain
additional information
-
construction of a truncated active variant DSR-F-DELTASPDELTAGBD of 1251 amino acids, with a molecular mass of 145544 Da, the mutant lacks the sequence encoding signal peptide and a portion of the C-terminal domain, i.e. the glucan binding domain
additional information
-
construction of a truncated active variant DSR-F-DELTASPDELTAGBD of 1251 amino acids, with a molecular mass of 145544 Da, the mutant lacks the sequence encoding signal peptide and a portion of the C-terminal domain, i.e. the glucan binding domain
-
additional information
directed evolution of a B-742CB dextransucrase gene (dsrB742) that elaborates a novel extracellular dextransucrase gene (dsrB742ck) after ultrasoft X-ray irradiation, producing a dextransucrase of increased activity and synthesis of a highly branched dextran
additional information
-
rational deletions of the signal peptide, the beginning of the variable region and the last four repeats of the C-terminal end cause no loss of activity. The new variant successfully purified is remarkably stable. With a kcat of 584 per s, it is the most efficient recombinant glucansucrase described to date. The synthesized polymer possesses more than 95% of alpha-1,6 links, like the dextran produced by the native enzyme
additional information
-
co-immobilization of dextransucrase and dextranase on calcium alginate for the facilitated synthesis of isomalto-oligosaccharides, reaction scheme, method optimization, and modeling, overview
additional information
-
construction of constitutive mutants by chemical mutagenesis using ethyl methane sulfonate in strain Lm M281, overview
additional information
-
construction of engineered enzyme variants for production of isomalto-oligosaccharides and dextrans of controlled molecular weight of about 10-40 kDa in a one-step process, method optimization, overview
additional information
-
construction of fourteen truncated forms of strain NRRL B512-F dextransucrase by N-, C- or N- plus C-terminal domain truncations, dextran binding properties of mutant enzymes, overview
additional information
-
the enzyme is usable in the production of isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, alteration of the ratio of sucrose to maltose and the amount of each sugar, overview
additional information
-
the partially purified native enzyme from strain PCSIR-4 is immobilized on alginate for application in the production of dextran from sucrose, method optimization, overview
additional information
construction of a fusion enzyme DXSR of dextransucrase, encoded by gene dsrBCB4, and dextranase, encoded by gene dex2, for one-step synthesis of isomalto-oligosaccharides. DXSR shows 150% increased endo-dextranase activity and 98% decreased dextransucrase activity. The engineered recombinant mutant enzyme DXSR, a fusion of dextransucrase and dextranase, produces linear isomalto-oligosaccharides with DP2-DP10 using sucrose as a sole substrate. DXSR gives 30fold higher production of isomalto-oligosaccharides than that of an equal activity mixture of the two enzymes such as dextranase and dextransucrase
additional information
-
construction of a truncated mutant of enzyme B-512F, the mutant shows sigmoidal shaped curves when the initial velocities are plotted against the concentration of added dextran. The increase in the reaction rate and the decrease in the sigmoidal curve with increasing dextran concentrations indicate that dextran binds at a noncatalytic or allosteric site to give a more active enzyme
additional information
-
optimization of culture conditions for high-level lactose-inducible expression of Leuconostoc mesenteroides dextransucrase in recombinant Escherichia coli strain BL 21(DE3), overview. Maximal activity of 60.18 U/ml from a fed-batch culture at 5 g/l lactose, added at an OD600 of 3.0, at 25°C for 7 h
additional information
construction and optimal expression of a fusion enzyme DSXR having dextransucrase and dextranase activities, for optimization of protein expression, response surface methodology is used
additional information
-
generation of diverse mutant enzymes using UV irradiation random mutagensis, mutant screeening, overview. Mutant KIBGE IB-22M20 exhibits 6.75fold increased dextransucrase activity compared to the wild-type enzyme
additional information
-
immobilisation of the enzyme directly on a 27 MHz quartz crystal microbalance, QCM, plate, or on a dextran-acceptor-QCM plate, method evaluation and binding kinetics,overview. The enzymatic activity of DSase is not affected by immobilization, possibly due to the use of a long PEG spacer group. Typical frequency changes of the dextran-immobilized QCM as a function of time in response to the addition of DSase and sucrose substrate in 50 mM acetate buffer pH 5.2, 150 mM NaCl, and 1 mM CaCl2 at 25°C
additional information
construction of two truncated derivative mutants DsrE563DCD2DGBD (DsrE563-1) and DsrE563DCD2DVR (DsrE563-2). Mutant DsrE563-1 with a deletion of 1620 amino acids from the C-terminus, and mutant DsrE563-2 with deletion of 1258 amino acids from the C-terminus and 349 amino acids from the N-terminus, are catalytically active synthesizing less-soluble dextran, mainly containing alpha-1,6 glucosidic linkage, the synthesized less-soluble dextran also has a branched alpha-1,3 linkage. Mutant DsrE563-2 shows 4.5fold higher dextransucrase activity than mutant DsrE563-1 and a higher acceptor reaction efficiency compared to the wild-type enzyme from Leuconostoc mesenteroides strain 512 FMCM when various mono- or disaccharides are used as acceptors
additional information
-
construction of two truncated derivative mutants DsrE563DCD2DGBD (DsrE563-1) and DsrE563DCD2DVR (DsrE563-2). Mutant DsrE563-1 with a deletion of 1620 amino acids from the C-terminus, and mutant DsrE563-2 with deletion of 1258 amino acids from the C-terminus and 349 amino acids from the N-terminus, are catalytically active synthesizing less-soluble dextran, mainly containing alpha-1,6 glucosidic linkage, the synthesized less-soluble dextran also has a branched alpha-1,3 linkage. Mutant DsrE563-2 shows 4.5fold higher dextransucrase activity than mutant DsrE563-1 and a higher acceptor reaction efficiency compared to the wild-type enzyme from Leuconostoc mesenteroides strain 512 FMCM when various mono- or disaccharides are used as acceptors
additional information
screening of diverse mutants of the eight conserved residues that are determined to be important for enzyme activity, overview. Construction of enzyme mutant DSR-S vardel DELTA4N
additional information
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
additional information
DSR-S1-DELTAV (residues 1-1425) and DSR-S2-DELTA(V) (residues 1-1279) are constructed by deleting partial YG repeats of domain V. DSR-S3-DELTA(V) (residues 1-1160), DSR-S-DELTA IV (residues 1-1124), and DSR-S-DELTA(B) (residues 1-1110) are constructed by deleting the relevant fragments from C-terminal ends. The truncation mutant DSR-S1-DELTA(A) (residues 1-1029) is constructed by deleting partial domain A while containing complete conserved Motif regions I. DSR-S2-DELTA(A) (residues 1-1022) is constructed by deleting partial domain A including conserved Motif regions I. DSRS3-DELTA(A) (residues 1-1000) is constructed by deleting more domain A fragment, allowing further investigation of the functions of C-terminal end domain. 102 amino acids of C-terminal end has no effect on dextran synthesis, but it will improve enzyme protein expression by deleting these amino acids. After further deletion, polysaccharidesynthesizing capability of dextransucrase will be inhibited. With the addition of maltose as postreceptors, truncated enzymes undergoes glycosylation reaction and transferred glucosyl from sucrose to acceptor effectively. By deleting the 417 amino acid fragment, its oligosaccharide synthesizing capability significantly increases. This is an effective way to make use of dextransucrase for prebiotic synthesis
additional information
-
DSR-S1-DELTAV (residues 1-1425) and DSR-S2-DELTA(V) (residues 1-1279) are constructed by deleting partial YG repeats of domain V. DSR-S3-DELTA(V) (residues 1-1160), DSR-S-DELTA IV (residues 1-1124), and DSR-S-DELTA(B) (residues 1-1110) are constructed by deleting the relevant fragments from C-terminal ends. The truncation mutant DSR-S1-DELTA(A) (residues 1-1029) is constructed by deleting partial domain A while containing complete conserved Motif regions I. DSR-S2-DELTA(A) (residues 1-1022) is constructed by deleting partial domain A including conserved Motif regions I. DSRS3-DELTA(A) (residues 1-1000) is constructed by deleting more domain A fragment, allowing further investigation of the functions of C-terminal end domain. 102 amino acids of C-terminal end has no effect on dextran synthesis, but it will improve enzyme protein expression by deleting these amino acids. After further deletion, polysaccharidesynthesizing capability of dextransucrase will be inhibited. With the addition of maltose as postreceptors, truncated enzymes undergoes glycosylation reaction and transferred glucosyl from sucrose to acceptor effectively. By deleting the 417 amino acid fragment, its oligosaccharide synthesizing capability significantly increases. This is an effective way to make use of dextransucrase for prebiotic synthesis
additional information
-
mutant dextransucrases are constructed by inserting amino acid into catalytic pocket. The mutant enzymes are constructed by inserting amino acid between A552 and V553 (inserted mutantion motif II, IMII) and D662 and S663 (inserted mutantion motif IV, IMIV). Variants with catalytic activity are screened of library which synthesize high molecular weight alpha-glucans with different proportions of alpha(1-4) linkages ranging from 0 to 52%. Mutant dextransucrases which synthesize hyperbranched dextran are obtained
additional information
-
mutant dextransucrases are constructed by inserting amino acid into catalytic pocket. The mutant enzymes are constructed by inserting amino acid between A552 and V553 (inserted mutantion motif II, IMII) and D662 and S663 (inserted mutantion motif IV, IMIV). Variants with catalytic activity are screened of library which synthesize high molecular weight alpha-glucans with different proportions of alpha(1-4) linkages ranging from 0 to 52%. Mutant dextransucrases which synthesize hyperbranched dextran are obtained
-
additional information
-
optimization of culture conditions for high-level lactose-inducible expression of Leuconostoc mesenteroides dextransucrase in recombinant Escherichia coli strain BL 21(DE3), overview. Maximal activity of 60.18 U/ml from a fed-batch culture at 5 g/l lactose, added at an OD600 of 3.0, at 25°C for 7 h
-
additional information
-
DSR-S1-DELTAV (residues 1-1425) and DSR-S2-DELTA(V) (residues 1-1279) are constructed by deleting partial YG repeats of domain V. DSR-S3-DELTA(V) (residues 1-1160), DSR-S-DELTA IV (residues 1-1124), and DSR-S-DELTA(B) (residues 1-1110) are constructed by deleting the relevant fragments from C-terminal ends. The truncation mutant DSR-S1-DELTA(A) (residues 1-1029) is constructed by deleting partial domain A while containing complete conserved Motif regions I. DSR-S2-DELTA(A) (residues 1-1022) is constructed by deleting partial domain A including conserved Motif regions I. DSRS3-DELTA(A) (residues 1-1000) is constructed by deleting more domain A fragment, allowing further investigation of the functions of C-terminal end domain. 102 amino acids of C-terminal end has no effect on dextran synthesis, but it will improve enzyme protein expression by deleting these amino acids. After further deletion, polysaccharidesynthesizing capability of dextransucrase will be inhibited. With the addition of maltose as postreceptors, truncated enzymes undergoes glycosylation reaction and transferred glucosyl from sucrose to acceptor effectively. By deleting the 417 amino acid fragment, its oligosaccharide synthesizing capability significantly increases. This is an effective way to make use of dextransucrase for prebiotic synthesis
-
additional information
-
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
additional information
-
construction of two truncated derivative mutants DsrE563DCD2DGBD (DsrE563-1) and DsrE563DCD2DVR (DsrE563-2). Mutant DsrE563-1 with a deletion of 1620 amino acids from the C-terminus, and mutant DsrE563-2 with deletion of 1258 amino acids from the C-terminus and 349 amino acids from the N-terminus, are catalytically active synthesizing less-soluble dextran, mainly containing alpha-1,6 glucosidic linkage, the synthesized less-soluble dextran also has a branched alpha-1,3 linkage. Mutant DsrE563-2 shows 4.5fold higher dextransucrase activity than mutant DsrE563-1 and a higher acceptor reaction efficiency compared to the wild-type enzyme from Leuconostoc mesenteroides strain 512 FMCM when various mono- or disaccharides are used as acceptors
-
additional information
-
construction of a fusion enzyme DXSR of dextransucrase, encoded by gene dsrBCB4, and dextranase, encoded by gene dex2, for one-step synthesis of isomalto-oligosaccharides. DXSR shows 150% increased endo-dextranase activity and 98% decreased dextransucrase activity. The engineered recombinant mutant enzyme DXSR, a fusion of dextransucrase and dextranase, produces linear isomalto-oligosaccharides with DP2-DP10 using sucrose as a sole substrate. DXSR gives 30fold higher production of isomalto-oligosaccharides than that of an equal activity mixture of the two enzymes such as dextranase and dextransucrase
-
additional information
-
the enzyme is usable in the production of isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, alteration of the ratio of sucrose to maltose and the amount of each sugar, overview
-
additional information
-
construction of a truncated mutant of enzyme B-512F, the mutant shows sigmoidal shaped curves when the initial velocities are plotted against the concentration of added dextran. The increase in the reaction rate and the decrease in the sigmoidal curve with increasing dextran concentrations indicate that dextran binds at a noncatalytic or allosteric site to give a more active enzyme
-
additional information
-
generation of diverse mutant enzymes using UV irradiation random mutagensis, mutant screeening, overview. Mutant KIBGE IB-22M20 exhibits 6.75fold increased dextransucrase activity compared to the wild-type enzyme
-
additional information
-
construction of constitutive mutants by chemical mutagenesis using ethyl methane sulfonate in strain Lm M281, overview
-
additional information
-
co-immobilization of dextransucrase and dextranase on calcium alginate for the facilitated synthesis of isomalto-oligosaccharides, reaction scheme, method optimization, and modeling, overview
-
additional information
-
construction of engineered enzyme variants for production of isomalto-oligosaccharides and dextrans of controlled molecular weight of about 10-40 kDa in a one-step process, method optimization, overview
-
additional information
-
rational deletions of the signal peptide, the beginning of the variable region and the last four repeats of the C-terminal end cause no loss of activity. The new variant successfully purified is remarkably stable. With a kcat of 584 per s, it is the most efficient recombinant glucansucrase described to date. The synthesized polymer possesses more than 95% of alpha-1,6 links, like the dextran produced by the native enzyme
-
additional information
-
screening of diverse mutants of the eight conserved residues that are determined to be important for enzyme activity, overview. Construction of enzyme mutant DSR-S vardel DELTA4N
-
additional information
-
construction of fourteen truncated forms of strain NRRL B512-F dextransucrase by N-, C- or N- plus C-terminal domain truncations, dextran binding properties of mutant enzymes, overview
-
additional information
-
the partially purified native enzyme from strain PCSIR-4 is immobilized on alginate for application in the production of dextran from sucrose, method optimization, overview
-
additional information
-
usage of two different artificial intelligence techniques, artificial neural network and genetic algorithm, for optimizing fermentation medium for the production of glucansucrase resulting in production of 6.75 U/ml, method development, overview
additional information
-
usage of two different artificial intelligence techniques, artificial neural network and genetic algorithm, for optimizing fermentation medium for the production of glucansucrase resulting in production of 6.75 U/ml, method development, overview
-
additional information
-
random mutagenesis of the most conserved motif around the transition state stabilizer in glucansucrase GTFR of Streptococcus oralis, yielding different variants with altered reaction specificity, generation of a mutant gtfR library, overview
additional information
-
co-immobilization of the enzyme with dextranase, EC 3.2.1.11, on calcium alginate, optimization of isomalto-oligosacchrides by the system, overview
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biotechnology
-
potential application of the C-terminal enzyme domain GBD-7 as an affinity tag onto cheap resins like for rapid purification of dextrans
biotechnology
-
potential application of the C-terminal enzyme domain GBD-7 as an affinity tag onto cheap resins like for rapid purification of dextrans
-
food industry
-
the enzyme is used to produce kimchi in a fermentation process, which is improved by addition of Ca2+ salts that reduce lactic acid and elevate the pH for optimal activity of Leuconostoc bacteria
food industry
the dextransucrase is responsible for production of dextran with predominant alpha-(1->6) linkages that might find applications as food hydrocolloids
food industry
the enzyme from Weissella confusa strain VTT E-90392 is useful in dextran production during sour dough production. The hydrocolloidal properties of dextran can facilitate a more substantial use of wheat bran and counter the negative effects of bran on bread quality, optimization of enzymatic dextran production in wheat bran
food industry
JX679020
the enzyme is a good food additive for improving the textures of dairy products due to dextran synthesis, e.g. solidification of sucrose-supplemented milk by the enzyme
food industry
-
the exopolysaccharides of Lactobacillus animalis TMW 1.971 improve the quality of gluten-free breads, they can be produced in situ to levels enabling baking applications
food industry
-
the exopolysaccharides of Lactobacillus curvatus TMW 1.624 improve the quality of gluten-free breads, they can be produced in situ to levels enabling baking applications
food industry
-
the exopolysaccharides of Lactobacillus reuteri TMW 1.106 improve the quality of gluten-free breads, they can be produced in situ to levels enabling baking applications
food industry
KY411819
biocatalytic conversion of sucrose into highly porous dextran. Response surface methodology is performed to optimize production conditions. Enhanced biocatalytic efficiency of 4.62fold is observed. The biopolymer produced under the optimized model can be utilized as an emulsifying, gelling, stabilizing and thickening agent in food industry
food industry
-
efficient production of prebiotic glucooligosaccharides in orange juice using immobilized and co-immobilized dextransucrase. Immobilization enhances the operational and storage stability of dextransucrase. Two hundred milligrammes (2.4 IU/mg) of alginate beads (immobilized and co-immobilized) are found to be optimum for the production of glucooligosaccharides (GOS) in orange juice with a high degree of polymerization. The pulp of the orange juice does not interfere in the reaction. In the batch process, coimmobilized dextransucrase (41 g/l) produced a significantly higher amount of GOS than immobilized dextransucrase (37 g/l). Alginate entrapment enhances the thermal stability of dextransucrase for up to 3 days in orange juice at 30°C. The production of GOS in semicontinuous process is 39 g/l in coimmobilized dextransucrase and 33 g/l in immobilized dextransucrase
food industry
-
immobilized enzyme is used successfully in synthesis of dextran and maltooligosaccharide with good prebiotic and fibrinolytic activities. Dextran 38397 and 125471 Da are yielded at enzyme protein concentration 4.78 and 5.78 mg, respectively. Proper dextrans (73378 and 117521 Da) demanded in pharmaceutical applications are achieved at 6% and 12% sucrose concentrations and at 4.78 and 5.78 mg enzyme protein concentration, respectively. Optimum temperature for conversion of glucose to dextran is 30°C (73% and 80% at 5.78 and 4.78 mg enzyme protein concentration, respectively). Varieties of maltooligosaccharides are yielded by synergistic cooperation between sucrose and maltose. Six maltooligosaccharide and three dextrans samples in vitro have prebiotic effect on Lactobacillus casei with degree of variation. Two samples of maltooligosaccharide with different degree of polymerization (DP) and three samples of dextran with different molecular weight (MW) reported different fibrinolytic activity
food industry
-
important enzyme in food industry. Ultrasound is a tool for increasing the activity, thermal stability and rate of catalysis of dextransucrase and supplies a potential method for expanding the application of dextransucrase
food industry
-
synthesis of caffeic acid-3-O-alpha-D-glucopyranoside. The production of caffeic acid-3-O-alpha-D-glucopyranoside at a concentration of 153 mM is optimized using 325 mM caffeic acid, 355 mM sucrose, and 650 mU/ml dextransucrase in the synthesis reaction. In comparison with the caffeic acid, the caffeic acid-3-O-alpha-D-glucopyranoside displays 3fold higher water solubility, 1.66fold higher antilipid peroxidation effect, 15% stronger inhibition of colon cancer cell growth, and 11.5fold higher browning resistance. These results indicate that caffeic acid-3-O-alpha-D-glucopyranoside may be a suitable functional component of food and pharmaceutical products
food industry
-
synthesis of chlorogenic acid-4'-O-alpha-D-glucopyranoside, which is a functional component that may be used in the food or pharmaceutical industry. It displays greater physical properties, anti-lipid peroxidation effect, and growth inhibition of colon cancer cell than those of chlorogenic acid
food industry
-
synthesis of glucosylated steviosides, which are more stable at pH 2, 60°C for 48 h than stevioside
food industry
-
the enzyme catalzes the in vitro synthesis of prebiotic oligosaccharides in mango and pineapple juices. Sucrose content of the juices is eliminated resulting in its lower calorific value. Potential of dextransucrase for production of functional foods
food industry
the enzyme synthesizes dextran and oligosaccharides, which act as prebiotics and are popularly used in such industries as food and medicine
food industry
-
the enzyme catalzes the in vitro synthesis of prebiotic oligosaccharides in mango and pineapple juices. Sucrose content of the juices is eliminated resulting in its lower calorific value. Potential of dextransucrase for production of functional foods
-
food industry
-
the enzyme synthesizes dextran and oligosaccharides, which act as prebiotics and are popularly used in such industries as food and medicine
-
food industry
-
efficient production of prebiotic glucooligosaccharides in orange juice using immobilized and co-immobilized dextransucrase. Immobilization enhances the operational and storage stability of dextransucrase. Two hundred milligrammes (2.4 IU/mg) of alginate beads (immobilized and co-immobilized) are found to be optimum for the production of glucooligosaccharides (GOS) in orange juice with a high degree of polymerization. The pulp of the orange juice does not interfere in the reaction. In the batch process, coimmobilized dextransucrase (41 g/l) produced a significantly higher amount of GOS than immobilized dextransucrase (37 g/l). Alginate entrapment enhances the thermal stability of dextransucrase for up to 3 days in orange juice at 30°C. The production of GOS in semicontinuous process is 39 g/l in coimmobilized dextransucrase and 33 g/l in immobilized dextransucrase
-
food industry
-
the exopolysaccharides of Lactobacillus curvatus TMW 1.624 improve the quality of gluten-free breads, they can be produced in situ to levels enabling baking applications
-
food industry
-
the enzyme from Weissella confusa strain VTT E-90392 is useful in dextran production during sour dough production. The hydrocolloidal properties of dextran can facilitate a more substantial use of wheat bran and counter the negative effects of bran on bread quality, optimization of enzymatic dextran production in wheat bran
-
food industry
-
the enzyme is a good food additive for improving the textures of dairy products due to dextran synthesis, e.g. solidification of sucrose-supplemented milk by the enzyme
-
food industry
-
the exopolysaccharides of Lactobacillus reuteri TMW 1.106 improve the quality of gluten-free breads, they can be produced in situ to levels enabling baking applications
-
food industry
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synthesis of caffeic acid-3-O-alpha-D-glucopyranoside. The production of caffeic acid-3-O-alpha-D-glucopyranoside at a concentration of 153 mM is optimized using 325 mM caffeic acid, 355 mM sucrose, and 650 mU/ml dextransucrase in the synthesis reaction. In comparison with the caffeic acid, the caffeic acid-3-O-alpha-D-glucopyranoside displays 3fold higher water solubility, 1.66fold higher antilipid peroxidation effect, 15% stronger inhibition of colon cancer cell growth, and 11.5fold higher browning resistance. These results indicate that caffeic acid-3-O-alpha-D-glucopyranoside may be a suitable functional component of food and pharmaceutical products
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food industry
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the enzyme is used to produce kimchi in a fermentation process, which is improved by addition of Ca2+ salts that reduce lactic acid and elevate the pH for optimal activity of Leuconostoc bacteria
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food industry
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synthesis of glucosylated steviosides, which are more stable at pH 2, 60°C for 48 h than stevioside
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food industry
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the dextransucrase is responsible for production of dextran with predominant alpha-(1->6) linkages that might find applications as food hydrocolloids
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food industry
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synthesis of chlorogenic acid-4'-O-alpha-D-glucopyranoside, which is a functional component that may be used in the food or pharmaceutical industry. It displays greater physical properties, anti-lipid peroxidation effect, and growth inhibition of colon cancer cell than those of chlorogenic acid
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food industry
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the exopolysaccharides of Lactobacillus animalis TMW 1.971 improve the quality of gluten-free breads, they can be produced in situ to levels enabling baking applications
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food industry
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important enzyme in food industry. Ultrasound is a tool for increasing the activity, thermal stability and rate of catalysis of dextransucrase and supplies a potential method for expanding the application of dextransucrase
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industry
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the enzyme immobilized on calcium alginate as entrapment matrix can be utilized for synthesis of dextran and can be easily separated from the product, resulting in high purity of dextran
industry
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the immobilized biocatalyst has potential in many industrial applications
industry
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the increased reusability, higher pH range and storage stability of immobilized enzyme as compared with free enzyme can increase the sustainability and applicability of the enzyme in industries
industry
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the immobilized biocatalyst has potential in many industrial applications
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industry
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the enzyme immobilized on calcium alginate as entrapment matrix can be utilized for synthesis of dextran and can be easily separated from the product, resulting in high purity of dextran
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medicine
industrial production of dextrans, that have important medical application in the production of fine chemicals such as plasma substitutes and Sephadex
medicine
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the effects of sodium ions on dextran succrase activity are specific, thus it can be useful to block its catalytic activity, and reducing the cariogenic potential of Streptococcus mutans
medicine
the enzyme synthesizes dextran and oligosaccharides, which act as prebiotics and are popularly used in such industries as food and medicine
medicine
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the enzyme synthesizes dextran and oligosaccharides, which act as prebiotics and are popularly used in such industries as food and medicine
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medicine
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the effects of sodium ions on dextran succrase activity are specific, thus it can be useful to block its catalytic activity, and reducing the cariogenic potential of Streptococcus mutans
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nutrition
industrial production of dextrans, that find use for texture improvement in the food industry, e.g. milk drinks, yogurts and ice cream
nutrition
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immobilisation of dextransucrase from Leuconostoc mesenteroides NRRL B-512F in alginate is optimised for applications in a fluidised bed reactor with high concentrated sugar solutions, in order to allow a continuous formation of defined oligosaccharides as prebiotic isomalto-oligosaccharides
nutrition
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production of controlled molecular weight isomaltooligosaccharides and oligodextrans from sucrose using the combined activity of a dextransucrase, EC 2.4.1.5, from Leuconostoc mesenteroides and endodextranase, EC 3.2.1.11, from Penicillium lilacinum. Higher substrate and dextranase concentrations give rise to products with lower molecular sizes and a dextransucrase/dextranase ratio of 1:1 or 1:2 appears to produce a polymer with a molecular weight which is desirable for prebiotic use
nutrition
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production of controlled molecular weight isomaltooligosaccharides and oligodextrans from sucrose using the combined activity of a dextransucrase, EC 2.4.1.5, from Leuconostoc mesenteroides and endodextranase, EC 3.2.1.11, from Penicillium lilacinum. Higher substrate and dextranase concentrations give rise to products with lower molecular sizes and a dextransucrase/dextranase ratio of 1:1 or 1:2 appears to produce a polymer with a molecular weight which is desirable for prebiotic use
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nutrition
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immobilisation of dextransucrase from Leuconostoc mesenteroides NRRL B-512F in alginate is optimised for applications in a fluidised bed reactor with high concentrated sugar solutions, in order to allow a continuous formation of defined oligosaccharides as prebiotic isomalto-oligosaccharides
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pharmacology
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synthesis of chlorogenic acid-4'-O-alpha-D-glucopyranoside, which is a functional component that may be used in the food or pharmaceutical industry. It displays greater physical properties, anti-lipid peroxidation effect, and growth inhibition of colon cancer cell than those of chlorogenic acid
pharmacology
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synthesis of chlorogenic acid-4'-O-alpha-D-glucopyranoside, which is a functional component that may be used in the food or pharmaceutical industry. It displays greater physical properties, anti-lipid peroxidation effect, and growth inhibition of colon cancer cell than those of chlorogenic acid
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synthesis
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enzymatic synthesis of salicin prodrugs by the reaction of cyclomaltodextrin glucanyltransferase from Bacillus macerans with cyclomaltohexaose and salicyl alcohol which gives a salicin as a major product and the reaction of Leuconostoc mesenteroides B-742CB dextransucrase with sucrose and salicyl alcohol which gives a isosalicin as the major product
synthesis
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alpha-glycosylation by GTFR with sucrose and different alcohols and amino acid derivatives for the synthesis of glycoethers and glycosylated amino acids, which are not easy to obtain by chemical or enzymatic synthetic methods. These products can be used for solid-phase synthesis to generate glycopeptides
synthesis
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potential use of the enzyme in production of glucooligosaccharides containing alpha(1,2) bonds for the dermocosmetic industry
synthesis
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production of dextran
synthesis
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the use of cashew apple juice as substrate is an interesting alternative to grow Leconostoc mesenteroides and to produce dextransucrase. High enzyme activities are obtained even when the substrate is used without yeast extract or phosphate addition
synthesis
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engineered enzyme variants are capable to produce isomalto-oligosaccharides and dextrans of controlled molecular weight of about 10-40 kDa in a one-step process, overview
synthesis
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the enzyme is usable in the production of isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, overview
synthesis
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Leuconostoc mesenteroides dextransucrase is useful for enzymatic synthesis of alkyl alpha-D-glucosides, best yield is 50% using 1-butyl alpha-D-glucoside with 0.9 M 1-butanol
synthesis
one-step synthesis of isomalto-oligosaccharides by a fusion enzyme of dextransucrase and dextranase
synthesis
the enzyme is useful for production of L-ascorbic acid 2-glucoside for use as an antioxidant in industrial applications
synthesis
the strain Leuconostoc citreum strain B/110-1-2 is used for industrial production of dextran and dextran derivatives
synthesis
purified Weissella confusa Cab3 dextransucrase (WcCab3-DSR) is used for in vitro synthesis of dextran and glucooligosaccharides
synthesis
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combined use of dextransucrase and dextranase and the maltose acceptor is a simple and effective method to promote the high-quality of functional isomaltooligosaccharides
synthesis
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synthesis of glucosylated steviosides, which are more stable at pH 2, 60°C for 48 h than stevioside
synthesis
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the mutant enzyme is highly suitable for the synthesis of different flavonoid glucosides. For substrates such as quercetin and its glycosides, a high glucosylation efficiency is achieved, whereas the incubation of e.g. neohesperidin dihydrochalcone and naringin only yields low portions of glucoconjugates. The different substrates are not only glucosylated with varying efficiencies but also at different positions. While glucosylation of the phenolic hydroxyl groups of the flavonoid B-ring occurrs almost exclusively at position O4', flavonoid bound beta-glucosyl units are conjugated at position O3, O4, and O6 depending on the substrate. It is possible to demonstrate that flavonoids with a rutinose and a neohesperidose residue can be glucosylated either at position O6 of the glucose unit or at position O4 of the alpha-rhamnose unit
synthesis
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the enzyme is usable in the production of isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, overview
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synthesis
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one-step synthesis of isomalto-oligosaccharides by a fusion enzyme of dextransucrase and dextranase
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synthesis
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engineered enzyme variants are capable to produce isomalto-oligosaccharides and dextrans of controlled molecular weight of about 10-40 kDa in a one-step process, overview
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synthesis
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Leuconostoc mesenteroides dextransucrase is useful for enzymatic synthesis of alkyl alpha-D-glucosides, best yield is 50% using 1-butyl alpha-D-glucoside with 0.9 M 1-butanol
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synthesis
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enzymatic synthesis of salicin prodrugs by the reaction of cyclomaltodextrin glucanyltransferase from Bacillus macerans with cyclomaltohexaose and salicyl alcohol which gives a salicin as a major product and the reaction of Leuconostoc mesenteroides B-742CB dextransucrase with sucrose and salicyl alcohol which gives a isosalicin as the major product
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synthesis
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the mutant enzyme is highly suitable for the synthesis of different flavonoid glucosides. For substrates such as quercetin and its glycosides, a high glucosylation efficiency is achieved, whereas the incubation of e.g. neohesperidin dihydrochalcone and naringin only yields low portions of glucoconjugates. The different substrates are not only glucosylated with varying efficiencies but also at different positions. While glucosylation of the phenolic hydroxyl groups of the flavonoid B-ring occurrs almost exclusively at position O4', flavonoid bound beta-glucosyl units are conjugated at position O3, O4, and O6 depending on the substrate. It is possible to demonstrate that flavonoids with a rutinose and a neohesperidose residue can be glucosylated either at position O6 of the glucose unit or at position O4 of the alpha-rhamnose unit
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synthesis
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synthesis of glucosylated steviosides, which are more stable at pH 2, 60°C for 48 h than stevioside
-
synthesis
-
the enzyme is useful for production of L-ascorbic acid 2-glucoside for use as an antioxidant in industrial applications
-
synthesis
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potential use of the enzyme in production of glucooligosaccharides containing alpha(1,2) bonds for the dermocosmetic industry
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synthesis
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the strain Leuconostoc citreum strain B/110-1-2 is used for industrial production of dextran and dextran derivatives
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