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1-kestotriose + sucrose
1,6-kestotetraose + ?
-
1-kestotriose is the preferred substrate
-
-
?
2 sucrose
6-kestose + D-glucose
2 sucrose
D-glucose + beta-D-fructofuranosyl-(2,6)-beta-D-fructofuranosyl-(2,1)-alpha-D-glucopyranoside
6G-kestotriose + sucrose
6-kestotriose + ?
-
-
-
-
?
alpha-D-galactopyranosyl-1,2-beta-D-fructofuranoside + alpha-D-galactopyranosyl-1,2-beta-D-fructofuranoside
?
alpha-D-mannopyranosyl-1,2-beta-D-fructofuranoside + alpha-D-mannopyranosyl-1,2-beta-D-fructofuranoside
?
alpha-D-xylopyranosyl-1,2-beta-D-fructofuranoside + alpha-D-xylopyranosyl-1,2-beta-D-fructofuranoside
?
D-raffinose
D-fructose + melibiose
-
-
-
?
jaggary
D-glucose + fructose + kestose + nystose + difructose + levan
raffinose + (2,6-beta-D-fructosyl)n
galactose + (2,6-beta-D-fructosyl)n+1
stachyose + (2,6-beta-D-fructosyl)n
?
-
-
-
-
?
sucrose
levan + fructooligosaccharides
sucrose + (2,6-beta-D-fructosyl)n
alpha-D-glucose + (2,6-beta-D-fructosyl)n+1
sucrose + (2,6-beta-D-fructosyl)n
D-glucose + (2,6-beta-D-fructosyl)n+1
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
sucrose + ?
polyfructan + ?
sucrose + acarbose
D-glucose + 1'-beta-D-fructofuranosyl alpha-acarbose
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n+1
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-beta-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-beta-D-fructosyl]n+1
sucrose + arabinose
?
-
-
-
?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
sucrose + cellobiose
?
-
-
-
-
?
sucrose + cellobiose
beta-D-glucopyranosyl-(1,4)-alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranoside + D-glucose
sucrose + cellobiose
D-glucose + beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
sucrose + cellobiose
fructosylated cellobiose + ?
sucrose + D-arabinose
?
-
-
-
-
?
sucrose + D-fucose
beta-D-fructofuranosyl-alpha-D-fucopyranoside + D-glucose
sucrose + D-galactose
?
-
-
-
-
?
sucrose + D-galactose
beta-D-fructofuranosyl-alpha-D-galactopyranoside + D-glucose
sucrose + D-glucose
glucose + sucrose
sucrose + D-xylose
beta-D-fructofuranosyl-alpha-D-xylopyranoside + D-glucose
sucrose + D-xylose
beta-D-fructofuranosyl-beta-D-xylopyranoside + D-glucose
-
-
-
?
sucrose + D-xylose
D-glucose + alpha-D-xylopyranosyl-(1->2)-beta-D-fructofuranoside
sucrose + D-xylose
D-glucose + beta-D-fructofuranosyl-(2,1)-alpha-D-xylopyranoside
-
-
NMR product analysis
-
?
sucrose + fructose
?
-
-
-
?
sucrose + galactose
Fru(beta-2,6)Gal + ?
sucrose + glucose
1-kestotriose + 6-kestotriose + 1-kestotetraose + ?
sucrose + glucose
?
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
sucrose + H2O
glucose + fructose + levan + sucrose + fructooligosaccharides
-
-
-
-
?
sucrose + hydroquinone
D-glucose + 4-hydroxyphenyl-beta-D-fructofuranoside
sucrose + inositol
?
-
low activity
-
-
?
sucrose + inulin
?
-
-
-
-
?
sucrose + isomaltose
D-glucose + theanderose
sucrose + isomaltose
isomaltosyl-fructose + D-glucose
-
-
-
?
sucrose + L-arabinose
6-kestotriose + ?
-
-
-
?
sucrose + L-arabinose
6-kestotriose + fructosylated L-arabinose
-
-
-
?
sucrose + L-arabinose
?
-
-
-
-
?
sucrose + L-galactose
beta-D-fructofuranosyl-beta-L-galactopyranoside + D-glucose
-
-
-
?
sucrose + L-glucose
beta-D-fructofuranosyl-beta-L-glucopyranoside + D-glucose
-
-
-
?
sucrose + L-xylose
beta-D-fructofuranosyl-beta-L-xylopyranoside + D-glucose
-
-
-
?
sucrose + lactose
beta-D-galactopyranosyl-(1,4)-alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranoside + D-glucose
-
-
-
?
sucrose + lactose
D-glucose + beta-D-fructofuranosyl-beta-D-galactopyranosyl-(1-4)-beta-D-glucopyranoside
-
-
-
-
?
sucrose + lactose
D-glucose + beta-D-galactopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
sucrose + lactose
D-glucose + beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
sucrose + lactose
D-glucose + lactosylfructoside
sucrose + lactose
D-glucose + O-beta-D-galactopyranosyl-(1,4)-O-beta-D-glucopyranosyl-(1,2)-beta-D-fructofuranoside
sucrose + lactose
fructosylated lactose + ?
-
-
-
?
sucrose + lactose
lactosucrose
sucrose + lactose
lactosucrose + D-glucose
the production condition is optimized as pH at 6.0, temperature at 35°C, 5 units/ml enzyme, 180 g/l sucrose, and 180 g/l lactose
-
-
?
sucrose + levan
?
mutant enzymes H243L and S164A synthesize either high or low levan molecular weight
-
-
?
sucrose + maltose
D-glucose + alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
sucrose + maltose
erlose + D-glucose
-
-
-
?
sucrose + maltotriose
?
-
-
-
-
?
sucrose + mannose
?
-
-
-
?
sucrose + melibiose
?
-
-
-
-
?
sucrose + melibiose
D-glucose + raffinose
sucrose + melibiose
raffinose + D-glucose
sucrose + methanol
glucose + methyl-beta-D-fructoside
sucrose + polygalacturonic acid
?
-
-
-
?
sucrose + raffinose
Fru(beta-2,1)Gal + fructosylated lactose + fructosylated cellobiose + 1-kestotriose + 6-kestotriose + ?
-
-
-
?
sucrose + raffinose
melibiose + ?
-
-
-
-
?
sucrose + raffinose
melibiose + D-fructose + levan
-
-
-
?
sucrose + stachyose
manninotriose + D-fructose
-
-
-
?
sucrose + sucrose
1-kestose + 6-kestose + neo-kestose + ?
sucrose + sucrose
6-kestose + levanbiose + blastose + 1-kestose + ?
sucrose + sucrose
D-glucose + (2,6-beta-D-fructosyl)3
Q60114
dimer form
degree of polymerisation 3
-
?
sucrose + sucrose
D-glucose + 1-kestose
sucrose + sucrose
D-glucose + 1-kestose + nystose + ?
sucrose + sucrose
D-glucose + 6-kestose
sucrose + sucrose
D-glucose + 6-kestose + 6-nystose + 6,6,6-kestopentaose + levanbiose + levantriose + ?
sucrose + sucrose
D-glucose + levan
sucrose + sucrose
D-glucose + levan + fructooligosaccharides
-
-
-
?
sucrose + sucrose
D-glucose + levan type-fructan
sucrose + sucrose
D-glucose + low-molecular weight levan + short-chain fructooligosaccharides (DP 3-6)
sucrose + sucrose
D-glucose + neokestose
-
-
identified by one-dimensional and correlation spectroscopy (i.e. COSY, TOCSY, HMBC, DEPT and HSQC)
-
?
sucrose + sucrose
D-glucose + nystose
-
-
identified by HPAEC
-
?
sucrose + sucrose
kestose + D-glucose
-
high concentration of sucrose
-
-
?
sucrose + triisopropylbenzenesulfonyllevan
?
-
-
-
-
?
sucrose + [6)-beta-D-fructofuranosyl-(2->]n alpha-D-glucopyranoside
D-glucose + [6)-beta-D-fructofuranosyl-(2->]n+1 alpha-D-glucopyranoside
Q60114
pH lower than 7.0, fibril form
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
surgarcane molasse
D-glucose + fructose + kestose + nystose + difructose + levan
-
-
-
?
sweet sorghum juice
D-glucose + fructose + kestose + nystose + difructose + levan
-
-
-
?
table sugar
D-glucose + fructose + kestose + nystose + difructose + levan
-
-
-
?
additional information
?
-
2 sucrose
6-kestose + D-glucose
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
?
2 sucrose
6-kestose + D-glucose
-
-
-
-
?
2 sucrose
D-glucose + beta-D-fructofuranosyl-(2,6)-beta-D-fructofuranosyl-(2,1)-alpha-D-glucopyranoside
-
-
-
-
?
2 sucrose
D-glucose + beta-D-fructofuranosyl-(2,6)-beta-D-fructofuranosyl-(2,1)-alpha-D-glucopyranoside
-
-
-
-
?
alpha-D-galactopyranosyl-1,2-beta-D-fructofuranoside + alpha-D-galactopyranosyl-1,2-beta-D-fructofuranoside
?
-
besides the major product, levan, the enzyme produces two galactosyloligofructosides with D-Gal-Fru
-
-
?
alpha-D-galactopyranosyl-1,2-beta-D-fructofuranoside + alpha-D-galactopyranosyl-1,2-beta-D-fructofuranoside
?
-
besides the major product, levan, the enzyme produces two galactosyloligofructosides with D-Gal-Fru
-
-
?
alpha-D-mannopyranosyl-1,2-beta-D-fructofuranoside + alpha-D-mannopyranosyl-1,2-beta-D-fructofuranoside
?
-
only one mannosyloligofructoside is formed
-
-
?
alpha-D-mannopyranosyl-1,2-beta-D-fructofuranoside + alpha-D-mannopyranosyl-1,2-beta-D-fructofuranoside
?
-
only one mannosyloligofructoside is formed
-
-
?
alpha-D-xylopyranosyl-1,2-beta-D-fructofuranoside + alpha-D-xylopyranosyl-1,2-beta-D-fructofuranoside
?
-
besides the major product, levan, the enzyme produces at least three different xylosyloligofructosides with D-Xyl-Fru
-
-
?
alpha-D-xylopyranosyl-1,2-beta-D-fructofuranoside + alpha-D-xylopyranosyl-1,2-beta-D-fructofuranoside
?
-
besides the major product, levan, the enzyme produces at least three different xylosyloligofructosides with D-Xyl-Fru
-
-
?
inulin + H2O
?
-
-
-
-
?
jaggary
D-glucose + fructose + kestose + nystose + difructose + levan
-
-
-
?
jaggary
D-glucose + fructose + kestose + nystose + difructose + levan
-
-
-
?
raffinose + (2,6-beta-D-fructosyl)n
galactose + (2,6-beta-D-fructosyl)n+1
-
-
the levan synthesized on raffinose contains one mol of galactosylglucose per mol as one of the 2 terminal glycosyl moieties
?
raffinose + (2,6-beta-D-fructosyl)n
galactose + (2,6-beta-D-fructosyl)n+1
-
in 0.38 M phosphate buffer
-
-
?
raffinose + (2,6-beta-D-fructosyl)n
galactose + (2,6-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose
levan + fructooligosaccharides
the reaction occurs only in the presence of high salt concentrations (more than 1.5 M NaCl)
-
-
?
sucrose
levan + fructooligosaccharides
the reaction occurs only in the presence of high salt concentrations (more than 1.5 M NaCl)
-
-
?
sucrose
levan + kestose
-
at concentrations below 85 mM (at 37°C). Above 85 mM sucrose, the transglycosylation activity of Lev gradually becomes significant. Transglycosylation never exceeds 50% of total enzyme activity
-
-
?
sucrose
levan + kestose
-
at concentrations below 85 mM (at 37°C). Above 85 mM sucrose, the transglycosylation activity of Lev gradually becomes significant. Transglycosylation never exceeds 50% of total enzyme activity
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
alpha-D-glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
alpha-D-glucose + (2,6-beta-D-fructosyl)n+1
-
capacity to produce extracellular homopolysaccharides of fructose, modulation of the composition of the biofilms that form on teeth
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
alpha-D-glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
alpha-D-glucose + (2,6-beta-D-fructosyl)n+1
-
capacity to produce extracellular homopolysaccharides of fructose, modulation of the composition of the biofilms that form on teeth
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
D-glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
D-glucose + (2,6-beta-D-fructosyl)n+1
-
reduction of glucose by yeasts (Candida cacaoi DSM 2226), introduced into a dialysing membrane, situated in the reaction medium, and the presence of Mn2+ results in an increase of levan synthesis efficiency to 64%
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
D-glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
D-glucose + (2,6-beta-D-fructosyl)n+1
-
polyfructan produced by the levansucrase from Bacillus megaterium has a molecular mass of 2711 kDa and consisted mainly of beta(2,6) linkages. Besides the polyfructan formation, the wild-type levansucrase of Bacillus megaterium also synthesizes five different detectable oligosaccharides. Three products are identified: 1-kestose (isokestose), 6-kestose and nystose which are known acceptors for the transfer of fructosyl units
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
D-glucose + (2,6-beta-D-fructosyl)n+1
-
polyfructan produced by the levansucrase from Bacillus megaterium has a molecular mass of 2711 kDa and consisted mainly of beta(2,6) linkages. Besides the polyfructan formation, the wild-type levansucrase of Bacillus megaterium also synthesizes five different detectable oligosaccharides. Three products are identified: 1-kestose (isokestose), 6-kestose and nystose which are known acceptors for the transfer of fructosyl units
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
reverse reaction is probably catalyzed by a different levanase
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
enzyme is probably involved in initiation and progression of dental caries and periodontal diseases
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
reverse reaction is probably catalyzed by a different levanase
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
enzyme is probably involved in initiation and progression of dental caries and periodontal diseases
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
high molecular weight branched levan, product forms a complex with the enzyme
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
Aerobacter levanicum
-
-
product forms a complex with the enzyme
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
Aerobacter levanicum
-
levan biosynthesis
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
activity is affected by sacU mutation
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
r
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
r
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
r
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
polymerase and hydrolase activity can be separately modulated by site-directed mutagenesis
-
r
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
reaction kinetics are dependent on sucrose concentration
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
activity is affected by sacU mutation
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
r
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
activity is affected by sacU mutation
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
various acceptors
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
beta-D-fructofuranosidase activity
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
synthesis of a high-molecular-mass fructan of the levan type
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
translocation of the enzyme is a rate-limiting step
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
additional beta-fructosidase, i.e. invertase, sucrose-sucrose 1-fructosyltransferase, and sucrose-sucrose 6-fructosyltransferase activities of recombinant enzyme from Pichia pastoris
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
various acceptors, e.g. fructosyl acceptors 2-1 linked or 2-6 linked, including water, the latter belongs to a fructosidase, i.e. invertase, activity of the purified enzyme, overview
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
transgenic plants
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
transgenic plants
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
biosynthesis of fructans, important in assimilate partitioning and possibly in stress tolerance in plants
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
key enzyme for the formation of the graminans and phleins
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
hydrolase, i.e. invertase, and transferase activities can be altered by modifying reaction conditions
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
beta-D-fructofuranosidase activity
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
molecular weight of levan product is dependent on temperature, salinity, and sucrose concentration
r
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
various D-fructosyl acceptors, overview
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
transfucosylation from sucrose to various acceptors, except sugar alcohols
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
the degree of polymerization of levan produced at high temperature is lower than that produced at low temperature
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
transfucosylation from sucrose to various acceptors, except sugar alcohols
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
the degree of polymerization of levan produced at high temperature is lower than that produced at low temperature
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
various D-fructosyl acceptors, overview
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
-
r
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
Q60114
-
-
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
-
enzyme plays an important role in the production of ethanol from sugar cane and other sucrose sources
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
Q60114
-
molecular weight of produced levan is dependent on preparation method, immobilized recombinant enzyme and recombinant enzyme in permeabilized E. coli cells produces low molecular weight levan, free recombinant enzyme produces high molecular weight levan
?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
at lower temperatures, such as 5°C and 15°C and pH 4.0-6.0 the transfructosylation is preferentially catalyzed rather than the hydrolysis of sucrose, but inversely at higher temperatures such as 30°C and 40°C and pH 7.0-8.0 the hydrolysis is preferentially catalyzed
-
r
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
enzyme catalyzes the liberation of reducing sugars from substrates having 2-beta-D-fructofuranose residues on a terminal such as sucrose, raffinose, levan from Aerobacter levanicum and inulin with a relative activity of 100:104:1:0.01
-
r
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
Q60114
-
-
?
sucrose + ?
blastose + ?
-
-
two-dimensional COSY, TOCSY, HMBC and HSQC experiments
-
?
sucrose + ?
blastose + ?
-
-
two-dimensional COSY, TOCSY, HMBC and HSQC experiments
-
?
sucrose + ?
polyfructan + ?
-
-
polyfructan, molecular mass of 2711 kDa and consisted mainly of beta(2-6) linkages
-
?
sucrose + ?
polyfructan + ?
-
-
polyfructan, molecular mass of 2711 kDa and consisted mainly of beta(2-6) linkages
-
?
sucrose + acarbose
D-glucose + 1'-beta-D-fructofuranosyl alpha-acarbose
-
-
product analysis and structure determination by NMR spectroscopy
-
?
sucrose + acarbose
D-glucose + 1'-beta-D-fructofuranosyl alpha-acarbose
-
-
product analysis and structure determination by NMR spectroscopy
-
?
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n+1
-
-
-
-
?
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n+1
-
-
-
-
?
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n+1
-
-
-
?
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n+1
-
-
-
?
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-beta-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-beta-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
the highest product molecular weight of 38 kDa is reached at 30°C, and gradually decreases at higher temperatures
-
-
?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
sucrose is used as a starter unit to which fructose residues, cleaved from another sucrose molecule, become attached
-
-
?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
sucrose is used as a starter unit to which fructose residues, cleaved from another sucrose molecule, become attached
-
-
?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + cellobiose
beta-D-glucopyranosyl-(1,4)-alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranoside + D-glucose
-
-
-
?
sucrose + cellobiose
beta-D-glucopyranosyl-(1,4)-alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranoside + D-glucose
-
-
-
?
sucrose + cellobiose
D-glucose + beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
-
the major transfructosylation product is identified to be cellobiose-fructose (beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside)
-
?
sucrose + cellobiose
D-glucose + beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
-
-
-
-
?
sucrose + cellobiose
D-glucose + beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
-
-
-
-
?
sucrose + cellobiose
fructosylated cellobiose + ?
-
-
-
?
sucrose + cellobiose
fructosylated cellobiose + ?
-
-
-
?
sucrose + D-fucose
beta-D-fructofuranosyl-alpha-D-fucopyranoside + D-glucose
-
-
-
?
sucrose + D-fucose
beta-D-fructofuranosyl-alpha-D-fucopyranoside + D-glucose
-
-
-
?
sucrose + D-galactose
beta-D-fructofuranosyl-alpha-D-galactopyranoside + D-glucose
-
-
-
?
sucrose + D-galactose
beta-D-fructofuranosyl-alpha-D-galactopyranoside + D-glucose
-
-
-
?
sucrose + D-glucose
glucose + sucrose
-
exchange reaction
-
?
sucrose + D-glucose
glucose + sucrose
-
exchange reaction
-
?
sucrose + D-maltose
?
-
-
-
?
sucrose + D-maltose
?
-
-
-
-
?
sucrose + D-maltose
?
-
-
-
-
?
sucrose + D-maltose
?
-
-
-
-
?
sucrose + D-sorbitol
?
-
low activity
-
-
?
sucrose + D-sorbitol
?
-
-
-
-
?
sucrose + D-sorbitol
?
-
-
-
-
?
sucrose + D-xylose
?
-
-
-
?
sucrose + D-xylose
?
-
-
-
?
sucrose + D-xylose
?
-
-
-
-
?
sucrose + D-xylose
?
-
-
-
-
?
sucrose + D-xylose
beta-D-fructofuranosyl-alpha-D-xylopyranoside + D-glucose
-
-
-
?
sucrose + D-xylose
beta-D-fructofuranosyl-alpha-D-xylopyranoside + D-glucose
-
-
-
?
sucrose + D-xylose
D-glucose + alpha-D-xylopyranosyl-(1->2)-beta-D-fructofuranoside
-
-
-
-
?
sucrose + D-xylose
D-glucose + alpha-D-xylopyranosyl-(1->2)-beta-D-fructofuranoside
-
-
-
-
?
sucrose + galactose
Fru(beta-2,6)Gal + ?
-
-
-
?
sucrose + galactose
Fru(beta-2,6)Gal + ?
-
-
-
?
sucrose + glucose
1-kestotriose + 6-kestotriose + 1-kestotetraose + ?
-
-
-
?
sucrose + glucose
1-kestotriose + 6-kestotriose + 1-kestotetraose + ?
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
hydrolysis
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
hydrolysis
-
-
?
sucrose + hydroquinone
D-glucose + 4-hydroxyphenyl-beta-D-fructofuranoside
-
-
NMR product analysis, the product shows anti-oxidation activities and inhibition of tyrosinase and of 1,1-diphenyl-2-picrylhydrazyl scavenging activity, it also shows inhibition of lipid peroxidation, kinetics, overview
-
?
sucrose + hydroquinone
D-glucose + 4-hydroxyphenyl-beta-D-fructofuranoside
-
-
NMR product analysis, the product shows anti-oxidation activities and inhibition of tyrosinase and of 1,1-diphenyl-2-picrylhydrazyl scavenging activity, it also shows inhibition of lipid peroxidation, kinetics, overview
-
?
sucrose + isomaltose
D-glucose + theanderose
-
-
-
-
?
sucrose + isomaltose
D-glucose + theanderose
-
-
-
-
?
sucrose + isomaltose
D-glucose + theanderose
-
-
-
-
?
sucrose + lactose
?
-
-
-
?
sucrose + lactose
?
-
-
-
?
sucrose + lactose
?
-
-
-
-
?
sucrose + lactose
?
-
-
-
-
?
sucrose + lactose
?
-
-
-
-
?
sucrose + lactose
D-glucose + beta-D-galactopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
-
-
-
-
?
sucrose + lactose
D-glucose + beta-D-galactopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
-
-
-
-
?
sucrose + lactose
D-glucose + beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
-
the major transfructosylation product is identified to be lactosefructose or lactosucrose (beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside)
-
?
sucrose + lactose
D-glucose + beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
optimized conditions are pH 6.5, 50°C, 27% w/v sucrose, 27% w/v lactose, and 5 U/ml of the purified recombinant enzyme
i.e. lactosefructose or lactosucrose
-
?
sucrose + lactose
D-glucose + beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
optimized conditions are pH 6.5, 50°C, 27% w/v sucrose, 27% w/v lactose, and 5 U/ml of the purified recombinant enzyme
i.e. lactosefructose or lactosucrose
-
?
sucrose + lactose
D-glucose + lactosylfructoside
-
method optimization for lactosylfructoside biosynthesis, overview. Equal concentration of the two substrates showed a better performance than the other concentration ratios
lactosylfructoside is a functional oligosaccharide consisting of D-glucose, D-galactose, and D-fructose. Purification of the trisaccharide from the product using a HPLC system and confirmation by NMR spectroscopy
-
?
sucrose + lactose
D-glucose + lactosylfructoside
-
method optimization for lactosylfructoside biosynthesis, overview. Equal concentration of the two substrates showed a better performance than the other concentration ratios
lactosylfructoside is a functional oligosaccharide consisting of D-glucose, D-galactose, and D-fructose. Purification of the trisaccharide from the product using a HPLC system and confirmation by NMR spectroscopy
-
?
sucrose + lactose
D-glucose + O-beta-D-galactopyranosyl-(1,4)-O-beta-D-glucopyranosyl-(1,2)-beta-D-fructofuranoside
-
levansucrase transfers the fructosyl moiety of sucrose to lactose to form lactosucrose
i.e. lactosucrose or 4G-beta-D-galactosylsucrose
-
?
sucrose + lactose
D-glucose + O-beta-D-galactopyranosyl-(1,4)-O-beta-D-glucopyranosyl-(1,2)-beta-D-fructofuranoside
-
levansucrase transfers the fructosyl moiety of sucrose to lactose to form lactosucrose, optimization of reaction conditions, 28.5% conversion in absence and 43.2% in presence of glucose oxidase, which eliminates the inhibitory D-glucose reaction product, overview
i.e. lactosucrose or 4G-beta-D-galactosylsucrose, product identification and quantification by NMR spectroscopy
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
Bacillus subtilis is the most effective producer of lactofructose
-
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
-
-
-
?
sucrose + maltose
?
-
-
-
?
sucrose + maltose
?
-
-
-
?
sucrose + maltose
?
-
-
-
-
?
sucrose + maltose
D-glucose + alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
-
-
-
-
?
sucrose + maltose
D-glucose + alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside
-
-
-
-
?
sucrose + melibiose
D-glucose + raffinose
-
-
-
?
sucrose + melibiose
D-glucose + raffinose
-
when 30% (w/v) sucrose and 30% (w/v) melibiose are catalyzed using 3% (w/v) whole cells at pH 6.5 (50 mM sodium phosphate buffer) and 55°C, the highest raffinose yield is 222 g/l after a 6 h reaction. The conversion ratio from each substrate to raffinose is 50%
-
-
?
sucrose + melibiose
D-glucose + raffinose
-
when 30% (w/v) sucrose and 30% (w/v) melibiose are catalyzed using 3% (w/v) whole cells at pH 6.5 (50 mM sodium phosphate buffer) and 55°C, the highest raffinose yield is 222 g/l after a 6 h reaction. The conversion ratio from each substrate to raffinose is 50%
-
-
?
sucrose + melibiose
raffinose + D-glucose
-
-
-
?
sucrose + melibiose
raffinose + D-glucose
-
-
-
?
sucrose + methanol
glucose + methyl-beta-D-fructoside
-
-
-
-
?
sucrose + methanol
glucose + methyl-beta-D-fructoside
-
-
-
?
sucrose + sorbitol
?
-
-
-
?
sucrose + sorbitol
?
-
-
-
?
sucrose + sucrose
1-kestose + 6-kestose + neo-kestose + ?
-
-
-
?
sucrose + sucrose
1-kestose + 6-kestose + neo-kestose + ?
-
-
-
?
sucrose + sucrose
1-kestose + 6-kestose + neo-kestose + ?
-
-
-
?
sucrose + sucrose
1-kestose + 6-kestose + neo-kestose + ?
-
-
-
?
sucrose + sucrose
1-kestose + 6-kestose + neo-kestose + ?
-
-
-
-
?
sucrose + sucrose
1-kestose + 6-kestose + neo-kestose + ?
-
-
-
-
?
sucrose + sucrose
6-kestose + levanbiose + blastose + 1-kestose + ?
-
-
-
-
?
sucrose + sucrose
6-kestose + levanbiose + blastose + 1-kestose + ?
-
-
-
-
?
sucrose + sucrose
?
-
-
-
-
?
sucrose + sucrose
?
-
product concentrations of fructose, kestose or fructan depend on the concentration of sucrose, pH and temperatur
-
-
?
sucrose + sucrose
D-glucose + 1-kestose
-
-
identified by HPAEC
-
?
sucrose + sucrose
D-glucose + 1-kestose
-
-
identified by HPAEC
-
?
sucrose + sucrose
D-glucose + 1-kestose + nystose + ?
-
-
-
-
?
sucrose + sucrose
D-glucose + 1-kestose + nystose + ?
-
-
-
-
?
sucrose + sucrose
D-glucose + 6-kestose
-
-
identified by HPAEC
-
?
sucrose + sucrose
D-glucose + 6-kestose
-
-
identified by HPAEC
-
?
sucrose + sucrose
D-glucose + 6-kestose + 6-nystose + 6,6,6-kestopentaose + levanbiose + levantriose + ?
-
-
-
-
?
sucrose + sucrose
D-glucose + 6-kestose + 6-nystose + 6,6,6-kestopentaose + levanbiose + levantriose + ?
-
-
-
?
sucrose + sucrose
D-glucose + 6-kestose + 6-nystose + 6,6,6-kestopentaose + levanbiose + levantriose + ?
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
the enzyme has high product specificity, and no fructooligosaccharide is identified in the product
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
the recombinant enzyme shows 80% conversion yield
-
-
?
sucrose + sucrose
D-glucose + levan
the recombinant enzyme shows 80% conversion yield
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
-
-
?
sucrose + sucrose
D-glucose + levan
-
is assayed in a standard reaction containing 1 ml 10% sucrose and 1 ml enzyme (0.01-0.05mg/ml) incubated at 15°C
-
-
?
sucrose + sucrose
D-glucose + levan type-fructan
-
-
-
?
sucrose + sucrose
D-glucose + levan type-fructan
-
-
-
?
sucrose + sucrose
D-glucose + low-molecular weight levan + short-chain fructooligosaccharides (DP 3-6)
-
-
-
?
sucrose + sucrose
D-glucose + low-molecular weight levan + short-chain fructooligosaccharides (DP 3-6)
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
additional information
?
-
Aerobacter levanicum
-
6-beta-D-fructosyl)n is levan
-
-
?
additional information
?
-
design and evaluation of a bi-enzymatic system: combined use of levansucrase from Bacillus amyloliquefaciens and endoinulinase from Aspergillus niger in a one-step reaction for the synthesis of fructooligosaccharides (FOS) and oligolevans using sucrose as the sole substrate, overview. At the initial stage of time course, short chain fructooligosaccharides, 1-kestose, nystose, and 1F-fructosylnystose are the major products, whilst 6-kestose, medium chain fructooligosaccharides (mcFOSs, levanohexaose, levanopentaose) and oligolevans become the dominant ones at the late stage. NMR analysis of levan, levanopentaose and levanohexaose, overview
-
-
?
additional information
?
-
levansucrase catalyzes simultaneously both the transfructosylation and the hydrolysis, which is regarded as the transfer of the fructosyl group to water, time courses for transfructosylation and hydrolysis reactions, overview. Measurement of sucrose hydrolysis releasing D-glucose and D-fructose. Disaccharides lactose, cellobiose and melibiose are used as acceptors, with high acceptor specificity towards lactose. Maple syrup is used as assay medium and sucrose source, profile of the end-products synthesized by the enzyme, overview
-
-
?
additional information
?
-
-
levansucrase catalyzes simultaneously both the transfructosylation and the hydrolysis, which is regarded as the transfer of the fructosyl group to water, time courses for transfructosylation and hydrolysis reactions, overview. Measurement of sucrose hydrolysis releasing D-glucose and D-fructose. Disaccharides lactose, cellobiose and melibiose are used as acceptors, with high acceptor specificity towards lactose. Maple syrup is used as assay medium and sucrose source, profile of the end-products synthesized by the enzyme, overview
-
-
?
additional information
?
-
design and evaluation of a bi-enzymatic system: combined use of levansucrase from Bacillus amyloliquefaciens and endoinulinase from Aspergillus niger in a one-step reaction for the synthesis of fructooligosaccharides (FOS) and oligolevans using sucrose as the sole substrate, overview. At the initial stage of time course, short chain fructooligosaccharides, 1-kestose, nystose, and 1F-fructosylnystose are the major products, whilst 6-kestose, medium chain fructooligosaccharides (mcFOSs, levanohexaose, levanopentaose) and oligolevans become the dominant ones at the late stage. NMR analysis of levan, levanopentaose and levanohexaose, overview
-
-
?
additional information
?
-
-
levansucrase catalyzes three distinct reactions depending on the fructosyl acceptor molecule, including polymerization, transfructosylation, and hydrolysis. Wide substrate specificity of levansucrase toward monosaccharides, disaccharides, and aromatic and alkyl alcohols, producing diverse sucrose analogues, hetero-oligosaccharides (especially lactosucrose), and fructosides, overview
-
-
?
additional information
?
-
-
broad transglycosylation capability of the levansucrase from Bacillus licheniformis strain 8-37-0-1, substrate specificity, overview. When using sucrose as the donor, the enzyme displays a wide range of acceptor specificity and is able to transfer fructosyl to a series of sugar acceptors including hexose, pentose, beta- or alpha-disaccharides, along with the difficult branched alcohols. Product analysis by mass and NMR spectrometry
-
-
?
additional information
?
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
-
?
additional information
?
-
-
levansucrase catalyzes three distinct reactions depending on the fructosyl acceptor molecule: polymerization (using the growing fructan chain as an acceptor), transfructosylation (using monosaccharides, disaccharides, or oligosaccharides as acceptors), and hydrolysis (using water as an acceptor), overview
-
-
?
additional information
?
-
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
-
broad transglycosylation capability of the levansucrase from Bacillus licheniformis strain 8-37-0-1, substrate specificity, overview. When using sucrose as the donor, the enzyme displays a wide range of acceptor specificity and is able to transfer fructosyl to a series of sugar acceptors including hexose, pentose, beta- or alpha-disaccharides, along with the difficult branched alcohols. Product analysis by mass and NMR spectrometry
-
-
?
additional information
?
-
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
mutant enzymes Y429N and R433A no longer produce levan but exclusively oligosaccharides
-
-
?
additional information
?
-
-
mutant enzymes Y429N and R433A no longer produce levan but exclusively oligosaccharides
-
-
?
additional information
?
-
-
levansucrase catalyzes the synthesis of levan from sucrose, but it may also transfer the fructosyl moiety from sucrose to acceptor molecules included in the reaction medium
-
-
?
additional information
?
-
-
levansucrase catalyzes the synthesis of levan from sucrose, but it may also transfer the fructosyl moiety from sucrose to acceptor molecules. The wild-type enzyme synthesizes levan with molecular weight bimodal distribution, while the mutants R360K and Y429N synthesize only oligosaccharides, substrate specificities, overview
-
-
?
additional information
?
-
levan synthesis from sucrose, structure analysis by NMR spectrometry, overview. Levan size analysis by gel filtration. As sucrose concentration increases, the average molecular weight of the low dextran distribution decreases, at 4°C compared to 37°C, the low molecular weight distribution region increases in size at any given substrate concentration, and a maximum of 20.64 kDa is obtained at 200 g/l
-
-
?
additional information
?
-
-
levansucrase catalyzes three distinct reactions depending on the fructosyl acceptor molecule, including polymerization, transfructosylation, and hydrolysis. Wide substrate specificity of levansucrase toward monosaccharides, disaccharides, and aromatic and alkyl alcohols, producing diverse sucrose analogues, hetero-oligosaccharides (especially lactosucrose), and fructosides, overview
-
-
?
additional information
?
-
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
-
?
additional information
?
-
-
levansucrase catalyzes three distinct reactions depending on the fructosyl acceptor molecule: polymerization (using the growing fructan chain as an acceptor), transfructosylation (using monosaccharides, disaccharides, or oligosaccharides as acceptors), and hydrolysis (using water as an acceptor), overview
-
-
?
additional information
?
-
measurement of sucrose hydrolysis, releasing D-glucose and D-fructose. As the reaction proceeds, SacB becomes less hydrolytic while transferase becomes preponderant to reach up to 80% at the end of the reaction
-
-
?
additional information
?
-
levan synthesis from sucrose, structure analysis by NMR spectrometry, overview. Levan size analysis by gel filtration. As sucrose concentration increases, the average molecular weight of the low dextran distribution decreases, at 4°C compared to 37°C, the low molecular weight distribution region increases in size at any given substrate concentration, and a maximum of 20.64 kDa is obtained at 200 g/l
-
-
?
additional information
?
-
measurement of sucrose hydrolysis, releasing D-glucose and D-fructose. As the reaction proceeds, SacB becomes less hydrolytic while transferase becomes preponderant to reach up to 80% at the end of the reaction
-
-
?
additional information
?
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
-
?
additional information
?
-
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
-
?
additional information
?
-
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
-
?
additional information
?
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
in Lactobacillus sanfranciscensis TMW 1.392, sucrose metabolism and formation of fructan and 1-kestose is dependent on the activity of a single enzyme, levansucrase
-
-
?
additional information
?
-
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
-
?
additional information
?
-
in Lactobacillus sanfranciscensis TMW 1.392, sucrose metabolism and formation of fructan and 1-kestose is dependent on the activity of a single enzyme, levansucrase
-
-
?
additional information
?
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
-
?
additional information
?
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
the enzyme cannot hydrolyze levan from Halomonas smyrnensis, Zymomonas mobilis and Bacillus subtilis, and inulin from chicory
-
-
-
additional information
?
-
-
the enzyme cannot hydrolyze levan from Halomonas smyrnensis, Zymomonas mobilis and Bacillus subtilis, and inulin from chicory
-
-
-
additional information
?
-
the enzyme cannot hydrolyze levan from Halomonas smyrnensis, Zymomonas mobilis and Bacillus subtilis, and inulin from chicory
-
-
-
additional information
?
-
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
-
?
additional information
?
-
-
levan synthesis from sucrose
-
-
?
additional information
?
-
-
measurement of sucrose hydrolysis
-
-
?
additional information
?
-
-
levan synthesis from sucrose
-
-
?
additional information
?
-
-
measurement of sucrose hydrolysis
-
-
?
additional information
?
-
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
-
?
additional information
?
-
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
-
?
additional information
?
-
-
levansucrase catalyzes three distinct reactions depending on the fructosyl acceptor molecule, including polymerization, transfructosylation, and hydrolysis. Wide substrate specificity of levansucrase toward monosaccharides, disaccharides, and aromatic and alkyl alcohols, producing diverse sucrose analogues, hetero-oligosaccharides (especially lactosucrose), and fructosides, overview
-
-
?
additional information
?
-
-
levansucrase catalyzes three distinct reactions depending on the fructosyl acceptor molecule: polymerization (using the growing fructan chain as an acceptor), transfructosylation (using monosaccharides, disaccharides, or oligosaccharides as acceptors), and hydrolysis (using water as an acceptor), overview
-
-
?
additional information
?
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
-
levan, a polymer of fructose linked by fructofurano side bonds, is produced by the transfructosylation reaction of levansucrase
-
-
?
additional information
?
-
the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
-
-
-
additional information
?
-
the enzyme also shows hydrolytic activity with sucrose producing D-glucose and D-fructose
-
-
-
additional information
?
-
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
-
?
additional information
?
-
-
levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
-
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additional information
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levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions. The enzyme cleaves raffinose and stachyose
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additional information
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the product levan has not a major impact on biofilm formation
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additional information
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thermo-responsive expression and differential secretion of the enzyme. The extracellular levansucrase is encoded by two functional genes, lscB and lscC. Transcription of lscB and lscC is temperature-dependent. Quantification of Lsc in supernatants and cellular protein samples of mutants defective in either lscB or lscC confirm that LscB secretion at low temperature is due to a combination of thermo-regulated transcription and secretion. LscC accumulates in the periplasmic space
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additional information
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levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions. No activity with raffinose or stachyose
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additional information
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isozyme Lsc3 synthesizes a high molecular weight fructan polymer, levan, from sucrose, but it also shows formation of fructooligosaccharides with potential prebiotic effects from both sucrose and raffinose, degrees of polymerization up to five, overview. Formation of fructooligosaccharides is enhanced by increased sucrose or raffinose concentrations of 600 mM and higher. Analysis of product in underivatized form by fully automated chip-based nanoelectrospray ionization, nanoESI, high-capacity ion trap mass spectrometry, HCT-MS. Structural analysis by tandem mass spectrometry, MS/MS, employing collision-induced dissociation at low energies, overview
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additional information
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assay of the growth phenotype of levansucrase-expressing bacteria on agar plate containing sucrose. Only wild-type Lsc3 produces levan giving a mucoid phenotype to the streaks of respective transformant. Quantitative evaluation of the sucrose-splitting (total) levansucrase activity on microplates
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additional information
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assay of the growth phenotype of levansucrase-expressing bacteria on agar plate containing sucrose. Only wild-type Lsc3 produces levan giving a mucoid phenotype to the streaks of respective transformant. Quantitative evaluation of the sucrose-splitting (total) levansucrase activity on microplates
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additional information
?
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levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions. The enzyme cleaves raffinose and stachyose
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?
additional information
?
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levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions. The enzyme cleaves raffinose and stachyose
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?
additional information
?
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levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions. The enzyme cleaves raffinose and stachyose
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?
additional information
?
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levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions. The enzyme cleaves raffinose and stachyose
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?
additional information
?
-
isozyme Lsc3 synthesizes a high molecular weight fructan polymer, levan, from sucrose, but it also shows formation of fructooligosaccharides with potential prebiotic effects from both sucrose and raffinose, degrees of polymerization up to five, overview. Formation of fructooligosaccharides is enhanced by increased sucrose or raffinose concentrations of 600 mM and higher. Analysis of product in underivatized form by fully automated chip-based nanoelectrospray ionization, nanoESI, high-capacity ion trap mass spectrometry, HCT-MS. Structural analysis by tandem mass spectrometry, MS/MS, employing collision-induced dissociation at low energies, overview
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additional information
?
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assay of the growth phenotype of levansucrase-expressing bacteria on agar plate containing sucrose. Only wild-type Lsc3 produces levan giving a mucoid phenotype to the streaks of respective transformant. Quantitative evaluation of the sucrose-splitting (total) levansucrase activity on microplates
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additional information
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the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
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additional information
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the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
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additional information
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the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
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additional information
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Q60114
production of low molecular weight levan in permeabilized recombinant E. coli cells
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additional information
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6-beta-D-fructosyl)n is levan
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additional information
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Q60114
change in substrate specificity appears to be unique to Zymomonas mobilis levansucrase because the levansucrases from Bacillus subtilis, Rahnella aquatilis, and Lactobacillus reuteri are capable of synthesizing levan in their soluble form and are not reported to form fibril-like structures
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additional information
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change in substrate specificity appears to be unique to Zymomonas mobilis levansucrase because the levansucrases from Bacillus subtilis, Rahnella aquatilis, and Lactobacillus reuteri are capable of synthesizing levan in their soluble form and are not reported to form fibril-like structures
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additional information
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levan biosynthesis and fructooligosaccharide biosynthesis
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additional information
?
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levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
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additional information
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three activities are displayed by the levansucrase from Zymomonas mobilis: formation of levan (polymerization), production of short-chain fructooligosaccharides (FOS), and sucrose hydrolysis. Several inulin-type FOS (1-kestose, nystose, 1F-fructosylnystose), neo-FOS (blastose, neokestose, neonystose) and levan-type FOS (6-kestose, 6,6-nystose) are synthesized by levansucrase, identification by mass spectroscopy and NMR spectrometry, e.g. of 6,6-nystose (i.e. Fru-beta(2->6)-Fru-beta(2->6)-Fru-beta(2->1)-alphaGlc). Assay method optimization, transfructosylation to hydrolysis ratio. , overview
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additional information
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levan biosynthesis and fructooligosaccharide biosynthesis
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 sucrose
D-glucose + beta-D-fructofuranosyl-(2,6)-beta-D-fructofuranosyl-(2,1)-alpha-D-glucopyranoside
sucrose + (2,6-beta-D-fructosyl)n
alpha-D-glucose + (2,6-beta-D-fructosyl)n+1
sucrose + (2,6-beta-D-fructosyl)n
D-glucose + (2,6-beta-D-fructosyl)n+1
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n+1
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
sucrose + lactose
D-glucose + O-beta-D-galactopyranosyl-(1,4)-O-beta-D-glucopyranosyl-(1,2)-beta-D-fructofuranoside
-
levansucrase transfers the fructosyl moiety of sucrose to lactose to form lactosucrose
i.e. lactosucrose or 4G-beta-D-galactosylsucrose
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?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
additional information
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2 sucrose
D-glucose + beta-D-fructofuranosyl-(2,6)-beta-D-fructofuranosyl-(2,1)-alpha-D-glucopyranoside
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2 sucrose
D-glucose + beta-D-fructofuranosyl-(2,6)-beta-D-fructofuranosyl-(2,1)-alpha-D-glucopyranoside
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-
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?
sucrose + (2,6-beta-D-fructosyl)n
alpha-D-glucose + (2,6-beta-D-fructosyl)n+1
-
capacity to produce extracellular homopolysaccharides of fructose, modulation of the composition of the biofilms that form on teeth
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sucrose + (2,6-beta-D-fructosyl)n
alpha-D-glucose + (2,6-beta-D-fructosyl)n+1
-
capacity to produce extracellular homopolysaccharides of fructose, modulation of the composition of the biofilms that form on teeth
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sucrose + (2,6-beta-D-fructosyl)n
D-glucose + (2,6-beta-D-fructosyl)n+1
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?
sucrose + (2,6-beta-D-fructosyl)n
D-glucose + (2,6-beta-D-fructosyl)n+1
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?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
enzyme is probably involved in initiation and progression of dental caries and periodontal diseases
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?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
enzyme is probably involved in initiation and progression of dental caries and periodontal diseases
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sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
Aerobacter levanicum
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levan biosynthesis
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?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
activity is affected by sacU mutation
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sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
activity is affected by sacU mutation
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?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
activity is affected by sacU mutation
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?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
synthesis of a high-molecular-mass fructan of the levan type
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?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
translocation of the enzyme is a rate-limiting step
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?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
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?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
transgenic plants
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sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
transgenic plants
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sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
biosynthesis of fructans, important in assimilate partitioning and possibly in stress tolerance in plants
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?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
-
key enzyme for the formation of the graminans and phleins
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?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
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-
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?
sucrose + (2,6-beta-D-fructosyl)n
glucose + (2,6-beta-D-fructosyl)n+1
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?
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n+1
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?
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n+1
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-
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?
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n+1
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-
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?
sucrose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n
D-glucose + alpha-D-glucosyl-(1->2)-[(2->6)-alpha-D-fructosyl]n+1
-
-
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?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
-
-
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?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
-
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?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
-
-
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?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
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?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
-
-
?
additional information
?
-
Aerobacter levanicum
-
6-beta-D-fructosyl)n is levan
-
-
?
additional information
?
-
-
levansucrase catalyzes three distinct reactions depending on the fructosyl acceptor molecule, including polymerization, transfructosylation, and hydrolysis. Wide substrate specificity of levansucrase toward monosaccharides, disaccharides, and aromatic and alkyl alcohols, producing diverse sucrose analogues, hetero-oligosaccharides (especially lactosucrose), and fructosides, overview
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-
?
additional information
?
-
-
levansucrase catalyzes the synthesis of levan from sucrose, but it may also transfer the fructosyl moiety from sucrose to acceptor molecules included in the reaction medium
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?
additional information
?
-
levan synthesis from sucrose, structure analysis by NMR spectrometry, overview. Levan size analysis by gel filtration. As sucrose concentration increases, the average molecular weight of the low dextran distribution decreases, at 4°C compared to 37°C, the low molecular weight distribution region increases in size at any given substrate concentration, and a maximum of 20.64 kDa is obtained at 200 g/l
-
-
?
additional information
?
-
-
levansucrase catalyzes three distinct reactions depending on the fructosyl acceptor molecule, including polymerization, transfructosylation, and hydrolysis. Wide substrate specificity of levansucrase toward monosaccharides, disaccharides, and aromatic and alkyl alcohols, producing diverse sucrose analogues, hetero-oligosaccharides (especially lactosucrose), and fructosides, overview
-
-
?
additional information
?
-
levan synthesis from sucrose, structure analysis by NMR spectrometry, overview. Levan size analysis by gel filtration. As sucrose concentration increases, the average molecular weight of the low dextran distribution decreases, at 4°C compared to 37°C, the low molecular weight distribution region increases in size at any given substrate concentration, and a maximum of 20.64 kDa is obtained at 200 g/l
-
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?
additional information
?
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in Lactobacillus sanfranciscensis TMW 1.392, sucrose metabolism and formation of fructan and 1-kestose is dependent on the activity of a single enzyme, levansucrase
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additional information
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in Lactobacillus sanfranciscensis TMW 1.392, sucrose metabolism and formation of fructan and 1-kestose is dependent on the activity of a single enzyme, levansucrase
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additional information
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levan synthesis from sucrose
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additional information
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levan synthesis from sucrose
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additional information
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levansucrase catalyzes three distinct reactions depending on the fructosyl acceptor molecule, including polymerization, transfructosylation, and hydrolysis. Wide substrate specificity of levansucrase toward monosaccharides, disaccharides, and aromatic and alkyl alcohols, producing diverse sucrose analogues, hetero-oligosaccharides (especially lactosucrose), and fructosides, overview
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additional information
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levan, a polymer of fructose linked by fructofurano side bonds, is produced by the transfructosylation reaction of levansucrase
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additional information
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the product levan has not a major impact on biofilm formation
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additional information
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thermo-responsive expression and differential secretion of the enzyme. The extracellular levansucrase is encoded by two functional genes, lscB and lscC. Transcription of lscB and lscC is temperature-dependent. Quantification of Lsc in supernatants and cellular protein samples of mutants defective in either lscB or lscC confirm that LscB secretion at low temperature is due to a combination of thermo-regulated transcription and secretion. LscC accumulates in the periplasmic space
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additional information
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isozyme Lsc3 synthesizes a high molecular weight fructan polymer, levan, from sucrose, but it also shows formation of fructooligosaccharides with potential prebiotic effects from both sucrose and raffinose, degrees of polymerization up to five, overview. Formation of fructooligosaccharides is enhanced by increased sucrose or raffinose concentrations of 600 mM and higher. Analysis of product in underivatized form by fully automated chip-based nanoelectrospray ionization, nanoESI, high-capacity ion trap mass spectrometry, HCT-MS. Structural analysis by tandem mass spectrometry, MS/MS, employing collision-induced dissociation at low energies, overview
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additional information
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isozyme Lsc3 synthesizes a high molecular weight fructan polymer, levan, from sucrose, but it also shows formation of fructooligosaccharides with potential prebiotic effects from both sucrose and raffinose, degrees of polymerization up to five, overview. Formation of fructooligosaccharides is enhanced by increased sucrose or raffinose concentrations of 600 mM and higher. Analysis of product in underivatized form by fully automated chip-based nanoelectrospray ionization, nanoESI, high-capacity ion trap mass spectrometry, HCT-MS. Structural analysis by tandem mass spectrometry, MS/MS, employing collision-induced dissociation at low energies, overview
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additional information
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Q60114
production of low molecular weight levan in permeabilized recombinant E. coli cells
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additional information
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6-beta-D-fructosyl)n is levan
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additional information
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levan biosynthesis and fructooligosaccharide biosynthesis
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additional information
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levan biosynthesis and fructooligosaccharide biosynthesis
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K372A
-
the mutant shows reduced activity compared to the wild type enzyme
K372Y
-
the mutant shows reduced activity compared to the wild type enzyme
N251W
-
the mutant shows reduced activity compared to the wild type enzyme
N251W/E349W/K372Y
-
inactive
N251W/K372Y
-
the mutant shows reduced activity compared to the wild type enzyme
K372A
-
the mutant shows reduced activity compared to the wild type enzyme
-
K372Y
-
the mutant shows reduced activity compared to the wild type enzyme
-
N251W
-
the mutant shows reduced activity compared to the wild type enzyme
-
A344P
site directed mutagenesis, same behavior like the wild-type
F414W
site directed mutagenesis, same behavior like the wild-type
G361F
site-directed mutagenesis, less stable than the wild-type, synthesizes mainly oligosaccharides, still catalyzes the synthesis of low amounts of polymer, pH-optimum 6, affinity for sucrose is reduced, shift of reaction specificity (hydrolysis/transfer)
H331R
-
invers directed mutation of natural point mutation R331H to H331R restores the wild-type enzyme properties
N242H
the mutant shows 31fold decrease in catalytic efficiency compared to the wild type enzyme
R331H
-
natural point mutation, low polymerase activity, invers mutation H331R restores the wild-type enzyme properties
R360H
the mutant shows 5fold decrease in catalytic efficiency compared to the wild type enzyme. The mutant still can produce levan, but has 60% less transfructosylation activity
R433A
site-directed mutagenesis, synthesizes only oligosaccharides, pH-optimum 6-7, affinity for sucrose is reduced, shift of reaction specificity (hydrolysis/transfer)
Y429
site-directed mutagenesis, Y429 plays an indirect but important role in catalysis and acceptor specificity, as this is a key residue coordinating the sucrose position in the levansucrase binding pocket through a complex water network
Y429A
site-directed mutagenesis
H243L
-
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
-
S164A
-
the mutant shows 8fold decrease in catalytic efficiency compared to the wild type enzyme
-
A154S
-
the mutant shows reduced activity compared to the wild type enzyme
E404A
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404C
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404D
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404F
the mutant exhibits an enhanced thermostability and the melting temperature of the mutant is enhanced by 1.5°C compared to the wild type enzyme
E404G
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404H
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404I
the mutant exhibits an enhanced thermostability and and the melting temperature of the mutant is enhanced by 1.5°C compared to the wild type enzyme
E404K
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404L
the melting temperature of the mutant is enhanced by 2.8°C and the half-life is increased by 12.5 and 1.3fold at 35 and 45°C, respectively, as compared to the wild type enzyme
E404M
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404N
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404P
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404Q
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404R
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404S
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404T
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404V
the mutant exhibits an enhanced thermostability and the melting temperature of the mutant is enhanced by 1.4°C compared to the wild type enzyme
E404W
the mutant exhibits an enhanced thermostability and and the melting temperature of the mutant is enhanced by 1.6°C compared to the wild type enzyme
E404Y
the mutant exhibits a decreased thermostability compared to the wild type enzyme
H327A
-
the mutant shows reduced activity compared to the wild type enzyme
H327R
-
the mutant shows reduced activity compared to the wild type enzyme
C339S
kcat/Km for hydrolysis of sucrose is 68.75fold lower than wild-type value
C395S
kcat/Km for hydrolysis of sucrose is 60fold lower than wild-type value
D135N
kcat/Km for hydrolysis of sucrose is 1257fold lower than wild-type value
D309N
site-directed mutagenesis of RDP-motif, no affection of enzyme secretion but hydrolysis activity, 13fold increase of kcat, 71fold decrease of kcat/Km, unaltered Km for sucrose
C339S
-
kcat/Km for hydrolysis of sucrose is 68.75fold lower than wild-type value
-
C395S
-
kcat/Km for hydrolysis of sucrose is 60fold lower than wild-type value
-
D135N
-
kcat/Km for hydrolysis of sucrose is 1257fold lower than wild-type value
-
K373A
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
K373R
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
N252D
the mutant shows wild type activity
N252G
the mutant shows wild type activity
N252H
the mutant shows 8fold decrease in catalytic efficiency compared to the wild type enzyme
S173G
the mutant shows 59fold decrease in catalytic efficiency compared to the wild type enzyme
S173T
the mutant shows 7fold decrease in catalytic efficiency compared to the wild type enzyme
S422A
the mutant shows 4fold decrease in catalytic efficiency compared to the wild type enzyme
Y247A
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
Y247I
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
Y247W
the mutant shows 0.2fold decrease in catalytic efficiency compared to the wild type enzyme
Y421F
the mutant shows 33fold decrease in catalytic efficiency compared to the wild type enzyme
Y421M
the mutant shows 302fold decrease in catalytic efficiency compared to the wild type enzyme
Y421W
the mutant shows 101fold decrease in catalytic efficiency compared to the wild type enzyme
Y439A
the mutant shows 2130fold decrease in catalytic efficiency compared to the wild type enzyme
Y439F
the mutant shows 9fold decrease in catalytic efficiency compared to the wild type enzyme
Y439M
the mutant shows 131fold decrease in catalytic efficiency compared to the wild type enzyme
Y439W
the mutant shows 41fold decrease in catalytic efficiency compared to the wild type enzyme
L118A
-
site-directed mutagenesis
-
R256A
-
nearly inactive
-
D300A
-
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
D300N
-
the mutant shows 4fold decrease in catalytic efficiency compared to the wild type enzyme
D333A
-
the mutant shows 6fold decrease in catalytic efficiency compared to the wild type enzyme
D333N
-
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
E146Q
-
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
E236Q
-
the mutant shows 42fold decrease in catalytic efficiency compared to the wild type enzyme
H321K
-
the mutant shows 75fold decrease in catalytic efficiency compared to the wild type enzyme
H321L
-
the mutant shows 61fold decrease in catalytic efficiency compared to the wild type enzyme
H321R
-
the mutant shows 82fold decrease in catalytic efficiency compared to the wild type enzyme
H321S
-
the mutant shows 234fold decrease in catalytic efficiency compared to the wild type enzyme
Q301A
-
the mutant shows 55fold decrease in catalytic efficiency compared to the wild type enzyme
Q301E
-
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
T302M
-
the mutant shows wild type activity
T302P
-
the mutant shows 3fold decrease in catalytic efficiency compared to the wild type enzyme
W61A
-
the mutant shows 137fold decrease in catalytic efficiency compared to the wild type enzyme
W61N
-
the mutant shows 3708fold decrease in catalytic efficiency compared to the wild type enzyme
D31N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E110D
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
E146Q
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
E211Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
V248A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W109F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W109R
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W63A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W80R
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D219A
-
site-directed mutagenesis, inactive mutant
-
E211Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
H113A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
P220A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
D275N
-
site-directed mutagenesis, enhanced kcat and Km for sucrose, activity with sucrose similar to wild-type, reduced activity with raffinose and stachyose
D302N
-
site-directed mutagenesis, enhanced kcat and Km for sucrose, activity with sucrose similar to wild-type, reduced activity with raffinose and stachyose
E278H
-
site-directed mutagenesis, 210fold reduced kcat and enhanced Km for sucrose, reduced activity with sucrose and reduced activity with raffinose
H296C
-
site-directed mutagenesis, no detectable activities
H296E
-
site-directed mutagenesis, no detectable activities
H296Q
-
site-directed mutagenesis, minimal hydrolysis and transfructosylation activities, transfructosylation activity is reduced to 2.5% of the wild-type
H296Y
-
site-directed mutagenesis, no detectable activities
Q339H/P340A
-
random mutagenesis, reduced activity with stachyose, slightly enhanced kcat and enhanced Km for sucrose, slightly reduced activity with sucrose
R193H
-
the mutant shows 298fold decrease in catalytic efficiency compared to the wild type enzyme
R193K
-
the mutant shows 521fold decrease in catalytic efficiency compared to the wild type enzyme
V223A
-
random mutagenesis, reduced kcat, highly enhanced Km, and reduced activity with sucrose, enhanced activity with raffinose and 3.8fold with stachyose
W118H
-
the mutant shows 521fold decrease in catalytic efficiency compared to the wild type enzyme
W118N
-
the mutant shows 521fold decrease in catalytic efficiency compared to the wild type enzyme
W47H
-
the mutant shows 695fold decrease in catalytic efficiency compared to the wild type enzyme
W47N
-
the mutant shows 72fold decrease in catalytic efficiency compared to the wild type enzyme
W80R
-
random mutagenesis, reduced kcat for sucrose, enhanced Km, reduced activity with sucrose, slightly reduced activity with raffinose
T14V
-
levanase-deficient mutant
T14V
-
levanase-deficient mutant
-
Y237S
the mutant efficiently produces a higher amount of short-chain levan-typed fructooligosaccharide than wild type with increased prebiotic activity
Y237S
-
the mutant efficiently produces a higher amount of short-chain levan-typed fructooligosaccharide than wild type with increased prebiotic activity
-
D247A
inactive
D247A
single site mutant, substitutions have little effect on the active site geometry, catalytically inactive
D86A
inactive
D86A
single site mutant, substitutions have little effect on the active site geometry, catalytically inactive
E342A
inactive
E342A
single site mutant, catalytically inactive, the E342A mutant reveals conformational flexibility of functionally relevant side chains in the vicinity of the general acid Glu342, including Arg360, a residue required for levan polymerisation
H243L
site-directed mutagenesis, less stable than the wild-type, pH-optimum 6, shift of reaction specificity (hydrolysis/transfer)
H243L
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
I341V
site-directed mutagenesis, pH-optimum 6
I341V
the mutant shows wild type catalytic efficiency
R331K
-
site-directed mutagenesis, loss of ability to perform the whole production of levan from sucrose, only capable to perform the first reaction step, the formation of the trisaccharide kestose, higher kcat than the wild-type for sucrose hydrolysis
R331K
mutant enzyme loses the ability to synthesize levan and is only able to produce the trisaccharide kestose
R331L
-
site-directed mutagenesis, loss of ability to perform the whole production of levan from sucrose, only capable to perform the first reaction step, the formation of the trisaccharide kestose, reduced fructosyl-enzyme intermediate formation
R331L
mutant enzyme loses the ability to synthesize levan and is only able to produce the trisaccharide kestose
R331S
-
site-directed mutagenesis, loss of ability to perform the whole production of levan from sucrose, only capable to perform the first reaction step, the formation of the trisaccharide kestose, reduced fructosyl-enzyme intermediate formation
R331S
mutant enzyme loses the ability to synthesize levan and is only able to produce the trisaccharide kestose
R360K
site-directed mutagenesis, pH-optimum 6, affinity for sucrose is reduced, shift of reaction specificity (hydrolysis/transfer)
R360K
-
the immobilized mutant enzyme shows increased activity and is improved for fructosyl-xyloside synthesis compared to the wild-type enzyme
R360K
the mutant shows 1-4fold decrease in catalytic efficiency compared to the wild type enzyme
R360S
site-directed mutagenesis, pH-optimum 6, decrease in activity, affinity for sucrose is reduced, shift of reaction specificity (hydrolysis/transfer)
R360S
the mutant shows 98-226fold decrease in catalytic efficiency compared to the wild type enzyme
S164A
site-directed mutagenesis, S164A is catalytically important, as it maintains the nucleophile in an appropriate position regarding the sucrose molecule. S164A results in a 12fold more stable and less hydrolytic enzyme than the wild-type, with a half-life of 628.0 (+51.0) min, pH-optimum 6, decrease in activity, slightly higher affinity for sucrose
S164A
the mutant shows 8fold decrease in catalytic efficiency compared to the wild type enzyme
Y429N
site-directed mutagenesis, synthesizes only oligosaccharides, pH-optimum 5-6, decrease in activity, affinity for sucrose is reduced, shift of reaction specificity (hydrolysis/transfer)
Y429N
-
the immobilized mutant enzyme shows increased activity and is improved for fructosyl-xyloside synthesis compared to the wild-type enzyme
Y429N
the mutant shows 1015fold decrease in catalytic efficiency compared to the wild type enzyme
D500A
at 45°C the mutant enzyme is inactive in absence of Ca2+, 45% of wild-type activity remains in presence of 1 mM Ca2+
D500A
at 45°C the mutant enzyme is inactive in the absence of Ca2+ ions, with 15% of wild-type activity remaining in the presence of 1 mM Ca2+. In the presence of 1 mM Ca2+ mutant enzyme displays highest activity at 40°C. In the absence of Ca2+ ions, the optimal temperature is 30°C
D500N
at 45°C the mutant enzyme is inactive in absence of Ca2+, 45% of wild-type activity remains in presence of 1 mM Ca2+
D500N
at 45°C the mutant enzyme is inactive in the absence of Ca2+ ions, with 45% of wild-type activity remaining in the presence of 1 mM Ca2+. In the presence of 1 mM Ca2+ mutant enzyme displays highest activity at 40°C. In the absence of Ca2+ ions, the optimal temperature is 30°C
D500A
-
at 45°C the mutant enzyme is inactive in absence of Ca2+, 45% of wild-type activity remains in presence of 1 mM Ca2+
-
D500A
-
at 45°C the mutant enzyme is inactive in the absence of Ca2+ ions, with 15% of wild-type activity remaining in the presence of 1 mM Ca2+. In the presence of 1 mM Ca2+ mutant enzyme displays highest activity at 40°C. In the absence of Ca2+ ions, the optimal temperature is 30°C
-
D500N
-
at 45°C the mutant enzyme is inactive in absence of Ca2+, 45% of wild-type activity remains in presence of 1 mM Ca2+
-
D500N
-
at 45°C the mutant enzyme is inactive in the absence of Ca2+ ions, with 45% of wild-type activity remaining in the presence of 1 mM Ca2+. In the presence of 1 mM Ca2+ mutant enzyme displays highest activity at 40°C. In the absence of Ca2+ ions, the optimal temperature is 30°C
-
D257A
inactive
D257A
-
site-directed mutagenesis, no activity
D257A
-
mutant shows almost no activity
D95A
inactive
D95A
-
site-directed mutagenesis, no activity
E350A
-
mutant is nearly inactive
E350A
-
site-directed mutagenesis, nearly inactive
E352A
inactive
E352A
-
site-directed mutagenesis, no measureable activity
L118A
-
site-directed mutagenesis
L118A
-
kcat/Km is 5.5% of wild-type value
N252A
-
site-directed mutagenesis
N252A
-
kcat/Km is 104% of wild-type value
N252A
the mutant shows wild type activity
R256A
-
mutant is nearly inactive
R256A
-
site-directed mutagenesis, nearly inactive
R370A
-
site-directed mutagenesis, after a reaction time of 60 min an accumulation of neokestose (2,6-beta-Fru-betaGlc-1,2-beta-Fru, 32.7 mM) is determined, whereas after 19 h, blastose (2,6-beta-Fru-alpha,betaGlc) is the main reaction product (69.7 mM)
R370A
the mutant shows 57fold decrease in catalytic efficiency compared to the wild type enzyme
S173A
-
site-directed mutagenesis
S173A
-
kcat/Km is 46% of wild-type value
S173A
the mutant shows 19fold decrease in catalytic efficiency compared to the wild type enzyme
W172A
-
kcat/Km is 1.4% of wild-type value
W172A
-
site-directed mutagenesis, 72fold increase of the KM of the wild-type
W172A
the mutant shows 69fold decrease in catalytic efficiency compared to the wild type enzyme
W94A
-
kcat/Km is 9% of wild-type value
W94A
-
site-directed mutagenesis, 9% of the catalytic efficiency of the wild-type
W94A
the mutant shows 11fold decrease in catalytic efficiency compared to the wild type enzyme
Y421A
-
kcat/Km is 1.9% of wild-type value
Y421A
-
site-directed mutagenesis, 3%of the wild-type activity
Y421A
the mutant shows 520fold decrease in catalytic efficiency compared to the wild type enzyme
E350A
-
mutant is nearly inactive
-
E350A
-
site-directed mutagenesis, nearly inactive
-
E350A
-
nearly inactive
-
W172A
-
kcat/Km is 1.4% of wild-type value
-
W172A
-
site-directed mutagenesis, 72fold increase of the KM of the wild-type
-
W172A
-
the mutant shows 69fold decrease in catalytic efficiency compared to the wild type enzyme
-
D219A
site-directed mutagenesis, inactive mutant
D219A
site-directed mutagenesis, inactive mutant
D225A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D225A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D225N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D225N
site-directed mutagenesis, the mutant shows enhanced activity compared to the wild-type enzyme
D300A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D300A
site-directed mutagenesis, the mutant shows slightly enhanced activity compared to the wild-type enzyme
D333A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D333A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D333N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D333N
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
D62A
site-directed mutagenesis, inactive mutant
D62A
site-directed mutagenesis, inactive mutant
E236Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E236Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E303A
site-directed mutagenesis, inactive mutant
E303A
site-directed mutagenesis, inactive mutant
E303Q
site-directed mutagenesis, inactive mutant
E303Q
site-directed mutagenesis, inactive mutant
H113A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H113A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H113Q
site-directed mutagenesis, inactive mutant
H113Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H306A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H306A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H321K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H321K
site-directed mutagenesis, almost inactive mutant
H321L
site-directed mutagenesis, almost inactive mutant
H321L
site-directed mutagenesis, almost inactive mutant
H321R
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H321R
site-directed mutagenesis, almost inactive mutant
H321R
site-directed mutagenesis, significantly decreased polymerizing ability compared to the wild-type
H321S
site-directed mutagenesis, almost inactive mutant
H321S
site-directed mutagenesis, almost inactive mutant
L66A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L66A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
P220A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
P220A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q301A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Q301A
site-directed mutagenesis, significantly decreased polymerizing ability compared to the wild-type
Q301E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q301E
site-directed mutagenesis, the mutant shows slightly enhanced activity compared to the wild-type enzyme
R304A
site-directed mutagenesis, inactive mutant
R304A
site-directed mutagenesis, almost inactive mutant
R304C
site-directed mutagenesis, inactive mutant
R304C
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
T302M
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
T302M
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
T302P
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T302P
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T302P
site-directed mutagenesis, significantly decreased polymerizing ability compared to the wild-type
W109A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W109A
site-directed mutagenesis, almost inactive mutant
W61A
site-directed mutagenesis, inactive mutant
W61A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W61N
site-directed mutagenesis, inactive mutant
W61N
site-directed mutagenesis, almost inactive mutant
D333N
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
D333N
-
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
-
H113Q
-
site-directed mutagenesis, inactive mutant
-
H113Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
D194N
-
site-directed mutagenesis, 3400fold decreased kcat and 3fold increased Km for sucrose, activity with sucrose similar to wild-type, reduced activity with raffinose and stachyose
D194N
-
the mutant shows 8300fold decrease in catalytic efficiency compared to the wild type enzyme
D308N
-
site-directed mutagenesis, enhanced kcat and Km for sucrose, activity with sucrose similar to wild-type, reduced activity with raffinose and stachyose
D308N
-
the mutant shows 3fold decrease in catalytic efficiency compared to the wild type enzyme
E117Q
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site-directed mutagenesis, slightly reduced kcat and enhanced Km for sucrose, slightly enhanced activity with sucrose, reduced activity with raffinose and stachyose
E117Q
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the mutant shows 5fold decrease in catalytic efficiency compared to the wild type enzyme
E211Q
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site-directed mutagenesis, highly reduced kcat and enhanced Km for sucrose, highly reduced activity with sucrose, reduced activity with raffinose, increased activity with stachyose
E211Q
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the mutant shows 22fold decrease in catalytic efficiency compared to the wild type enzyme
E278D
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random mutagenesis, 30fold reduced kcat and reduced Km for sucrose, slightly enhanced activity with sucrose, reduced activity with raffinose
E278D
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transfructosylation activity of the variant decreases 15% at 15°C as compared to the wild type enzyme
E278D
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transfructosylation activity of the variant increases 18% at 15°C as compared to the wild type enzyme
H296K
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site-directed mutagenesis, reduced kcat and highly increased Km for sucrose, unaltered activity with sucrose, increased activity with raffinose, highly increased activity with stachyose
H296K
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site-directed mutagenesis, minimal hydrolysis and transfructosylation activities, transfructosylation activity is reduced to 4.6% of the wild-type
H296K
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the mutant shows 29fold decrease in catalytic efficiency compared to the wild type enzyme
H296L
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site-directed mutagenesis, reduced kcat and highly increased Km for sucrose, unaltered activity with sucrose, increased activity with raffinose, highly increased activity with stachyose
H296L
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site-directed mutagenesis, minimal hydrolysis and transfructosylation activities, transfructosylation activity is reduced to 1.0% of the wild-type, mediates the accumulation of low amounts of trisaccharide, but did not produce pentasaccharide
H296L
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the mutant shows 41fold decrease in catalytic efficiency compared to the wild type enzyme
H296R
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site-directed mutagenesis, reduced kcat and highly increased Km for sucrose, unaltered activity with sucrose, increased activity with raffinose, highly increased activity with stachyose
H296R
Q60114
no ability of the enzyme to form microfibrils and to synthesize levan at pH 6.0
H296R
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site-directed mutagenesis, retains partial hydrolysis and transfructosylation activities, transfructosylation activity is reduced to 23.1% of the wild-type
H296R
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the mutant shows 23fold decrease in catalytic efficiency compared to the wild type enzyme
H296S
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site-directed mutagenesis, reduced kcat and highly increased Km for sucrose, unaltered activity with sucrose, increased activity with raffinose, highly increased activity with stachyose
H296S
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site-directed mutagenesis, no detectable activities
H296S
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the mutant shows 77fold decrease in catalytic efficiency compared to the wild type enzyme
H296W
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site-directed mutagenesis, retains partial hydrolysis and transfructosylation activities, transfructosylation activity is reduced to 19.8% of the wild-type
H296W
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the mutant shows 14fold decrease in catalytic efficiency compared to the wild type enzyme
additional information
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allelic mutagenesis of wild-type strain, inactivation of ftf gene, no remaining levansucrase activity in the mutated strain
additional information
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allelic mutagenesis of wild-type strain, inactivation of ftf gene, no remaining levansucrase activity in the mutated strain
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additional information
design and evaluation of a bi-enzymatic system: combined use of levansucrase from Bacillus amyloliquefaciens and endoinulinase from Aspergillus niger in a one-step reaction for the synthesis of fructooligosaccharides (FOSs) and oligolevans using sucrose as the sole substrate, overview
additional information
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design and evaluation of a bi-enzymatic system: combined use of levansucrase from Bacillus amyloliquefaciens and endoinulinase from Aspergillus niger in a one-step reaction for the synthesis of fructooligosaccharides (FOSs) and oligolevans using sucrose as the sole substrate, overview
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additional information
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covalent immobilization of recombinant purified wild-type and mutant enzymes by glutaraldehyde to give cross-linked enzyme aggregates, CLEAs. Usage of 60% ammonium sulfate, 0.2% glutaraldehyde and 4 mg protein/ml. All CLEAs show higher thermal stability than corresponding soluble enzymes, but in the long term, the operational stability is affected by levan synthesis
additional information
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partially purified enzyme immobilization on Ca-alginate beads, or entrapment in agar and agarose, or crosslinking on chitosan by glutaraldehyde, activity of the immobilized enzyme is relatively lower than the activity of the free enzyme. The immobilized levansucrase shows a slight increase in activity compared with the free enzyme above 35°C. The activation energies are 6.62 and 9.27 kcal/mol for free and immobilized enzyme, respectively. The immobilized enzyme shows an increased thermal stability and reduced deactivation energy, as well as increased pH stability at acidic pH
additional information
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partially purified enzyme immobilization on Ca-alginate beads, or entrapment in agar and agarose, or crosslinking on chitosan by glutaraldehyde, activity of the immobilized enzyme is relatively lower than the activity of the free enzyme. The immobilized levansucrase shows a slight increase in activity compared with the free enzyme above 35°C. The activation energies are 6.62 and 9.27 kcal/mol for free and immobilized enzyme, respectively. The immobilized enzyme shows an increased thermal stability and reduced deactivation energy, as well as increased pH stability at acidic pH
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additional information
deletion mutant, Lactobacillus sanfranciscensis TMW 1392DELTAlev, loses the ability to hydrolyze sucrose, and does not produce fructan or 1-kestose
additional information
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deletion mutant, Lactobacillus sanfranciscensis TMW 1392DELTAlev, loses the ability to hydrolyze sucrose, and does not produce fructan or 1-kestose
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additional information
construction of mutants AD6, AD8, and AD9, that are unable to secrete LsdA due to nptII insertions in the type II secretion, gsp, operon. None of the mutants released extracellular LsdB, the exolavanase organized in one operon with the levansucrase LsdA
additional information
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construction of mutants AD6, AD8, and AD9, that are unable to secrete LsdA due to nptII insertions in the type II secretion, gsp, operon. None of the mutants released extracellular LsdB, the exolavanase organized in one operon with the levansucrase LsdA
additional information
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enzyme functionally expressed in Pichia pastoris and secreted into the medium shows additional sucrose-sucrose 1-fructosyltransferase activity, methanol induction
additional information
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construction of transgenic Nicotiana tabacum and Cichorium intybus plants expressing the 6-SFT gene via Agrobacterium tumefaciens infection, levansucrase activity in leaf and root extracts, levan analysis
additional information
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construction of transgenic Nicotiana plumbaginifolia plants that transiently express the functional levansucrase
additional information
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enzyme immobilization on wool, leading to higher optimal reaction temperature, low activation energy, higher Km and lower Vmax, compared to the free enzyme, with thermal stability and resistance to chemical denaturation, overview. The immobilized enzyme shows 78.12% of the free enzyme's specific activity
additional information
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formation of enzyme-polysaccharide conjugates at 4°C, variations of activity retained of the glycosylated levansucrase are affected by the carbohydrate residue, which is covalently linked to the enzyme molecule, dextran conjugates show highest, pectin conjugates lowest activity. In general, the glycosylated enzyme retains 25-57% of the original specific activity of the free enzyme
additional information
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immobilization of whole cells on Ca-alginate, and on different carriers loaf, stone, wool, ceramic by 0.1% glutaraldehyde, enzyme production in continuous fermentation at 30°C and pH 5.3, enzyme production and activities, and reaction parameters, overview
additional information
Vmax values for sucrose splitting of mutants, structure-function analysis of enzyme mutants, overview
additional information
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Vmax values for sucrose splitting of mutants, structure-function analysis of enzyme mutants, overview
additional information
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Vmax values for sucrose splitting of mutants, structure-function analysis of enzyme mutants, overview
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additional information
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The His296 mutation influences the substrate recognizing and binding, and then has an effect on sucrose hydrolysis and fructosyl-enzyme intermediate formation. Its mutations weakens the transfructosylation reaction and changes product specificities
additional information
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enhanced levan production using chitin-binding domain fused levansucrase immobilized on chitin beads
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