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4-nitrophenyl alpha-D-glucoside
?
isomaltotriose
?
wild-type AZOG
-
-
?
methyl alpha-D-glucoside
?
wild-type AZOG
-
-
?
saccharose
isomaltulose
-
-
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
sucrose
alpha-D-glucopyranosyl-1,1-D-fructofuranose
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
sucrose
alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
?
sucrose
isomaltulose + trehalulose
sucrose
isomaltulose + trehalulose + D-glucose
sucrose
palatinose
-
-
-
-
?
sucrose
palatinose + trehalulose + D-glucose + D-fructose
additional information
?
-
4-nitrophenyl alpha-D-glucoside
?
wild-type AZOG and enzyme chimeric mutant AZF3
-
-
?
4-nitrophenyl alpha-D-glucoside
?
wild-type AZOG and enzyme chimeric mutant AZF3
-
-
?
4-nitrophenyl alpha-D-glucoside
?
enzyme chimeric mutant AZF3
-
-
?
isomaltulose
sucrose
wild-type AZOG and enzyme chimeric mutant AZF3
-
-
r
isomaltulose
sucrose
enzyme chimeric mutant AZF3
-
-
r
kojibiose
?
wild-type AZOG
-
-
?
kojibiose
?
wild-type AZOG
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
main product isomaltulose, i.e. alpha-D-glucopyranosyl-1,6-D-fructofuranose or palatinose, and by-product trehalulose, i.e. alpha-D-glucopyranosyl-1,1-D-fructofuranose are two structural isomers of sucrose
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
main product isomaltulose, i.e. alpha-D-glucopyranosyl-1,6-D-fructofuranose or palatinose, and by-product trehalulose, i.e. alpha-D-glucopyranosyl-1,1-D-fructofuranose are two structural isomers of sucrose
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
the purified sucrose isomerase converts sucrose into 63% of isomaltulose and 30% of trehalulose at pH 6.3 and 33°C. Optimal reaction conditions for the conversion of sucrose into isomaltulose catalyzed by the immobilized sucrose isomerase is at a pH range 6.0-6.5 and 35-40°C
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
production of trehalulose and isomaltulose in a ratio of 64:36
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
production of trehalulose and isomaltulose in a ratio of 64:36 at 40°C. The product ratio depends on the reaction temperature, overview. The amount of trehalulose increases from 47.5% to 79.1% as temperature is lowered from 50°C to 30°C
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
production of trehalulose and isomaltulose in a ratio of 64:36
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
production of trehalulose and isomaltulose in a ratio of 64:36 at 40°C. The product ratio depends on the reaction temperature, overview. The amount of trehalulose increases from 47.5% to 79.1% as temperature is lowered from 50°C to 30°C
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
main products
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
high product specificity for trehalulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
activity involves residues D241, E295, H368, and D369
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
activity involves residues D241, E295, H368, and D369
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
wild-type AZOG and enzyme chimeric mutant AZF3
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
wild-type AZOG and enzyme chimeric mutant AZF3
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Bemisia argentifolia
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
enzyme chimeric mutant AZF3
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
isomaltulose + alpha 1,1-linked disaccharide
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
ir
i.e. isomaltulose, i.e. palatinose , formation of isomaltulose and a second alpha-1,1-linked disaccharide, trehalulose, by hydrolysis of sucrose followed by reaction of glucose with the C-6 and C-1 positions of the fructofuranose respectively
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
the enzyme is sucrose-specific
i.e. isomaltulose, i.e. palatinose , formation of isomaltulose and a second alpha-1,1-linked disaccharide, trehalulose, by hydrolysis of sucrose followed by reaction of glucose with the C-6 and C-1 positions of the fructofuranose respectively
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola
-
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola
-
-
isomaltulose + trehalulose. The ratio of trehalulose to isomaltulose increases at lower reaction temperatures. The optimal conditions for trehalulose production are pH 5.5-6.5 at 20 C
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola MX-45
-
-
isomaltulose + trehalulose. The ratio of trehalulose to isomaltulose increases at lower reaction temperatures. The optimal conditions for trehalulose production are pH 5.5-6.5 at 20 C
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola MX-45
-
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola MX-45
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
i.e. beta-D-glucopyranosyl-D-fructofuranose
isomaltulose + glucose,fructose 1,1'-disaccharide
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
isomerization of sucrose to isomaltulose is a highly efficient reaction, the formation of the beta-glucopyranosyl-enzyme complex followed by the nucleophilic attack of the 6'-OH group of fructose is concerted
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
isomerization of sucrose to isomaltulose is a highly efficient reaction, the formation of the beta-glucopyranosyl-enzyme complex followed by the nucleophilic attack of the 6'-OH group of fructose is concerted
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
i.e. beta-D-glucopyranosyl-D-fructofuranose
isomaltulose + glucose,fructose 1,1'-disaccharide
?
sucrose
alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
-
more than 90% conversion of sucrose. Small amounts of trehalulose, glucose, and fructose are produced as by-products
-
?
sucrose
alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
-
more than 90% conversion of sucrose. Small amounts of trehalulose, glucose, and fructose are produced as by-products
-
?
sucrose
alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
-
plus small amounts of glucose, fructose and eventually isomaltose as by-products
-
?
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
-
the major product is alpha-D-glucopyranosyl-1,6-D-fructofuranose, small amounts of alpha-D-glucopyranosyl-1,1-D-fructofuranose
?
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
-
wild-type enzyme: 82.8% alpha-D-glucopyranosyl-1,6-D-fructofuranose and 12.1% alpha-D-glucopyranosyl-1,1-D-fructofuranose
?
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
two-step reaction mechanism for hydrolysis and isomerization, which occurs in the same pocket
-
?
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 22:1 across pH- and temperature-range. Reaction is fast, conversion of 97% of sucrose in assay within 45 min
-
ir
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 22:1 across pH- and temperature-range. Reaction is fast, conversion of 97% of sucrose in assay within 45 min
-
ir
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 8:1 across pH- and temperature-range. Enzyme converts 84% of sucrose present in assay within 2 h
-
ir
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 8:1 across pH- and temperature-range. Enzyme converts 84% of sucrose present in assay within 2 h
-
ir
sucrose
isomaltulose
99% conversion
-
-
?
sucrose
isomaltulose
99% conversion
-
-
?
sucrose
isomaltulose
-
-
89-94% yield
-
?
sucrose
isomaltulose
-
-
89-94% yield
-
?
sucrose
isomaltulose + trehalulose
-
the product ratio is 78% isomaltulose and 22% trehalulose
-
?
sucrose
isomaltulose + trehalulose
-
-
-
-
?
sucrose
isomaltulose + trehalulose
-
-
-
-
?
sucrose
isomaltulose + trehalulose + D-glucose
Paraburkholderia acidicola
MutB catalyzes the isomerization of sucrose to mainly trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose)
-
-
r
sucrose
isomaltulose + trehalulose + D-glucose
Paraburkholderia acidicola MX-45
MutB catalyzes the isomerization of sucrose to mainly trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose)
-
-
r
sucrose
palatinose + trehalulose + D-glucose + D-fructose
-
-
at 30°C, 76.8% palatinose, 21.2% trehalulose, 1% each of D-glucose and D-fructose. Percentage of palatinose increases with temperature and reaches a maximum of 79.7% at 40°C
-
ir
sucrose
palatinose + trehalulose + D-glucose + D-fructose
-
-
at 30°C, 76.8% palatinose, 21.2% trehalulose, 1% each of D-glucose and D-fructose. Percentage of palatinose increases with temperature and reaches a maximum of 79.7% at 40°C
-
ir
turanose
?
enzyme chimeric mutant AZF3
-
-
?
turanose
?
enzyme chimeric mutant AZF3
-
-
?
additional information
?
-
gene Avin_08330 encodes the putative sucrose isomerase AZOG in the nitrogen-fixing bacterium Azotobacter vinelandii. The enzyme is a type of pseudo-sucrose isomerase harboring the RLDRD motif, a sucrose isomerase-specific region in 329-333. Neither sucrose isomerization nor hydrolysis activities are observed in recombinant AZOG (rAZOG). The rAZOG shows similar substrate specificity to the enzyme from Bacillus sp. O16G as it catalyzes the hydrolysis of isomaltulose and isomaltose, which contain alpha-1,6-glycosidic linkages. rAZOG generates isomaltose from the small substrate methyl-alpha-glucoside (MaG) via intermolecular transglycosylation. In addition, sucrose isomers isomaltulose and trehalulose are produced when 250 mM fructose is added to the MaG reaction mixture. Enzyme substrate specificity, overview. No activity with trehalose, maltose, nigerose, turanose, and panose. Comparison of substrate specificity with oligo-1,6-glucosidase, EC 3.2.1.10, from Bacillus halodurans strain O16G, UniProt ID BH2903, gene BH2903
-
-
?
additional information
?
-
-
gene Avin_08330 encodes the putative sucrose isomerase AZOG in the nitrogen-fixing bacterium Azotobacter vinelandii. The enzyme is a type of pseudo-sucrose isomerase harboring the RLDRD motif, a sucrose isomerase-specific region in 329-333. Neither sucrose isomerization nor hydrolysis activities are observed in recombinant AZOG (rAZOG). The rAZOG shows similar substrate specificity to the enzyme from Bacillus sp. O16G as it catalyzes the hydrolysis of isomaltulose and isomaltose, which contain alpha-1,6-glycosidic linkages. rAZOG generates isomaltose from the small substrate methyl-alpha-glucoside (MaG) via intermolecular transglycosylation. In addition, sucrose isomers isomaltulose and trehalulose are produced when 250 mM fructose is added to the MaG reaction mixture. Enzyme substrate specificity, overview. No activity with trehalose, maltose, nigerose, turanose, and panose. Comparison of substrate specificity with oligo-1,6-glucosidase, EC 3.2.1.10, from Bacillus halodurans strain O16G, UniProt ID BH2903, gene BH2903
-
-
?
additional information
?
-
gene Avin_08330 encodes the putative sucrose isomerase AZOG in the nitrogen-fixing bacterium Azotobacter vinelandii. The enzyme is a type of pseudo-sucrose isomerase harboring the RLDRD motif, a sucrose isomerase-specific region in 329-333. Neither sucrose isomerization nor hydrolysis activities are observed in recombinant AZOG (rAZOG). The rAZOG shows similar substrate specificity to the enzyme from Bacillus sp. O16G as it catalyzes the hydrolysis of isomaltulose and isomaltose, which contain alpha-1,6-glycosidic linkages. rAZOG generates isomaltose from the small substrate methyl-alpha-glucoside (MaG) via intermolecular transglycosylation. In addition, sucrose isomers isomaltulose and trehalulose are produced when 250 mM fructose is added to the MaG reaction mixture. Enzyme substrate specificity, overview. No activity with trehalose, maltose, nigerose, turanose, and panose. Comparison of substrate specificity with oligo-1,6-glucosidase, EC 3.2.1.10, from Bacillus halodurans strain O16G, UniProt ID BH2903, gene BH2903
-
-
?
additional information
?
-
Bemisia argentifolia
-
the enzymic potential for metabolizing sucrose shifts from favoring sucrose hydrolysis at low sucrose concentrations to sucrose isomerization at high sucrose concentrations. Trehalulose is synthesized for excretion when the carbon input from sucrose is in excess of metabolic needs
-
-
?
additional information
?
-
enzyme substrate specificity, overview. No activity with methyl alpha-D-glucoside, trehalose, nigerose, maltose, isomaltotriose, and panose, and poor activity with kojibiose and isomaltose. The sucrose is converted into isomaltose, isomatulose and trehalulose, as well as the hydrolysis products glucose and fructose by enzyme mutant AZF3, while wild-type AZOG only produces glucose and fructose
-
-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main product, and trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) as minor product, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
-
-
?
additional information
?
-
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main product, and trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) as minor product, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
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-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
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-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
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-
?
additional information
?
-
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
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?
additional information
?
-
-
enzyme does not catalyze the formation of any disaccharide from glucose and fructose. No trehalulose is detected when palatinose is the substrate and vice versa
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-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
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-
?
additional information
?
-
-
enzyme does not catalyze the formation of any disaccharide from glucose and fructose. No trehalulose is detected when palatinose is the substrate and vice versa
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-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
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-
?
additional information
?
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no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
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-
?
additional information
?
-
-
no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
-
-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
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-
?
additional information
?
-
no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
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-
?
additional information
?
-
-
no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
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-
?
additional information
?
-
Paraburkholderia acidicola
the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
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?
additional information
?
-
Paraburkholderia acidicola
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
Paraburkholderia acidicola MX-45
the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
-
-
?
additional information
?
-
Paraburkholderia acidicola MX-45
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main products, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
-
-
?
additional information
?
-
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main products, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
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-
?
additional information
?
-
the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
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-
?
additional information
?
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
-
-
?
additional information
?
-
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
-
-
?
additional information
?
-
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
-
the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
additional information
?
-
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
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-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
production of trehalulose and isomaltulose in a ratio of 64:36
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
production of trehalulose and isomaltulose in a ratio of 64:36
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
main products
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
high product specificity for trehalulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola MX-45
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
?
additional information
?
-
Bemisia argentifolia
-
the enzymic potential for metabolizing sucrose shifts from favoring sucrose hydrolysis at low sucrose concentrations to sucrose isomerization at high sucrose concentrations. Trehalulose is synthesized for excretion when the carbon input from sucrose is in excess of metabolic needs
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?
additional information
?
-
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main product, and trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) as minor product, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
-
-
?
additional information
?
-
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main product, and trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) as minor product, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
-
-
?
additional information
?
-
Paraburkholderia acidicola
the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
-
-
?
additional information
?
-
Paraburkholderia acidicola MX-45
the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
-
-
?
additional information
?
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main products, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
-
-
?
additional information
?
-
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main products, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
-
-
?
additional information
?
-
the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
-
-
?
additional information
?
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
-
-
?
additional information
?
-
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
-
-
?
additional information
?
-
the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
-
-
?
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evolution
the enzyme belongs to the glycoside hydrolase family 13 (GH13) in the CAZy classification
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
Paraburkholderia acidicola
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
Paraburkholderia acidicola MX-45
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
additional information
active site structure and substrate and ligand binding structures, overview
additional information
-
active site structure and substrate and ligand binding structures, overview
additional information
enzyme-substrate complex, docking study with sucrose and fructose
additional information
-
enzyme-substrate complex, docking study with sucrose and fructose
additional information
-
structural basis for the product specificity of NX-5, docking of fructofuranose and fructopyranose into the active site of the enzyme mutant D241A-glucose complex, molecular dynamics simulations, molecular mechanism controlling sucrose isomer formation, overview. Phe297 and Phe321 in enzyme NX-5 form an aromatic clamp near the entrance of the active pocket. Residues Asp102, His145, Arg239, His368, Asp369, Glu428, and Arg456 are responsible for sucrose binding and residues Asp241 (the nucleophile) and Glu295 (the acid catalyst) are crucial for sucrose hydrolysis. The active site pocket is stabilized by the salt bridge interactions between Arg239-Asp241, Asp102-Arg456 and Asp369-Arg456. Residues Arg325 and Arg328 are located in the325RLDRD329 motif and play roles in the product specificity
additional information
proteins AS9 PalI and SmuA differ in only one amino acid, structure of the wild-type sucrose isomerases is obtained by single point mutation through pymol using the crystal structure of SmuA from Protaminobacter rubrum strain CBS 547.77 (PDB ID 3GBD). Homology models of structures of the mutant sucrose isomerases are constructed based on the crystal structure of SmuA, using the EMBL-EBI server
additional information
-
proteins AS9 PalI and SmuA differ in only one amino acid, structure of the wild-type sucrose isomerases is obtained by single point mutation through pymol using the crystal structure of SmuA from Protaminobacter rubrum strain CBS 547.77 (PDB ID 3GBD). Homology models of structures of the mutant sucrose isomerases are constructed based on the crystal structure of SmuA, using the EMBL-EBI server
additional information
-
the unique RLDRD motif is located in a loop adjacent to the active site cleft and is determined to play an important role in the isomerization process and in the control of product specificity
additional information
-
the unique RLDRD motif is located in a loop adjacent to the active site cleft and is determined to play an important role in the isomerization process and in the control of product specificity
-
additional information
-
enzyme-substrate complex, docking study with sucrose and fructose
-
additional information
-
proteins AS9 PalI and SmuA differ in only one amino acid, structure of the wild-type sucrose isomerases is obtained by single point mutation through pymol using the crystal structure of SmuA from Protaminobacter rubrum strain CBS 547.77 (PDB ID 3GBD). Homology models of structures of the mutant sucrose isomerases are constructed based on the crystal structure of SmuA, using the EMBL-EBI server
-
additional information
-
the unique RLDRD motif is located in a loop adjacent to the active site cleft and is determined to play an important role in the isomerization process and in the control of product specificity
-
additional information
-
structural basis for the product specificity of NX-5, docking of fructofuranose and fructopyranose into the active site of the enzyme mutant D241A-glucose complex, molecular dynamics simulations, molecular mechanism controlling sucrose isomer formation, overview. Phe297 and Phe321 in enzyme NX-5 form an aromatic clamp near the entrance of the active pocket. Residues Asp102, His145, Arg239, His368, Asp369, Glu428, and Arg456 are responsible for sucrose binding and residues Asp241 (the nucleophile) and Glu295 (the acid catalyst) are crucial for sucrose hydrolysis. The active site pocket is stabilized by the salt bridge interactions between Arg239-Asp241, Asp102-Arg456 and Asp369-Arg456. Residues Arg325 and Arg328 are located in the325RLDRD329 motif and play roles in the product specificity
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D241A
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site-directed mutagenesis, glucose binding structure in comparison to the wild-type enzyme by crystal structure analysis
E295Q
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site-directed mutagenesis, sucrose binding structure in comparison to the wild-type enzyme by crystal structure analysis
F297A
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site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
F321A
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site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
R325D
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site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
R328D
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
R335H/R336T/K337I/D338P
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site-directed mutagenesis, glucose binding structure in comparison to the wild-type enzyme by crystal structure analysis
E295Q
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site-directed mutagenesis, sucrose binding structure in comparison to the wild-type enzyme by crystal structure analysis
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F297A
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site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
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R325D
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site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
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R328D
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site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
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D140E
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almost complete loss of catalytic activity
D140G
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almost complete loss of catalytic activity
D140N
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almost complete loss of catalytic activity
D329A
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42% of wild-type activity, no change in major products
L326Y
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20% of wild-type activity, no change in major products
L326Y/D329A
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3.4% of wild-type activity, no change in major products
D140E
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almost complete loss of catalytic activity
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D140G
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almost complete loss of catalytic activity
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D140N
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almost complete loss of catalytic activity
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D329A
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42% of wild-type activity, no change in major products
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L326Y
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20% of wild-type activity, no change in major products
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D327N
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turnover number for sucrose: 1.4fold decrease, KM-value for sucrose: 1.65fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 43.7% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 41.0% increase
D327R
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turnover number for sucrose: 2.45fold decrease, KM-value for sucrose: 2.2fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 26.5% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 17.7% increase
D329N
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turnover number for sucrose: 1.17fold decrease, KM-value for sucrose: 2.9fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 52.4% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 54.7% increase
E498P
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temperature-optimum is 40°C compared to 35°C for the wild-type enzyme, maximal specific activity increases by 7%. Half-life at 50°C is 9.45 min compared to 1.81 min for wild-type enzyme. Mutation slightly increases the ratio of turnover number to KM-value. Percent content of monosaccharide decreases from 5.9% of the wild-type enzyme to 3.4%
E498P/R310P
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temperature-optimum is 45°C compared to 35°C for the wild-type enzyme, maximal specific activity increases by 16%. Half-life is 13.61 min compared to 1.81 min for wild-type enzyme. Mutation slightly increases the ratio of turnover number to KM-value. Percent content of monosaccharide decreases from 5.9% of the wild-type enzyme to 3.3%
R325D
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turnover number for sucrose: 14.5fold decrease, KM-value for sucrose: 1.2fold decrease, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 67% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 43.6% increase
R325L
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turnover number for sucrose: 14.5fold decrease, KM-value for sucrose: 1.1fold decrease, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 54.3% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 31.3% increase
R328D
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turnover number for sucrose: 11.9fold decrease, KM-value for sucrose: 2fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 65.6% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 61.2% increase
R328L
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turnover number for sucrose: 14.5fold decrease, KM-value for sucrose: 5fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 51.9% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 50.3% increase
D200A
Paraburkholderia acidicola
enzyme mutant structure analysis
D442N
Paraburkholderia acidicola
the mutant favors the transfer reaction with an isomer preference for isomaltulose
E254Q
Paraburkholderia acidicola
enzyme mutant structure analysis
R311C
Paraburkholderia acidicola
the mutant demonstrates higher catalytic efficiency for D-glucose production over trehalulose production
D200A
Paraburkholderia acidicola MX-45
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enzyme mutant structure analysis
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D442N
Paraburkholderia acidicola MX-45
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the mutant favors the transfer reaction with an isomer preference for isomaltulose
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E254Q
Paraburkholderia acidicola MX-45
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enzyme mutant structure analysis
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R311C
Paraburkholderia acidicola MX-45
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the mutant demonstrates higher catalytic efficiency for D-glucose production over trehalulose production
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F164L
site-directed mutagenesis, three-dimensional structure from crystal structure analysis, comparison to the wild-type. The mutant shows hydrolytic activity converting sucrose to glucose and fructose, kinetics
R284C
site-directed mutagenesis, three-dimensional structure from crystal structure analysis, comparison to the wild-type. The mutant shows hydrolytic activity converting sucrose to glucose and fructose, kinetics. Presence of Mg2+, Ca2+ and Zn2+ ions and glucose have no effect on the activity of the R284C mutant
F164L
enzyme mutant structure analysis
R284C
enzyme mutant structure analysis
E175N
site-directed mutagenesis, the mutant shows increased activity and exhibits an identical pH optimum and a slightly increased optimal temperature (35°C) compared to wild-type enzyme (30°C)
E175N/K576
site-directed mutagenesis, the mutant shows increased activity and exhibits an identical pH optimum and a slightly increased optimal temperature (35°C) compared to wild-type enzyme (30°C)
E428D
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
F297A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F297P
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F297P/R333K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
F321A
site-directed mutagenesis, the mutant shows only hydrolytic activity
F321A/F319A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G176D
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
K174D
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
K576D
site-directed mutagenesis, the mutant shows increased activity and exhibits an identical pH optimum and a slightly increased optimal temperature (35°C) compared to wild-type enzyme (30°C)
N577K
site-directed mutagenesis, the mutant's activity is similar to the wild-type enzyme
R333K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R456K
site-directed mutagenesis, inactive mutant
S575D
site-directed mutagenesis, the mutant's activity is similar to the wild-type enzyme
E175N
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site-directed mutagenesis, the mutant shows increased activity and exhibits an identical pH optimum and a slightly increased optimal temperature (35°C) compared to wild-type enzyme (30°C)
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G176D
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site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
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K174D
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site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
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K576D
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site-directed mutagenesis, the mutant shows increased activity and exhibits an identical pH optimum and a slightly increased optimal temperature (35°C) compared to wild-type enzyme (30°C)
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E428D
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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F297A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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F297P
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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F297P/R333K
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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additional information
construction of chimeric mutant enzymes AZF3 and AZF5 from sucrose isomerase AZOG of Azotobacter vinelanddii and and sucrose isomerase, encoded by esi gene, from Enterobacter sp. FMB-1. Mutant AZF3 has the N-terminal region of Enterobacter SIase and C-terminal region of AZOG, while mutant AZF5 contains the N-terminal region of AZOG and C-terminal region of Enterobacter SIase. Determination of transglycosylation activity, overview. Mutant AZF3 shows altered substrate specificity and reduced activity compared to the wild-type enzyme
additional information
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construction of chimeric mutant enzymes AZF3 and AZF5 from sucrose isomerase AZOG of Azotobacter vinelanddii and and sucrose isomerase, encoded by esi gene, from Enterobacter sp. FMB-1. Mutant AZF3 has the N-terminal region of Enterobacter SIase and C-terminal region of AZOG, while mutant AZF5 contains the N-terminal region of AZOG and C-terminal region of Enterobacter SIase. Determination of transglycosylation activity, overview. Mutant AZF3 shows altered substrate specificity and reduced activity compared to the wild-type enzyme
additional information
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construction of chimeric mutant enzymes AZF3 and AZF5 from sucrose isomerase AZOG of Azotobacter vinelanddii and and sucrose isomerase, encoded by esi gene, from Enterobacter sp. FMB-1. Mutant AZF3 has the N-terminal region of Enterobacter SIase and C-terminal region of AZOG, while mutant AZF5 contains the N-terminal region of AZOG and C-terminal region of Enterobacter SIase. Determination of transglycosylation activity, overview. Mutant AZF3 shows altered substrate specificity and reduced activity compared to the wild-type enzyme
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additional information
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isomaltulose production via yeast surface display of sucrose isomerase from Enterobacter sp. strain FMB-1 on Saccharomyces cerevisiae strain EBY100, stable at a broad range of temperatures (35-55°C) and pHs (pH 5-7) with optimal temperature and pH at 45°C and pH 7.0, respectively
additional information
construction of chimeric mutant enzymes AZF3 and AZF5 from sucrose isomerase SIase from Enterobacter sp. strain FMB-1 and AZOG of Azotobacter vinelanddii. Mutant AZF3 has the N-terminal region of Enterobacter SIase and C-terminal region of AZOG, while mutant AZF5 contains the N-terminal region of AZOG and C-terminal region of Bacillus halodurans SIase. Gene Avin_08330 encodes the putative sucrose isomerase AZOG in the nitrogen-fixing bacterium Azotobacter vinelandii. The enzyme is a type of pseudo-sucrose isomerase harboring the RLDRD motif, a sucrose isomerase-specific region in 329-333. Neither sucrose isomerization nor hydrolysis activities are observed in recombinant AZOG. Determination of transglycosylation activity, overview. Mutant AZF3 shows altered substrate specificity and reduced activity compared to the wild-type enzyme AZOG. The sucrose is converted into isomaltose, isomatulose and trehalulose, as well as the hydrolysis products glucose and fructose by mutant AZF3, while wild-type AZOG only produces glucose and fructose
additional information
immobilization of Escherichia coli strain BL21(DE3) cells recombinantly expressing the enzyme by sodium alginate and CaCl2 solution in untreated cane molasses and corn steep liquor medium for enzyme production and isomaltulose production
additional information
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mutations of the loop region of enzyme NX-5 result in significant changes of the product ratio between isomaltulose and trehalulose
additional information
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bioinspired production of antibacterial sucrose isomerase-sponge for the synthesis of isomaltulose, enzyme immobilization, method development, optimization, and evaluation, overview. The enzyme is immobilized on a epsilon-poly-L-lysine (epsilons-PL)-gelatin sponge as matrix is produced by the lyophilizing method, using water as a porogen. The carboxyl groups of gelatin are activated by 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) and N-hydroxysuccinimide (NHS) to form reactive NHS esters, which can promote the rate of the synthesis reaction to form a stable amide bond. Then the esters react with amine groups of epsilon-PL to form peptide bonds. Through a series of cross-linking reactions, gelatin and epsilon-PL form a sponge. The affinity of immobilized enzyme SIase to substrate is basically unchanged. Immobilized SIase still exhibits more than 90% sucrose conversion after 13 consecutive cycles, which indicates that it has a good operational stability. Furthermore, the immobilized SIase has the potential for isomaltulose production, with 200 g/l sucrose solution as its substrate in the food industry. Isomaltulose is isolated in 83.58% yield and high purity (97.3%). epsilon-Poly-L-lysine (epsilon-PL), is an ideal carrier for enzyme immobilization and has attracted considerable attention because of its good biocompatibility, antimicrobial activity, and non-toxic characteristic. The loose and porous structures of epsilon-PL-gelatin sponge are critical for ensuring relatively high catalytic efficiency
additional information
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immobilization of cells expressing the recombinant wild-type enzyme, and mutant BN 68069 cells, on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the recombinant wild-type enzyme, and mutant BN 68069 cells, on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the recombinant wild-type enzyme, and mutant BN 68069 cells, on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the recombinant wild-type enzyme, and mutant BN 68069 cells, on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
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immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
-
immobilization of cells expressing the recombinant wild-type enzyme, and mutant BN 68069 cells, on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
additional information
-
mutations of the loop region of enzyme NX-5 result in significant changes of the product ratio between isomaltulose and trehalulose
-
additional information
-
bioinspired production of antibacterial sucrose isomerase-sponge for the synthesis of isomaltulose, enzyme immobilization, method development, optimization, and evaluation, overview. The enzyme is immobilized on a epsilon-poly-L-lysine (epsilons-PL)-gelatin sponge as matrix is produced by the lyophilizing method, using water as a porogen. The carboxyl groups of gelatin are activated by 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) and N-hydroxysuccinimide (NHS) to form reactive NHS esters, which can promote the rate of the synthesis reaction to form a stable amide bond. Then the esters react with amine groups of epsilon-PL to form peptide bonds. Through a series of cross-linking reactions, gelatin and epsilon-PL form a sponge. The affinity of immobilized enzyme SIase to substrate is basically unchanged. Immobilized SIase still exhibits more than 90% sucrose conversion after 13 consecutive cycles, which indicates that it has a good operational stability. Furthermore, the immobilized SIase has the potential for isomaltulose production, with 200 g/l sucrose solution as its substrate in the food industry. Isomaltulose is isolated in 83.58% yield and high purity (97.3%). epsilon-Poly-L-lysine (epsilon-PL), is an ideal carrier for enzyme immobilization and has attracted considerable attention because of its good biocompatibility, antimicrobial activity, and non-toxic characteristic. The loose and porous structures of epsilon-PL-gelatin sponge are critical for ensuring relatively high catalytic efficiency
-
additional information
-
immobilization of Escherichia coli strain BL21(DE3) cells recombinantly expressing the enzyme by sodium alginate and CaCl2 solution in untreated cane molasses and corn steep liquor medium for enzyme production and isomaltulose production
-
additional information
-
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
additional information
-
enzyme immobilization by adsorption on a chromatographic resin, optimal reaction conditions for the conversion of sucrose into isomaltulose catalyzed by the immobilized sucrose isomerase is at a pH range 6.0-6.5 and 35-40°C
additional information
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immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
cloning of the PdSIase gene into the expression vector pET28a, functional recombinant expression in Yarrowia lipolytica strain CGMCC7326 on the cell surface using the cell wall protein Pir1 as an anchor protein. Selection via a hygromycin B resistance gene as a selection marker, method, overview
additional information
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cloning of the PdSIase gene into the expression vector pET28a, functional recombinant expression in Yarrowia lipolytica strain CGMCC7326 on the cell surface using the cell wall protein Pir1 as an anchor protein. Selection via a hygromycin B resistance gene as a selection marker, method, overview
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additional information
engineering of the enzyme to exhibit isomelezitose synthase activity for production of the probiotically nutrial component, overview
additional information
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engineering of the enzyme to exhibit isomelezitose synthase activity for production of the probiotically nutrial component, overview
additional information
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immobilization of cells expressing the recombinant wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
-
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
the half-lives of the enzyme mutants E175N, K576D and E175N/K576D are 2.30, 1.78 and 7.65 times greater than that of the wild-type enzyme at 45°C, respectively. The Km values for the E175N, K576D and E175N/K576D mutants decrease by 6.6%, 2.0% and 11.0%, respectively, and their kcat/Km values increase by 38.2%, 4.2% and 19.4%, respectively, compared with those of the wild-type enzyme. After optimizing the conditions for isomaltulose production at 45°C, the E175N, K576D and E175N/K576D mutants display slightly improved isomaltulose yields, compared with the wild-type enzyme. The catalytic efficiencies (kcat/Km values) of E175N, K576D and E175N/K576D are increased by 38.2%, 4.2% and 19.4%, respectively
additional information
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the half-lives of the enzyme mutants E175N, K576D and E175N/K576D are 2.30, 1.78 and 7.65 times greater than that of the wild-type enzyme at 45°C, respectively. The Km values for the E175N, K576D and E175N/K576D mutants decrease by 6.6%, 2.0% and 11.0%, respectively, and their kcat/Km values increase by 38.2%, 4.2% and 19.4%, respectively, compared with those of the wild-type enzyme. After optimizing the conditions for isomaltulose production at 45°C, the E175N, K576D and E175N/K576D mutants display slightly improved isomaltulose yields, compared with the wild-type enzyme. The catalytic efficiencies (kcat/Km values) of E175N, K576D and E175N/K576D are increased by 38.2%, 4.2% and 19.4%, respectively
additional information
-
the half-lives of the enzyme mutants E175N, K576D and E175N/K576D are 2.30, 1.78 and 7.65 times greater than that of the wild-type enzyme at 45°C, respectively. The Km values for the E175N, K576D and E175N/K576D mutants decrease by 6.6%, 2.0% and 11.0%, respectively, and their kcat/Km values increase by 38.2%, 4.2% and 19.4%, respectively, compared with those of the wild-type enzyme. After optimizing the conditions for isomaltulose production at 45°C, the E175N, K576D and E175N/K576D mutants display slightly improved isomaltulose yields, compared with the wild-type enzyme. The catalytic efficiencies (kcat/Km values) of E175N, K576D and E175N/K576D are increased by 38.2%, 4.2% and 19.4%, respectively
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additional information
-
immobilization of cells expressing the recombinant wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
additional information
-
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
additional information
-
immobilization of cells expressing the recombinant wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
additional information
-
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
additional information
-
engineering of the enzyme to exhibit isomelezitose synthase activity for production of the probiotically nutrial component, overview
-
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food industry
-
isomaltulose is widely used as sucrose substitute in diet and diabetes products
food industry
sucrose isomerase activity is used industrially for the conversion of sucrose into isomers, particularly isomaltulose or trehalulose, which have properties advantageous over sucrose for some food uses. The industrial potential may be further enhanced by selection for variants that do not catabolize the sucrose substrate
food industry
sucrose isomerase activity is used industrially for the conversion of sucrose into isomers, particularly isomaltulose or trehalulose, which have properties advantageous over sucrose for some food uses.The industrial potential may be further enhanced by selection for variants that do not catabolize the sucrose substrate
food industry
-
sucrose isomerase activity is used industrially for the conversion of sucrose into isomers, particularly isomaltulose or trehalulose, which have properties advantageous over sucrose for some food uses.The industrial potential may be further enhanced by selection for variants that do not catabolize the sucrose substrate
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synthesis
-
formation of isomaltulose by immobilized Erwinia rhapontici cells
synthesis
-
production of palatinose, which is used as a sweetener and as a substitute for sucrose
synthesis
-
strain produces isomaltulose with maximum yield of 78-89% of supplied sucrose and 4% contaminating trehalose
synthesis
-
strain FMB1 show more than 90% conversion of sucrose at 4 g per l into isomaltulose in 2 days, with small amounts of trehalulose, glucose, and fructose as by-products. Use of strain in industrial production of isomaltulose
synthesis
immobilized cells of Protaminobacter rubrum strain CBS 574.77 are commonly used for the synthesis of isomaltulose from sucrose on an industrial scale
synthesis
isomaltulose production by the enzyme roduced from immobilized of Escherichia coli cells recombinantly expressing the enzyme, method overview
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
Paraburkholderia acidicola
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
strain produces isomaltulose with maximum yield of 78-89% of supplied sucrose and 4% contaminating trehalose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
immobilized cells of Protaminobacter rubrum strain CBS 574.77 are commonly used for the synthesis of isomaltulose from sucrose on an industrial scale
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
Paraburkholderia acidicola MX-45
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
strain FMB1 show more than 90% conversion of sucrose at 4 g per l into isomaltulose in 2 days, with small amounts of trehalulose, glucose, and fructose as by-products. Use of strain in industrial production of isomaltulose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
isomaltulose production by the enzyme roduced from immobilized of Escherichia coli cells recombinantly expressing the enzyme, method overview
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synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
Paraburkholderia acidicola
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
Paraburkholderia acidicola MX-45
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
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-
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Characterization of divergent pseudo-sucrose isomerase from Azotobacter vinelandii Deciphering the absence of sucrose isomerase activity
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483
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brenda
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Isomaltulose production by yeast surface display of sucrose isomerase from Pantoea dispersa on Yarrowia lipolytica
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32
208-217
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-
brenda
Duan, X.; Cheng, S.; Ai, Y.; Wu, J.
Enhancing the thermostability of Serratia plymuthica sucrose isomerase using B-factor-directed mutagenesis
PLoS ONE
11
e0149208
2016
Serratia plymuthica (D0VX20), Serratia plymuthica, Serratia plymuthica AS9 (D0VX20), Serratia plymuthica AS9
brenda