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2 lactose
lactulose + epilactose
the yields of lactulose and epilactose catalyzed by the wild-type enzyme reaches around 57% and 16%, respectively, after 4 h
-
-
r
2 lactulose
lactose + epilactose
4-O-alpha-D-glucopyranosyl-D-mannose
maltose
-
-
-
r
4-O-beta-D-glucopyranosyl-D-mannose
cellobiose
-
-
-
r
4-O-beta-D-glucosyl-D-mannose
4-O-beta-D-galactosyl-D-mannose
4-O-beta-D-glucosyl-D-mannose
cellobiose
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
4-O-beta-D-mannopyranosyl-D-glucose
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
4-O-beta-D-mannopyranosyl-D-glucose
mannobiose
-
-
-
r
4-O-beta-D-mannopyranosyl-D-mannose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
beta-1,4-mannobiose
4-O-beta-D-mannopyranosyl-D-glucose
beta-mannobiose
4-O-beta-D-mannopyranosyl-D-glucose
-
putative product
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
cellobiose
D-glucosyl-D-mannose
cellotetraose
4-O-beta-D-glucopyranosyl-(1-4)-O-beta-D-glucopyranosyl-(1-4)-O-beta-D-glucopyranosyl-(1-4)-D-mannose
the enzyme is found to 2-epimerize the reducing terminal glucose moieties of cellotriose and cellotetraose in addition to cellobiose
-
-
?
cellotetraose
beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-D-mannose
-
-
-
r
cellotriose
4-O-beta-D-glucopyranosyl-(1-4)-O-beta-D-glucopyranosyl-(1-4)-D-mannose
the enzyme is found to 2-epimerize the reducing terminal glucose moieties of cellotriose and cellotetraose in addition to cellobiose
-
-
?
cellotriose
4-O-beta-D-glucopyranosyl-4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
-
?
cellotriose
4-O-beta-D-glucopyranosyl-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellotriose
beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-D-mannose
-
-
-
r
D-fructose
D-glucose + D-mannose
-
-
-
-
?
D-lyxose
D-xylose
-
-
-
-
?
D-xylose
D-lyxose
-
-
-
-
?
D-xylulose
D-xylose + D-lyxose
-
low activity
-
-
?
globotriose
O-alpha-D-galactopyranosyl-(1,4)-O-beta-D-galactopyranosyl-(1,4)-D-mannose
-
putative product
-
r
L-allose
L-altrose
-
low activity
-
-
?
L-altrose
L-allose
-
-
-
-
?
L-arabinose
L-ribose
-
low activity
-
-
?
L-gulose
L-idose
-
low activity
-
-
?
L-idose
L-gulose
-
-
-
-
?
L-psicose
L-allose + L-altrose
-
low activity
-
-
?
L-ribulose
L-arabinose + L-ribose
-
low activity
-
-
?
L-sorbose
L-gulose + L-idose
-
low activity
-
-
?
lactose
4-O-beta-D-galactopyranosyl-D-mannose
maltose
4-O-alpha-D-glucopyranosyl-D-mannose
maltotriose
4-O-alpha-D-glucopyranosyl-4-O-alpha-D-glucopyranosyl-D-mannose
-
-
-
-
?
maltotriose
4-O-alpha-D-glucopyranosyl-O-alpha-D-glucopyranosyl-D-mannose
-
-
-
r
mannobiose
4-O-beta-D-mannopyranosyl-D-glucose
mannose
D-glucose + D-fructose
-
the enzyme exhibits the highest isomerization activity for mannose among monosaccharides
-
-
?
mannotriose
4-O-beta-D-mannopyranosyl-O-beta-D-mannopyranosyl-D-glucose
-
-
-
r
additional information
?
-
2 lactulose
lactose + epilactose
-
-
-
r
2 lactulose
lactose + epilactose
-
-
-
r
2 lactulose
lactose + epilactose
-
-
-
r
4-O-beta-D-glucosyl-D-mannose
4-O-beta-D-galactosyl-D-mannose
-
-
-
r
4-O-beta-D-glucosyl-D-mannose
4-O-beta-D-galactosyl-D-mannose
-
-
-
r
4-O-beta-D-glucosyl-D-mannose
cellobiose
-
-
-
-
r
4-O-beta-D-glucosyl-D-mannose
cellobiose
-
-
-
r
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
4-O-beta-D-mannopyranosyl-D-glucose
-
-
-
-
r
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
4-O-beta-D-mannopyranosyl-D-glucose
-
best substrate
-
-
r
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
4-O-beta-D-mannopyranosyl-D-glucose
-
-
-
-
r
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
beta-D-mannopyranosyl-(1->4)-D-glucose
-
-
-
?
beta-1,4-mannobiose
4-O-beta-D-mannopyranosyl-D-glucose
-
-
-
r
beta-1,4-mannobiose
4-O-beta-D-mannopyranosyl-D-glucose
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
-
-
r
beta-1,4-mannobiose
4-O-beta-D-mannopyranosyl-D-glucose
best substrate
-
-
r
beta-1,4-mannobiose
4-O-beta-D-mannopyranosyl-D-glucose
best substrate
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
preferred substrate
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
Caldicellulosiruptor obsidiansis ATCC BAA-2073 / strain OB47
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
Caldicellulosiruptor obsidiansis ATCC BAA-2073 / strain OB47
preferred substrate
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
the enzyme activity is approximately 100fold higher for cellobiose than for D-glucose
-
-
?
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
i.e. 4-O-beta-D-glucopyranosyl-D-mannose
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
-
?
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
-
?
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
binding structure, overview
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
?
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
-
?
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
r
-
?
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
at equilibrium the enzymic interconversion favors the cellobiose configuration
-
?
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
the enzyme is found to 2-epimerize the reducing terminal glucose moieties of cellotriose and cellotetraose in addition to cellobiose
-
-
?
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
cellobiose 2-epimerase catalyzes a hydroxyl stereoisomerism at C-2 of the reducing terminal glucose moiety
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
-
?
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
i.e. 4-O-beta-D-glucopyranosyl-D-mannose
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
i.e. 4-O-beta-D-glucopyranosyl-D-mannose
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
(beta1,4)
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
(beta1,4), best substrate of md2
-
-
r
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
?
cellobiose
4-O-beta-D-glucopyranosyl-D-mannose
-
-
-
r
cellobiose
D-glucosyl-D-mannose
-
-
-
-
?
cellobiose
D-glucosyl-D-mannose
-
-
-
-
?
cellobiose
D-glucosyl-D-mannose
-
-
-
r
cellobiose
D-glucosyl-D-mannose
-
-
-
r
D-glucose
D-mannose
-
-
-
-
?
D-glucose
D-mannose
-
-
-
-
?
D-glucose
D-mannose
-
-
-
-
?
D-glucose
D-mannose
-
-
-
r
D-glucose
D-mannose
-
-
-
r
D-mannose
D-glucose
-
-
-
-
?
D-mannose
D-glucose
-
-
-
-
r
D-mannose
D-glucose
-
-
-
-
r
D-mannose
D-glucose
-
-
-
r
D-mannose
D-glucose
-
-
-
r
epilactose
lactose
lactose production occurs earlier and faster than lactulose production. The lactose content decreases after an initial increase. Simultaneously, the epilactose content decreases rapidly during this first part of the conversion to about 26%. Therefore, 20 min into the conversion of epilactose as a starting substrate, an inversion of the amounts of the two sugars occurr, resulting in about 26% epilactose and 66% lactose
-
-
r
epilactose
lactose
lactose production occurs earlier and faster than lactulose production. The lactose content decreases after an initial increase. Simultaneously,the epilactose content decreases rapidly during this first part of the conversion to about 26%. Therefore, 20 min into the conversion of epilactose as a starting substrate, an inversion of the amounts of the two sugars occurrs, resulting in about 26% epilactose and 66% lactose
-
-
r
epilactose
lactose
lactose production occurs earlier and faster than lactulose production. The lactose content decreases after an initial increase. Simultaneously,the epilactose content decreases rapidly during this first part of the conversion to about 26%. Therefore, 20 min into the conversion of epilactose as a starting substrate, an inversion of the amounts of the two sugars occurrs, resulting in about 26% epilactose and 66% lactose
-
-
r
epilactose
lactose
i.e. 4-O-beta-D-galactopyranosyl-D-mannose
-
-
r
epilactose
lactose
(beta1,4)
-
-
r
epilactose
lactulose
lactose production occurs earlier and faster than lactulose production. The lactose content decreases after an initial increase. Simultaneously,the epilactose content decreases rapidly during this first part of the conversion to about 26%. Therefore, 20 min into the conversion of epilactose as a starting substrate, an inversion of the amounts of the two sugars occurr, resulting in about 26% epilactose and 66% lactose
-
-
r
epilactose
lactulose
lactose production occurs earlier and faster than lactulose production. The lactose content decreases after an initial increase. Simultaneously,the epilactose content decreases rapidly during this first part of the conversion to about 26%. Therefore, 20 min into the conversion of epilactose as a starting substrate, an inversion of the amounts of the two sugars occurrs, resulting in about 26% epilactose and 66% lactose
-
-
r
epilactose
lactulose
lactose production occurs earlier and faster than lactulose production. The lactose content decreases after an initial increase. Simultaneously,the epilactose content decreases rapidly during this first part of the conversion to about 26%. Therefore, 20 min into the conversion of epilactose as a starting substrate, an inversion of the amounts of the two sugars occurrs, resulting in about 26% epilactose and 66% lactose
-
-
r
lactose
4-O-beta-D-galactopyranosyl-D-mannose
-
-
-
r
lactose
4-O-beta-D-galactopyranosyl-D-mannose
-
-
-
r
lactose
4-O-beta-D-galactopyranosyl-D-mannose
-
-
i.e. epilactose
-
?
lactose
4-O-beta-D-galactopyranosyl-D-mannose
-
epilactose
-
r
lactose
4-O-beta-D-galactopyranosyl-D-mannose
-
i.e. epilactose
-
?
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
-
r
lactose
epilactose
-
-
-
?
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
-
r
lactose
epilactose
the epimerisation and, therefore, the production of epilactose can be seen to occure arlier and faster than the production of lactulose. After reaching a maximal ratio of about 28% after 10 min, the epilactose content decreases and so does the lactose content, while the lactulose content increases over the course of the whole conversion. The conversion reaches an apparent steady state with apparent final sugar ratios of 55.0% lactulose, 14.6% epilactose and 30.4% lactose
-
-
r
lactose
epilactose
the yields of lactulose and epilactose catalyzed by the wild-type enzyme reaches around 57% and 16%, respectively, after 4 h. The concentration of lactulose catalyzed by mutant enzyme R5M/A12S/I52V/F231L/K328I rapidly increases from 0 min to 90 min and then increases gradually to the steady-state level with a yield of lactulose up to approximately 76%. No obvious epilactose is detected at any time
-
-
?
lactose
epilactose
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
-
-
r
lactose
epilactose
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
-
-
?
lactose
epilactose
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
-
r
lactose
epilactose
-
-
-
-
r
lactose
epilactose
-
-
-
-
?
lactose
epilactose
-
-
-
r
lactose
epilactose
the epimerisation and, therefore, the production of epilactose can be seen to occure arlier and faster than the production of lactulose. After reaching a maximal ratio of about 28% after 10 min, the epilactose content decreases and so does the lactose content, while the lactulose content increases over the course of the whole conversion. The conversion reaches an apparent steady state with apparent final sugar ratios of 54.4% lactulose, 14.8% epilactose and 30.8% lactose
-
-
r
lactose
epilactose
-
-
-
-
?
lactose
epilactose
the epimerisation and, therefore, the production of epilactose can be seen to occure arlier and faster than the production of lactulose. After reaching a maximal ratio of about 28% after 10 min, the epilactose content decreases and so does the lactose content, while the lactulose content increases over the course of the whole conversion. The conversion reaches an apparent steady state with apparent final sugar ratios of 54.4% lactulose, 14.8% epilactose and 30.8% lactose
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
binding structure, overview
-
r
lactose
epilactose
enzyme reaction assay with immobilized enzyme
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
-
r
lactose
epilactose
enzyme reaction assay with immobilized enzyme
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
i.e. 4-O-beta-galactosyl-D-mannose
-
?
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
i.e. 4-O-beta-galactosyl-D-mannose
-
?
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
i.e. 4-O-beta-D-galactopyranosyl-D-glucose
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
i.e. 4-O-beta-D-galactopyranosyl-D-glucose
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
at pH 7.0 and 60°C, 50 mM epilactose is produced from 200 mM lactose by a 600 nM of enzyme concentration after reaction for 4 h
-
-
r
lactose
epilactose
-
-
-
r
lactose
epilactose
at pH 7.0 and 60°C, 50 mM epilactose is produced from 200 mM lactose by a 600 nM of enzyme concentration after reaction for 4 h
-
-
r
lactose
epilactose
(beta1,4)
-
-
r
lactose
epilactose
-
-
-
r
lactose
lactulose
-
-
-
r
lactose
lactulose
-
-
-
r
lactose
lactulose
-
-
-
-
r
lactose
lactulose
when lactose is used as substrate, epilactose is rapidly produced in a short period, and afterwards both epilactose and lactose are steadily isomerised to lactulose, with a final ratio of 35:11:54 for lactose:epilactose:lactulose
-
-
r
lactose
lactulose
Caldicellulosiruptor obsidiansis ATCC BAA-2073 / strain OB47
when lactose is used as substrate, epilactose is rapidly produced in a short period, and afterwards both epilactose and lactose are steadily isomerised to lactulose, with a final ratio of 35:11:54 for lactose:epilactose:lactulose
-
-
r
lactose
lactulose
-
-
-
?
lactose
lactulose
-
-
-
r
lactose
lactulose
cellobiose 2-epimerase from Caldicellulosiruptor saccharolyticus can be used in the presence of borate for the production of lactulose from lactose, method development, overview
-
-
?
lactose
lactulose
the epimerisation and, therefore, the production of epilactose can be seen to occure earlier and faster than the production of lactulose. After reaching a maximal ratio of about 28% after 10 min, the epilactose content decreases and so does the lactose content, while the lactulose content increases over the course of the whole conversion. The conversion reaches an apparent steady state with apparent final sugar ratios of 55.0% lactulose, 14.6% epilactose and 30.4% lactose
-
-
r
lactose
lactulose
the yields of lactulose and epilactose catalyzed by the wild-type enzyme reaches around 57% and 16%, respectively, after 4 h. The concentration of lactulose catalyzed by mutant enzyme R5M/A12S/I52V/F231L/K328I rapidly increases from 0 min to 90 min and then increases gradually to the steady-state level with a yield of lactulose up to approximately 76%. No obvious epilactose is detected at any time
-
-
?
lactose
lactulose
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
-
-
?, r
lactose
lactulose
-
-
-
-
?
lactose
lactulose
the epimerisation and, therefore, the production of epilactose can be seen to occure arlier and faster than the production of lactulose. After reaching a maximal ratio of about 28% after 10 min, the epilactose content decreases and so does the lactose content, while the lactulose content increases over the course of the whole conversion. The conversion reaches an apparent steady state with apparent final sugar ratios of 54.4% lactulose, 14.8% epilactose and 30.8% lactose
-
-
r
lactose
lactulose
the epimerisation and, therefore, the production of epilactose can be seen to occure arlier and faster than the production of lactulose. After reaching a maximal ratio of about 28% after 10 min, the epilactose content decreases and so does the lactose content, while the lactulose content increases over the course of the whole conversion. The conversion reaches an apparent steady state with apparent final sugar ratios of 54.4% lactulose, 14.8% epilactose and 30.8% lactose
-
-
r
lactose
lactulose
-
-
-
r
lactose
lactulose
-
-
-
r
lactose
lactulose
-
-
-
r
lactose
lactulose
-
-
-
r
lactose
lactulose
-
-
-
r
lactose
lactulose
-
-
-
r
lactose
lactulose
-
-
-
r
lactose
lactulose
-
-
-
r
maltose
4-O-alpha-D-glucopyranosyl-D-mannose
-
-
-
-
?
maltose
4-O-alpha-D-glucopyranosyl-D-mannose
i.e.4-O-alpha-D-glucopyranosyl-D-glucose
-
-
r
mannobiose
4-O-beta-D-mannopyranosyl-D-glucose
i.e 4-O-b-D-mannopyranosyl-D-mannose
-
-
r
mannobiose
4-O-beta-D-mannopyranosyl-D-glucose
i.e 4-O-beta-D-mannopyranosyl-D-mannose
-
-
r
mannobiose
4-O-beta-D-mannopyranosyl-D-glucose
(beta1,4)
-
-
r
mannobiose
4-O-beta-D-mannopyranosyl-D-glucose
(beta1,4), best substrate of md1
-
-
r
additional information
?
-
recombinant enzyme catalyzes a hydroxyl stereoisomerism at the C2-positions of the reducing terminal glucose and at the mannose moiety of cello-oligosaccharides: lactose, beta-mannobiose and globotriose
-
-
?
additional information
?
-
-
recombinant enzyme catalyzes a hydroxyl stereoisomerism at the C2-positions of the reducing terminal glucose and at the mannose moiety of cello-oligosaccharides: lactose, beta-mannobiose and globotriose
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the recombinant enzyme shows both epimerisation and isomerisation activities against lactose
-
-
?
additional information
?
-
-
the recombinant enzyme shows both epimerisation and isomerisation activities against lactose
-
-
?
additional information
?
-
Caldicellulosiruptor obsidiansis ATCC BAA-2073 / strain OB47
the recombinant enzyme shows both epimerisation and isomerisation activities against lactose
-
-
?
additional information
?
-
-
the enzyme is not active for N-acyl-D-glucosamine
-
-
?
additional information
?
-
enzyme CsCE not only has the ability to convert lactose into lactulose, but can also epimerise lactose into epilactose. A Na2HPO4-NaH2PO4 buffer system results in the highest lactulose conversion yield and the lowest epilactose production
-
-
?
additional information
?
-
the concentration of lactulose catalyzed by mutant G4-C5 rapidly increases from 0 min to 90 min and then increased gradually to the steady-state level with a yield of lactulose up to approximately 76%. No obvious epilactose is detected at any time intervals with mutant G4-C5 (R5M/I52V/A12S/K328I/F231L)
-
-
?
additional information
?
-
-
the concentration of lactulose catalyzed by mutant G4-C5 rapidly increases from 0 min to 90 min and then increased gradually to the steady-state level with a yield of lactulose up to approximately 76%. No obvious epilactose is detected at any time intervals with mutant G4-C5 (R5M/I52V/A12S/K328I/F231L)
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
enzyme CsCE not only has the ability to convert lactose into lactulose, but can also epimerise lactose into epilactose. A Na2HPO4-NaH2PO4 buffer system results in the highest lactulose conversion yield and the lowest epilactose production
-
-
?
additional information
?
-
-
epiA has been assigned to encode an epimerase for converting D-mannose to D-glucose, even though the amino acid sequence of EpiA is similar to that of cellobiose 2-epimerases (CEs). Recombinant EpiA catalyzes the epimerization of the 2-OH group of sugar residue at the reducing end of cellobiose, lactose, and beta-(1->4)-mannobiose in a similar manner to other CEs. The reaction efficiency of EpiA for beta-(1->4)-mannobiose is 55000fold higher than it is for D-mannose. Recombinant EpiA does not act on any of the other disaccharides tested, i.e. maltose, isomaltose, sophorose, laminaribiose, gentiobiose, and beta-(1->4)-xylobiose. Recombinant EpiA shows a significant preference for disaccharides over D-mannose. EpiA has high epimerization activity to beta-(1->4)-linked disaccharides, and beta-(1->4)-mannobiose is the best substrate among beta-(1->4)-linked disaccharides
-
-
?
additional information
?
-
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
-
epiA has been assigned to encode an epimerase for converting D-mannose to D-glucose, even though the amino acid sequence of EpiA is similar to that of cellobiose 2-epimerases (CEs). Recombinant EpiA catalyzes the epimerization of the 2-OH group of sugar residue at the reducing end of cellobiose, lactose, and beta-(1->4)-mannobiose in a similar manner to other CEs. The reaction efficiency of EpiA for beta-(1->4)-mannobiose is 55000fold higher than it is for D-mannose. Recombinant EpiA does not act on any of the other disaccharides tested, i.e. maltose, isomaltose, sophorose, laminaribiose, gentiobiose, and beta-(1->4)-xylobiose. Recombinant EpiA shows a significant preference for disaccharides over D-mannose. EpiA has high epimerization activity to beta-(1->4)-linked disaccharides, and beta-(1->4)-mannobiose is the best substrate among beta-(1->4)-linked disaccharides
-
-
?
additional information
?
-
-
the enzyme catalyzes not only epimerization but also isomerization for beta-1,4- and alpha-1,4-gluco-oligosaccharides. No activity with trehalose, sophorose, laminaribiose, gentiobiose, or xylobiose
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
-
the enzyme catalyzes not only epimerization but also isomerization for beta-1,4- and alpha-1,4-gluco-oligosaccharides. No activity with trehalose, sophorose, laminaribiose, gentiobiose, or xylobiose
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme is capable of converting lactose to prebiotic epilactose not only in buffer but also in a complex milk system. No side products are detected other than epilactose
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme is capable of converting lactose to prebiotic epilactose not only in buffer but also in a complex milk system. No side products are detected other than epilactose
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme is capable of converting lactose to prebiotic epilactose not only in buffer but also in a complex milk system. No side products are detected other than epilactose
-
-
?
additional information
?
-
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
the enzyme is capable of converting lactose to prebiotic epilactose not only in buffer but also in a complex milk system. No side products are detected other than epilactose
-
-
?
additional information
?
-
cellobiose 2-epimerase reversibly converts alpha-glucose residue to alpha-mannose residue at the reducing end of beta-1,4-linked oligosaccharides
-
-
?
additional information
?
-
-
cellobiose 2-epimerase reversibly converts alpha-glucose residue to alpha-mannose residue at the reducing end of beta-1,4-linked oligosaccharides
-
-
?
additional information
?
-
cellobiose 2-epimerase reversibly converts D-glucose residues into D-mannose residues at the reducing end of unmodified beta-1,4-linked oligosaccharides, including beta-1,4-mannobiose, cellobiose, and lactose
-
-
?
additional information
?
-
-
cellobiose 2-epimerase reversibly converts D-glucose residues into D-mannose residues at the reducing end of unmodified beta-1,4-linked oligosaccharides, including beta-1,4-mannobiose, cellobiose, and lactose
-
-
?
additional information
?
-
substrate specificity, overview. No activity with glucose, galactose, mannose, sophorose, laminaribiose, gentiobiose, maltose. Cellobiose 2-epimerase efficiently produces epilactose carrying prebiotic properties from lactose. The enzyme shows preference for lactose compared to cellobiose
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with glucose, galactose, mannose, sophorose, laminaribiose, gentiobiose, maltose. Cellobiose 2-epimerase efficiently produces epilactose carrying prebiotic properties from lactose. The enzyme shows preference for lactose compared to cellobiose
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
cellobiose 2-epimerase reversibly converts alpha-glucose residue to alpha-mannose residue at the reducing end of beta-1,4-linked oligosaccharides
-
-
?
additional information
?
-
-
cellobiose 2-epimerase reversibly converts alpha-glucose residue to alpha-mannose residue at the reducing end of beta-1,4-linked oligosaccharides
-
-
?
additional information
?
-
substrate specificity, overview. No activity with glucose, galactose, mannose, sophorose, laminaribiose, gentiobiose, maltose. Cellobiose 2-epimerase efficiently produces epilactose carrying prebiotic properties from lactose. The enzyme shows preference for lactose compared to cellobiose
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with glucose, galactose, mannose, sophorose, laminaribiose, gentiobiose, maltose. Cellobiose 2-epimerase efficiently produces epilactose carrying prebiotic properties from lactose. The enzyme shows preference for lactose compared to cellobiose
-
-
?
additional information
?
-
-
no substrates: N-acetyl-D-glucosamine, uridine 5'-diphosphate-glucose, D-glucose 6-phosphate, maltose, sophorose, laminaribiose, and gentiobiose
-
-
?
additional information
?
-
-
cellobiose 2-epimerase catalyzes interconversion between D-glucose and D-mannose residues at the reducing end of beta-1,4-linked oligosaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Cellobiose isomerase is the sole enzyme catalyzing the epimerization of oligosaccharides among known carbohydrate isomerases/epimerases. The enzyme also has epimerization activity toward cellotriose, cellotetraose, lactose, and beta-(1->4)-mannobiose (Manbeta1->4Man). beta-D-Glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-D-mannose, beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-D-mannose, epilactose [beta-D-galactopyranosyl-(1->4)-D-mannose], and beta-D-mannopyranosyl-(1->4)-D-glucose (Manbeta1->4Glc) are generated from cellotriose, cellotetraose, lactose, and Manbeta1->4Man, respectively. In the reactions with lactose and cellobiose, the conversion levels of epilactose and Glcbeta1->4Man are both approximately 30%. Among beta-(1->4)-linked disaccharides, Manbeta1->4Man is the best substrate for RaCE in terms of catalytic efficiency. No epimerization activity of RaCE is detectable toward monosaccharides (N-acetyl-D-glucosamine, uridine 5'-diphosphate-D-glucose, D-glucose 6-phosphate, D-glucose, and D-mannose) or glucobioses linked other than by a beta-(1->4)-linkage [e.g. maltose: alpha-(1->4)-linkage, sophorose: beta-(1->2)-linkage, laminaribiose: beta-(1->3)-linkage, or gentiobiose: beta-(1->6)-linkage]. Thus enzyme RaCE is highly specific to a beta-(1->4)-linkage at the reducing end of substrates, but can catalyze the conversion of substrates with a D-glucosyl, D-mannosyl, or D-galactosyl residue next to the reducing end sugar residue
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme exhibits a higher epimerization activity for mannose or the mannose moiety at the reducing end of beta- and alpha-1,4-glycosylmannose than for glucose or the glucose moiety of beta- and alpha-1,4-glycosyl-glucose
-
-
?
additional information
?
-
-
the enzyme exhibits a higher epimerization activity for mannose or the mannose moiety at the reducing end of beta- and alpha-1,4-glycosylmannose than for glucose or the glucose moiety of beta- and alpha-1,4-glycosyl-glucose
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme exhibits a higher epimerization activity for mannose or the mannose moiety at the reducing end of beta- and alpha-1,4-glycosylmannose than for glucose or the glucose moiety of beta- and alpha-1,4-glycosyl-glucose
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
additional information
?
-
no activity with N-acyl-D-glucosamine and D-glucose
-
-
?
additional information
?
-
no activity with N-acyl-D-glucosamine and D-glucose
-
-
?
additional information
?
-
substrate specificitiy of mD1 toward beta-linked disaccharides, overview. The enzyme is active on mannobiose (beta-1,4), cellobiose (beta-1,4), lactose (beta-1,4), and epilactose (beta-1,4), but not on laminaribiose (beta-1,3), gentiobiose (beta-1,6), and xylobiose (beta-1,4). No epimerization activity toward monosaccharides such as mannose, glucose, xylose, galactose, fructose, and GlcNAc and alpha-linked disaccharides such as trehalose (alpha-1,1), kojibiose (alpha-1,2), nigerose (alpha-1,3), maltose (alpha-1,4), sucrose (alpha-1,4), and melibiose (alpha-1,6). Enzyme mD1 favors mannobiose over cellobiose for catalysis
-
-
?
additional information
?
-
substrate specificitiy of mD1 toward beta-linked disaccharides, overview. The enzyme is active on mannobiose (beta-1,4), cellobiose (beta-1,4), lactose (beta-1,4), and epilactose (beta-1,4), but not on laminaribiose (beta-1,3), gentiobiose (beta-1,6), and xylobiose (beta-1,4). No epimerization activity toward monosaccharides such as mannose, glucose, xylose, galactose, fructose, and GlcNAc and alpha-linked disaccharides such as trehalose (alpha-1,1), kojibiose (alpha-1,2), nigerose (alpha-1,3), maltose (alpha-1,4), sucrose (alpha-1,4), and melibiose (alpha-1,6). Enzyme mD1 favors mannobiose over cellobiose for catalysis
-
-
?
additional information
?
-
substrate specificitiy of mD1 toward beta-linked disaccharides, overview. The enzyme is active on mannobiose (beta-1,4), cellobiose (beta-1,4), lactose (beta-1,4), and epilactose (beta-1,4), but not on laminaribiose (beta-1,3), gentiobiose (beta-1,6), and xylobiose (beta-1,4). No epimerization activity toward monosaccharides such as mannose, glucose, xylose, galactose, fructose, and GlcNAc and alpha-linked disaccharides such as trehalose (alpha-1,1), kojibiose (alpha-1,2), nigerose (alpha-1,3), maltose (alpha-1,4), sucrose (alpha-1,4), and melibiose (alpha-1,6). Enzyme mD2 favors mannobiose over cellobiose for catalysis
-
-
?
additional information
?
-
substrate specificitiy of mD1 toward beta-linked disaccharides, overview. The enzyme is active on mannobiose (beta-1,4), cellobiose (beta-1,4), lactose (beta-1,4), and epilactose (beta-1,4), but not on laminaribiose (beta-1,3), gentiobiose (beta-1,6), and xylobiose (beta-1,4). No epimerization activity toward monosaccharides such as mannose, glucose, xylose, galactose, fructose, and GlcNAc and alpha-linked disaccharides such as trehalose (alpha-1,1), kojibiose (alpha-1,2), nigerose (alpha-1,3), maltose (alpha-1,4), sucrose (alpha-1,4), and melibiose (alpha-1,6). Enzyme mD2 favors mannobiose over cellobiose for catalysis
-
-
?
additional information
?
-
no substrates: N-acetyl-D-glucosamine, UDP-glucose, D-glucose 6-phosphate, glucose, mannose, galactose, fructose, xylose, arabinose, sophorose, laminaribiose, and gentiobiose
-
-
?
additional information
?
-
-
no substrates: N-acetyl-D-glucosamine, UDP-glucose, D-glucose 6-phosphate, glucose, mannose, galactose, fructose, xylose, arabinose, sophorose, laminaribiose, and gentiobiose
-
-
?
additional information
?
-
the enzyme catalyzes the epimerization of a D-glucose residue at the reducing end of cellobiose to a D-mannose residue, i.e. cellobiose is converted to beta-D-glucopyranosyl-(1->4)-D-mannose. Enzyme cellobiose 2-epimerase, CE, is highly specific for disaccharides
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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3.5 - 8.74
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
70.9
D-glucose
-
in 50 mM PIPES buffer (pH 7.5), at 75°C
additional information
additional information
-
3.5
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
4.03
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
-
pH 7.5, 30°C, recombinant enzyme
4.03
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
-
pH 8.0, 40°C, recombinant enzyme
5.25
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
5.51
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
8.74
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
3.7 - 5
cellobiose
pH 7.5, 30°C, recombinant enzyme
3.7 - 5
cellobiose
recombinant enzyme, 100 mM sodium phosphate, 20 mM cellobiose, pH 7.5, 30°C
3.92
cellobiose
recombinant enzyme, pH 7.5, 25°C
4.3
cellobiose
pH 7.5, 30°C, recombinant enzyme
4.3
cellobiose
pH 7.0, 60°C
10.8
cellobiose
recombinant enzyme, pH 7.5, 30°C
11.3
cellobiose
pH 7.5, 35°C
11.3
cellobiose
pH 7.5, 30°C, recombinant enzyme
13.8
cellobiose
-
pH 7.5, 30°C
13.8
cellobiose
pH 7.5, 30°C, recombinant enzyme
13.8
cellobiose
recombinant enzyme, 100 mM sodium phosphate, 20 mM cellobiose, pH 7.5, 30°C
13.8
cellobiose
wild type enzyme, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
18
cellobiose
M270T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
20
cellobiose
M212T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
22.6
cellobiose
pH 7.5, 30°C, recombinant enzyme
24.5
cellobiose
-
pH 7.5, 30°C, recombinant enzyme
24.5
cellobiose
-
pH 8.0, 40°C, recombinant enzyme
27.2
cellobiose
pH 7.5, 30°C, recombinant enzyme
27.2
cellobiose
pH 6.3, 60°C, recombinnat enzyme
28.2
cellobiose
pH 7.5, 30°C, recombinant enzyme
29.6
cellobiose
pH 7.5, 30°C, recombinant enzyme
34
cellobiose
M380T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
37
cellobiose
R377A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
53.2
cellobiose
pH 7.5, 30°C, recombinant enzyme
54
cellobiose
M62T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
56
cellobiose
F114A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
56
cellobiose
M95T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
75.8
cellobiose
pH 7.5, 30°C, recombinant enzyme
75.8
cellobiose
-
purified recombinant His-tagged enzyme, pH 7.0, 70°C
84
cellobiose
M378T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
104
cellobiose
pH 7.5, 30°C, recombinant enzyme
108
cellobiose
W303F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
121
cellobiose
M96T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
127
cellobiose
W55F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
128
cellobiose
M106T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
146
cellobiose
M179T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
164.5
cellobiose
recombinant His6-tagged enzyme, pH 7.5, 70°C
179
cellobiose
pH 7.5, 30°C, recombinant enzyme
198
cellobiose
pH 7.5, 30°C, recombinant enzyme
241.1
cellobiose
recombinant enzyme, pH 7.0, 60°C
51.8
D-mannose
-
in 50 mM PIPES buffer (pH 7.5), at 75°C
245
D-mannose
-
pH 8.0, 40°C, recombinant enzyme
276
epilactose
pH 7.5, 50°C
276
epilactose
pH 7.5, 50°C, recombinant enzyme
381
epilactose
pH 7.5, 50°C
381
epilactose
pH 7.5, 50°C, recombinant enzyme
6.56
lactose
pH 7.5, 30°C, recombinant enzyme
6.56
lactose
recombinant enzyme, 100 mM sodium phosphate, 20 mM lactose, pH 7.5, 30°C
24.5
lactose
pH 7.5, 30°C, recombinant enzyme
28.7
lactose
-
pH 7.5, 30°C, recombinant enzyme
28.7
lactose
-
pH 8.0, 40°C, recombinant enzyme
28.8
lactose
pH 7.5, 30°C, recombinant enzyme
28.8
lactose
pH 6.3, 60°C, recombinnat enzyme
29.2
lactose
pH 7.5, 30°C, recombinant enzyme
33
lactose
-
pH 7.5, 30°C
33
lactose
pH 7.5, 30°C, recombinant enzyme
33
lactose
recombinant enzyme, 100 mM sodium phosphate, 20 mM lactose, pH 7.5, 30°C
33
lactose
wild type, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
34.9
lactose
pH 7.5, 30°C, recombinant enzyme
51.9
lactose
pH 7.5, 30°C, recombinant enzyme
72
lactose
pH 7.5, 30°C, recombinant enzyme
72
lactose
W55F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
73
lactose
R377A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
79.6
lactose
pH 7.5, 30°C, recombinant enzyme
79.6
lactose
-
purified recombinant His-tagged enzyme, pH 7.0, 70°C
95
lactose
F114A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
95.7
lactose
pH 7.5, 30°C, recombinant enzyme
124.7
lactose
recombinant enzyme, pH 7.0, 60°C
145
lactose
W303F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
206
lactose
pH 7.5, 30°C, recombinant enzyme
238
lactose
pH 7.5, 30°C, recombinant enzyme
301.7
lactose
recombinant His6-tagged enzyme, pH 7.5, 70°C
358.24
lactose
pH 7.5, 80°C, mutant enzyme R5M/A12S/I52V/F231L/K328I
358.24
lactose
pH 7.5, 80°C, recombinant mutant R5M/A12S/I52V/F231L/K328I
402.12
lactose
pH 7.5, 80°C, mutant enzyme R5M/A12S/F231L/K328I
402.12
lactose
pH 7.5, 80°C, recombinant mutant R5M/A12S/F231L/K328I
417.9
lactose
pH 7.5, 80°C, mutant enzyme E161D/N365P
417.9
lactose
recombinant mutant E161D/N365P, pH 7.5, 80°C
462
lactose
pH 7.5, 50°C, recombinant enzyme
475.43
lactose
pH 7.5, 80°C, mutant enzyme A12S/K328I
475.43
lactose
pH 7.5, 80°C, recombinant mutant A12S/K328I
537.12
lactose
pH 7.5, 80°C, mutant enzyme A12S
537.12
lactose
pH 7.5, 80°C, recombinant mutant A12S
553
lactose
pH 7.5, 50°C, recombinant enzyme
581.37
lactose
pH 7.5, 80°C, wild-type enzyme
581.37
lactose
recombinant wild-type enzyme, pH 7.5, 80°C
613.54
lactose
pH 7.5, 80°C, wild-type enzyme
613.54
lactose
pH 7.5, 80°C, recombinant wild-type enzyme
932.78
lactose
pH 7.5, 80°C, mutant enzyme E161D/S180P/S351G
932.78
lactose
recombinant mutant E161D/S180P/S351G, pH 7.5, 80°C
257
lactulose
pH 7.5, 50°C
257
lactulose
pH 7.5, 50°C, recombinant enzyme
339
lactulose
pH 7.5, 50°C
339
lactulose
pH 7.5, 50°C, recombinant enzyme
3.5
mannobiose
pH 7.0, 60°C
21.8
mannobiose
recombinant enzyme, pH 7.5, 30°C
25.1
mannobiose
recombinant enzyme, pH 7.5, 25°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
35.8 - 201
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
0.27
D-glucose
-
in 50 mM PIPES buffer (pH 7.5), at 75°C
35.8
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
102
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
102
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
-
pH 7.5, 30°C, recombinant enzyme
102
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
-
pH 8.0, 40°C, recombinant enzyme
104
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
201
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
2 - 8
cellobiose
pH 7.5, 30°C, recombinant enzyme
2 - 8
cellobiose
pH 7.0, 60°C
4.64
cellobiose
F114A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
5.16
cellobiose
M378T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
7.02
cellobiose
pH 7.5, 30°C, recombinant enzyme
14.4
cellobiose
M270T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
18.7
cellobiose
pH 7.5, 30°C, recombinant enzyme
26.1
cellobiose
pH 7.5, 30°C, recombinant enzyme
26.6
cellobiose
R377A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
28.5
cellobiose
pH 7.5, 30°C, recombinant enzyme
29.7
cellobiose
M106T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
30.3
cellobiose
M62T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
31.5
cellobiose
M212T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
32.5
cellobiose
pH 7.5, 35°C
33.3
cellobiose
M95T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
36.9
cellobiose
M179T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
38.8
cellobiose
-
pH 7.5, 30°C, recombinant enzyme
38.8
cellobiose
-
pH 8.0, 40°C, recombinant enzyme
39.9
cellobiose
pH 7.5, 30°C, recombinant enzyme
40
cellobiose
M380T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
43.8
cellobiose
M96T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
46.4
cellobiose
W303F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
63.3
cellobiose
wild type enzyme, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
63.8
cellobiose
-
pH 7.5, 30°C
63.8
cellobiose
pH 7.5, 30°C, recombinant enzyme
63.8
cellobiose
recombinant enzyme, 100 mM sodium phosphate, 20 mM cellobiose, pH 7.5, 30°C
67.6
cellobiose
pH 7.5, 30°C, recombinant enzyme
67.6
cellobiose
recombinant enzyme, 100 mM sodium phosphate, 20 mM cellobiose, pH 7.5, 30°C
80.8
cellobiose
pH 7.5, 30°C, recombinant enzyme
80.8
cellobiose
pH 6.3, 60°C, recombinnat enzyme
100.4
cellobiose
recombinant enzyme, pH 7.0, 60°C
109
cellobiose
recombinant enzyme, pH 7.5, 30°C
165
cellobiose
pH 7.5, 30°C, recombinant enzyme
166
cellobiose
recombinant enzyme, pH 7.5, 25°C
169
cellobiose
pH 7.5, 30°C, recombinant enzyme
169.1
cellobiose
-
purified recombinant His-tagged enzyme, pH 7.0, 70°C
215
cellobiose
W55F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
222
cellobiose
pH 7.5, 30°C, recombinant enzyme
233.7
cellobiose
recombinant His6-tagged enzyme, pH 7.5, 70°C
240
cellobiose
pH 7.5, 30°C, recombinant enzyme
0.113
D-mannose
-
pH 8.0, 40°C, recombinant enzyme
0.74
D-mannose
-
in 50 mM PIPES buffer (pH 7.5), at 75°C
101
epilactose
pH 7.5, 50°C
101
epilactose
pH 7.5, 50°C, recombinant enzyme
125
epilactose
pH 7.5, 50°C
125
epilactose
pH 7.5, 50°C, recombinant enzyme
1.79
lactose
F114A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
4.04
lactose
W303F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
5.43
lactose
pH 7.5, 30°C, recombinant enzyme
7.82
lactose
pH 7.5, 30°C, recombinant enzyme
14
lactose
pH 7.5, 30°C, recombinant enzyme
17.5
lactose
pH 7.5, 30°C, recombinant enzyme
18.6
lactose
-
pH 7.5, 30°C, recombinant enzyme
18.6
lactose
-
pH 8.0, 40°C, recombinant enzyme
20.9
lactose
R377A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
28.5
lactose
pH 7.5, 35°C
30.9
lactose
recombinant enzyme, pH 7.0, 60°C
32.5
lactose
pH 7.5, 30°C, recombinant enzyme
43.26
lactose
pH 7.5, 80°C, recombinant wild-type enzyme
43.26
lactose
pH 7.5, 80°C, wild-type enzyme
44.9
lactose
pH 7.5, 30°C, recombinant enzyme
47.5
lactose
pH 7.5, 80°C, mutant enzyme A12S
47.5
lactose
pH 7.5, 80°C, recombinant mutant A12S
51.77
lactose
pH 7.5, 80°C, mutant enzyme A12S/K328I
51.77
lactose
pH 7.5, 80°C, recombinant mutant A12S/K328I
52.1
lactose
-
pH 7.5, 30°C
52.1
lactose
pH 7.5, 30°C, recombinant enzyme
52.1
lactose
recombinant enzyme, 100 mM sodium phosphate, 20 mM lactose, pH 7.5, 30°C
52.1
lactose
wild type, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
55.83
lactose
pH 7.5, 80°C, mutant enzyme R5M/A12S/F231L/K328I
55.83
lactose
pH 7.5, 80°C, recombinant mutant R5M/A12S/F231L/K328I
72.44
lactose
pH 7.5, 80°C, mutant enzyme E161D/S180P/S351G
72.44
lactose
recombinant mutant E161D/S180P/S351G, pH 7.5, 80°C
75.27
lactose
pH 7.5, 80°C, mutant enzyme R5M/A12S/I52V/F231L/K328I
75.27
lactose
pH 7.5, 80°C, recombinant mutant R5M/A12S/I52V/F231L/K328I
75.57
lactose
pH 7.5, 80°C, mutant enzyme E161D/N365P
75.57
lactose
recombinant mutant E161D/N365P, pH 7.5, 80°C
78.3
lactose
W55F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
79.5
lactose
pH 7.5, 30°C, recombinant enzyme
79.5
lactose
recombinant enzyme, 100 mM sodium phosphate, 20 mM lactose, pH 7.5, 30°C
81.55
lactose
pH 7.5, 80°C, wild-type enzyme
81.55
lactose
recombinant wild-type enzyme, pH 7.5, 80°C
89.4
lactose
pH 7.5, 30°C, recombinant enzyme
89.4
lactose
-
purified recombinant His-tagged enzyme, pH 7.0, 70°C
92.1
lactose
pH 7.5, 30°C, recombinant enzyme
111
lactose
pH 7.5, 30°C, recombinant enzyme
111
lactose
pH 6.3, 60°C, recombinnat enzyme
175
lactose
pH 7.5, 30°C, recombinant enzyme
233.4
lactose
recombinant His6-tagged enzyme, pH 7.5, 70°C
237
lactose
pH 7.5, 50°C, recombinant enzyme
303
lactose
pH 7.5, 50°C, recombinant enzyme
0.54
lactulose
pH 7.5, 50°C
0.54
lactulose
pH 7.5, 50°C, recombinant enzyme
0.88
lactulose
pH 7.5, 50°C
0.88
lactulose
pH 7.5, 50°C, recombinant enzyme
35.7
mannobiose
pH 7.0, 60°C
113
mannobiose
recombinant enzyme, pH 7.5, 25°C
137
mannobiose
recombinant enzyme, pH 7.5, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10.2 - 25.3
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
0.0038
D-glucose
-
in 50 mM PIPES buffer (pH 7.5), at 75°C
0.000461 - 0.0143
D-mannose
0.0016 - 0.0034
lactulose
10.2
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
18.9
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
19.4
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
23
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
pH 7.5, 30°C, recombinant enzyme
25.3
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
-
pH 7.5, 30°C, recombinant enzyme
25.3
4-O-beta-D-mannopyranosyl-beta-D-mannopyranose
-
pH 8.0, 40°C, recombinant enzyme
0.037
cellobiose
-
purified recombinant His-tagged enzyme, pH 7.0, 70°C
0.06
cellobiose
M378T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
0.08
cellobiose
F114A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
0.23
cellobiose
M106T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
0.237
cellobiose
pH 7.5, 30°C, recombinant enzyme
0.25
cellobiose
M179T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
0.37
cellobiose
M96T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
0.417
cellobiose
recombinant enzyme, pH 7.0, 60°C
0.43
cellobiose
W303F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
0.58
cellobiose
M62T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
0.61
cellobiose
M95T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
0.663
cellobiose
pH 7.5, 30°C, recombinant enzyme
0.72
cellobiose
R377A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
0.75
cellobiose
pH 7.5, 30°C, recombinant enzyme
0.8
cellobiose
M270T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
0.833
cellobiose
pH 7.5, 30°C, recombinant enzyme
1.15
cellobiose
pH 7.5, 30°C, recombinant enzyme
1.17
cellobiose
M380T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
1.34
cellobiose
pH 7.5, 30°C, recombinant enzyme
1.421
cellobiose
recombinant His6-tagged enzyme, pH 7.5, 70°C
1.57
cellobiose
M212T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
1.58
cellobiose
-
pH 7.5, 30°C, recombinant enzyme
1.58
cellobiose
-
pH 8.0, 40°C, recombinant enzyme
1.69
cellobiose
W55F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
2.13
cellobiose
pH 7.5, 30°C, recombinant enzyme
2.23
cellobiose
pH 7.5, 30°C, recombinant enzyme
2.52
cellobiose
pH 7.5, 30°C, recombinant enzyme
2.97
cellobiose
pH 7.5, 30°C, recombinant enzyme
2.97
cellobiose
pH 6.3, 60°C, recombinnat enzyme
4.62
cellobiose
recombinant enzyme, 100 mM sodium phosphate, 20 mM cellobiose, pH 7.5, 30°C
4.62
cellobiose
wild type enzyme, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C
4.62
cellobiose
pH 7.5, 30°C, recombinant enzyme
6.5
cellobiose
pH 7.0, 60°C
6.51
cellobiose
pH 7.5, 30°C, recombinant enzyme
11
cellobiose
recombinant enzyme, pH 7.5, 30°C
18
cellobiose
pH 7.5, 30°C, recombinant enzyme
18.1
cellobiose
recombinant enzyme, 100 mM sodium phosphate, 20 mM cellobiose, pH 7.5, 30°C
42.8
cellobiose
recombinant enzyme, pH 7.5, 25°C
0.000461
D-mannose
-
pH 8.0, 40°C, recombinant enzyme
0.0143
D-mannose
-
in 50 mM PIPES buffer (pH 7.5), at 75°C
0.33
epilactose
pH 7.5, 50°C
0.33
epilactose
pH 7.5, 50°C, recombinant enzyme
0.37
epilactose
pH 7.5, 50°C
0.37
epilactose
pH 7.5, 50°C, recombinant enzyme
0.019
lactose
F114A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
0.019
lactose
-
purified recombinant His-tagged enzyme, pH 7.0, 70°C
0.028
lactose
W303F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
0.0705
lactose
pH 7.5, 80°C, wild-type enzyme
0.0705
lactose
pH 7.5, 80°C, recombinant wild-type enzyme
0.078
lactose
pH 7.5, 80°C, mutant enzyme E161D/S180P/S351G
0.078
lactose
recombinant mutant E161D/S180P/S351G, pH 7.5, 80°C
0.0884
lactose
pH 7.5, 80°C, mutant enzyme A12S
0.0884
lactose
pH 7.5, 80°C, recombinant mutant A12S
0.1089
lactose
pH 7.5, 80°C, recombinant mutant A12S/K328I
0.109
lactose
pH 7.5, 80°C, mutant enzyme A12S/K328I
0.1389
lactose
pH 7.5, 80°C, recombinant mutant R5M/A12S/F231L/K328I
0.139
lactose
pH 7.5, 80°C, mutant enzyme R5M/A12S/F231L/K328I
0.14
lactose
pH 7.5, 80°C, wild-type enzyme
0.14
lactose
recombinant wild-type enzyme, pH 7.5, 80°C
0.181
lactose
pH 7.5, 80°C, mutant enzyme E161D/N365P
0.181
lactose
recombinant mutant E161D/N365P, pH 7.5, 80°C
0.21
lactose
pH 7.5, 80°C, mutant enzyme R5M/A12S/I52V/F231L/K328I
0.2101
lactose
pH 7.5, 80°C, recombinant mutant R5M/A12S/I52V/F231L/K328I
0.222
lactose
pH 7.5, 30°C, recombinant enzyme
0.248
lactose
recombinant enzyme, pH 7.0, 60°C
0.268
lactose
pH 7.5, 30°C, recombinant enzyme
0.27
lactose
pH 7.5, 30°C, recombinant enzyme
0.285
lactose
R377A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
0.447
lactose
pH 7.5, 30°C, recombinant enzyme
0.451
lactose
pH 7.5, 30°C, recombinant enzyme
0.469
lactose
pH 7.5, 30°C, recombinant enzyme
0.501
lactose
pH 7.5, 30°C, recombinant enzyme
0.51
lactose
pH 7.5, 50°C
0.51
lactose
pH 7.5, 50°C, recombinant enzyme
0.55
lactose
pH 7.5, 50°C
0.55
lactose
pH 7.5, 50°C, recombinant enzyme
0.648
lactose
-
pH 7.5, 30°C, recombinant enzyme
0.648
lactose
-
pH 8.0, 40°C, recombinant enzyme
0.735
lactose
pH 7.5, 30°C, recombinant enzyme
0.773
lactose
recombinant His6-tagged enzyme, pH 7.5, 70°C
1.08
lactose
W55F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
1.12
lactose
pH 7.5, 30°C, recombinant enzyme
1.58
lactose
recombinant enzyme, 100 mM sodium phosphate, 20 mM lactose, pH 7.5, 30°C
1.58
lactose
wild type, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C
1.58
lactose
pH 7.5, 30°C, recombinant enzyme
3.85
lactose
pH 7.5, 30°C, recombinant enzyme
3.85
lactose
pH 6.3, 60°C, recombinnat enzyme
12.1
lactose
recombinant enzyme, 100 mM sodium phosphate, 20 mM lactose, pH 7.5, 30°C
12.1
lactose
pH 7.5, 30°C, recombinant enzyme
0.0016
lactulose
pH 7.5, 50°C
0.0016
lactulose
pH 7.5, 50°C, recombinant enzyme
0.0034
lactulose
pH 7.5, 50°C
0.0034
lactulose
pH 7.5, 50°C, recombinant enzyme
4.5
mannobiose
recombinant enzyme, pH 7.5, 25°C
6.33
mannobiose
recombinant enzyme, pH 7.5, 30°C
10.2
mannobiose
pH 7.0, 60°C
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0.009
substrate: 4-O-alpha-D-glucopyranosyl-D-mannose, pH 7.0, 60°C
0.0095
-
in 50 mM PIPES buffer (pH 7.5) containing 10 mM D-fructose as substrate at 75°C
0.02
substrate: D-glucose, pH 7.0, 60°C
0.035
-
in 50 mM PIPES buffer (pH 7.5) containing 10 mM D-glucose as substrate at 75°C
0.04
-
in 50 mM PIPES buffer (pH 7.5) containing 10 mM D-xylose as substrate at 75°C
0.05
substrate: D-mannose, pH 7.0, 60°C
0.06
-
in 50 mM PIPES buffer (pH 7.5) containing 10 mM D-lyxose as substrate at 75°C
0.1
substrate: cellotriose, pH 7.0, 60°C
0.15
-
in 50 mM PIPES buffer (pH 7.5) containing 10 mM D-mannose as substrate at 75°C
0.42
substrate: maltotriose, pH 7.0, 60°C
0.44
F114A mutant, kinetic value for cellobiose
0.53
W303F mutant, kinetic value for cellobiose
1.15
F114A mutant, kinetic value for cellobiose
1.4
M378T mutant, kinetic value for cellobiose
10.4
purified recombinant enzyme, pH 7.5, 30°C, substrate lactose
10.9
M62T mutant, kinetic value for cellobiose
12.06
purified recombinant mutant E161D/N365P, pH 7.5, 80°C, substrate lactose
12.1
R377A mutant, kinetic value for cellobiose
12.3
M95T mutant, kinetic value for cellobiose
13.5
substrate lactose, recombinant enzyme, pH 7.0, 60°C
13.68
substrate: lactose, pH 7.5, 80°C, mutant enzyme A12S
14.2
-
purified recombinant His-tagged enzyme, substrate lactose, pH 7.0, 70°C
14.3
substrate: 4-O-beta-D-glucopyranosyl-D-mannose, pH 7.0, 60°C
15.48
substrate cellobiose, recombinant enzyme, pH 7.0, 60°C
15.5
substrate: lactose, pH 7.0, 60°C
16.8 - 24.4
-
purified recombinant His-tagged enzyme, substrate cellolbiose, pH 7.0, 70°C
17.45
substrate: lactose, pH 7.5, 80°C, mutant enzyme A12S/K328I
19.6
substrate: lactose, pH 7.5, 80°C, mutant enzyme R5M/A12S/F231L/K328I
201
purified recombinant enzyme, pH 7.5, 25°C, substrate beta-1,4-mannobiose
21.1
purified recombinant enzyme, pH 7.5, 30°C, substrate epilactose
21.8
substrate: cellobiose, pH 7.0, 60°C
22.7
W55F mutant, kinetic value for cellobiose
25.5
substrate: mannobiose, pH 7.0, 60°C
25.8
M380T mutant, kinetic value for cellobiose
25.85
-
recombinant enzyme activity in vivo, substrate lactose, pH 7.0, 10°C
29.2
substrate: cellobiose, pH 7.0, 60°C
29.8
substrate mannobiose, recombinant enzyme, pH 7.0, 60°C
29.9
crude extract after expression in Escherichia coli cells
3
the specific activity toward cellobiose is 35 micromol/min/mg at a pH optimum 7.8 in 100 mM glycylglycine buffer
3.6
-
in 50 mM PIPES buffer (pH 7.5) containing 10 mM cellobiose as substrate at 75°C
30
purified recombinnat His-tagged enzyme, substrate lactose, pH 7.5, 80°C
30.08
substrate: lactose, pH 7.5, 80°C, mutant enzyme R5M/A12S/I52V/F231L/K328I
311.34
recombinant enzyme activity in vivo, substrate lactose, pH 7.0, 10°C
38.81
recombinant enzyme activity in vivo, substrate lactose, pH 7.0, 10°C
41.9
substrate: mannobiose, pH 7.0, 60°C
42
W55F mutant, kinetic value for cellobiose
46.91
recombinant enzyme activity in vivo, substrate lactose, pH 7.0, 10°C
5.6
M106T mutant, kinetic value for cellobiose
5.99
W303F mutant, kinetic value for cellobiose
58.3
recombinant enzyme after first purification step on a DEAE Sepharose FF column
58.91
recombinant enzyme activity in vivo, substrate lactose, pH 7.0, 10°C
6.35
M212T mutant, kinetic value for cellobiose
6.6
R377A mutant, kinetic value for cellobiose
6.89
purified recombinant mutant E161D/S180P/S351G, pH 7.5, 80°C, substrate lactose
61.8
recombinant enzyme after second purification step on a hydroxyapatite column, substrate is cellobiose
62.3
purified recombinant enzyme, pH 7.5, 25°C, substrate cellobiose
7.7
purified recombinant enzyme, pH 7.5, 25°C, substrate epilactose
7.8
substrate: epilactose, pH 7.0, 60°C
71.6
purified recombinant enzyme, pH 7.5, 30°C, substrate cellobiose
74.39
purified recombinant enzyme, pH 7.5, 50°C, substrate lactose
76.78
recombinant enzyme activity in vivo, substrate lactose, pH 7.0, 10°C
79.7
recombinant enzyme after second purification step on a hydroxyapatite column, substrate is lactose
8.73
M96T mutant, kinetic value for cellobiose
9
M270T mutant, kinetic value for cellobiose
9.06
purified recombinant enzyme, pH 7.5, 25°C, substrate lactose
9.9
substrate: maltose, pH 7.0, 60°C
90.58
purified recombinant enzyme, pH 7.5, 50°C, substrate lactose
93.6
purified recombinant His6-tagged enzyme, substrate lactose, pH 7.5, 70°C
97.5
purified recombinant enzyme, pH 7.5, 30°C, substrate beta-1,4-mannobiose
10.77
purified recombinant wild-type enzyme, pH 7.5, 80°C, substrate lactose
10.77
substrate: lactose, pH 7.5, 80°C, wild-type enzyme
28.4
-
substrate lactose, pH 7.5, 30°C
28.4
recombinant enzyme, substrate is lactose
28.4
wild type enzyme, kinetic value for lactose
51
-
substrate cellobiose, pH 7.5, 30°C
51
recombinant enzyme, substrate is cellobiose
51
wild type enzyme, kinetic value for cellobiose
6.3
M179T mutant, kinetic value for cellobiose
6.3
substrate: mannotriose, pH 7.0, 60°C
additional information
isomerase and epimerase activities of wild-type and mutant enzymes, overview
additional information
-
isomerase and epimerase activities of wild-type and mutant enzymes, overview
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metabolism
the enzyme is responsible for conversion of beta-1,4-mannobiose to 4-O-beta-D-mannosyl-D-glucose in mannan metabolism
evolution
-
structure, active site, and reaction mechanism of cellobiose 2-epimerase are similar to those of N-acyl-D-glucosamine 2-epimerase
evolution
-
the structure of RaCE shows strong similarity to those of N-acetyl-D-glucosamine 2-epimerase and aldose-ketose isomerase YihS with a high degree of conservation of residues around the catalytic center, although sequence identity between them is low
evolution
the cluster of CE and CE-like proteins is functionally and evolutionarily separated from that of N-acetyl-D-glucosamine 2-epimerase (AGE) and AGE-like proteins, phylogenetic analysis
evolution
-
structure, active site, and reaction mechanism of cellobiose 2-epimerase are similar to those of N-acyl-D-glucosamine 2-epimerase
-
physiological function
Caldicellulosiruptor saccharolyticus cellobiose 2-epimerase (CsCE) catalyses the single substrate lactose into lactulose and is a highly efficient enzyme for the enzymatic synthesis of lactulose
physiological function
cellobiose 2-epimerase from the thermophile Caldicellulosiruptor saccharolyticus (CsCE) catalyzes the isomerization of lactose into lactulose, a non-digestible disaccharide widely used in food and pharmaceutical industries
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
physiological function
the enzyme reversibly converts D-glucose residues into D-mannose residues at the reducing end of unmodified beta-1,4-linked oligosaccharides, including beta-1,4-mannobiose, cellobiose, and lactose
physiological function
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
physiological function
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
physiological function
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
physiological function
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
Caldicellulosiruptor saccharolyticus cellobiose 2-epimerase (CsCE) catalyses the single substrate lactose into lactulose and is a highly efficient enzyme for the enzymatic synthesis of lactulose
-
physiological function
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
the enzyme reversibly converts D-glucose residues into D-mannose residues at the reducing end of unmodified beta-1,4-linked oligosaccharides, including beta-1,4-mannobiose, cellobiose, and lactose
-
physiological function
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
physiological function
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
physiological function
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
physiological function
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
physiological function
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
physiological function
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
physiological function
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
physiological function
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
physiological function
-
physiological function of cellobiose 2-epimerase in carbohydrate metabolism, overview
-
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
enzyme structure-function relationship, overview
additional information
-
enzyme structure-function relationship, overview
additional information
determination of residues involved in substrate recognition, overview
additional information
-
determination of residues involved in substrate recognition, overview
additional information
three-dimensional structure and substrate binding structure analysis, residues Tyr114 and Asn184 play an important role in binding epilactose, overview. The active site, with its triple histidine center, is located inside the (alpha/alpha)6 barrel structure of the catalytic domain. Two essential conserved histidine residues, His247 and His377, and a third histidine residue located at the bottom of the substrate binding site are required for catalysis. Y114 and N184 in the catalyt domain are located at the interface of the mannose moiety of epilactose in the enzyme-product complex
additional information
-
three-dimensional structure and substrate binding structure analysis, residues Tyr114 and Asn184 play an important role in binding epilactose, overview. The active site, with its triple histidine center, is located inside the (alpha/alpha)6 barrel structure of the catalytic domain. Two essential conserved histidine residues, His247 and His377, and a third histidine residue located at the bottom of the substrate binding site are required for catalysis. Y114 and N184 in the catalyt domain are located at the interface of the mannose moiety of epilactose in the enzyme-product complex
additional information
three-dimensional structure, structure modeling
additional information
-
enzyme structure-function relationship, overview
-
additional information
-
enzyme structure-function relationship, overview
-
additional information
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
enzyme structure-function relationship, overview
-
additional information
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
three-dimensional structure and substrate binding structure analysis, residues Tyr114 and Asn184 play an important role in binding epilactose, overview. The active site, with its triple histidine center, is located inside the (alpha/alpha)6 barrel structure of the catalytic domain. Two essential conserved histidine residues, His247 and His377, and a third histidine residue located at the bottom of the substrate binding site are required for catalysis. Y114 and N184 in the catalyt domain are located at the interface of the mannose moiety of epilactose in the enzyme-product complex
-
additional information
-
enzyme structure-function relationship, overview
-
additional information
-
enzyme structure-function relationship, overview
-
additional information
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
-
enzyme structure-function relationship, overview
-
additional information
-
enzyme structure-function relationship, overview
-
additional information
-
enzyme structure-function relationship, overview
-
additional information
-
enzyme structure-function relationship, overview
-
additional information
-
enzyme structure-function relationship, overview
-
additional information
-
enzyme structure-function relationship, overview
-
additional information
-
enzyme structure-function relationship, overview
-
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E161D
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
E161D/S180P/S351G/N365P
site-directed mutagenesis, the mutant shows reduced thermostability compared to the wild-type enzyme
E94G
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
E94G/E161D
site-directed mutagenesis, the mutant shows a similar half-life compared to wild-type
N365P
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
R5M/A12S/I52V/F231L/K328I
t1/2 at 80°C increases approximately 18 min compared with that of the wild-type enzyme. The mutant enzyme retains higher activity than the wild-type enzyme at low temperatures. The mutant enzyme shows a broader pH-activity profile than the wild-type enzyme. The yields of lactulose and epilactose catalyzed from lactose by the wild-type enzyme reaches around 57% and 16%, respectively, after 4 h. The concentration of lactulose catalyzed by mutant enzyme R5M/A12S/I52V/F231L/K328I rapidly increases from 0 min to 90 min and then increases gradually to the steady-state level with a yield of lactulose up to approximately 76%. No obvious epilactose is detected at any time
R5M/I52V/A12S/K328I/F231L
random mutagnesis, the mutant shows 2.8 and 3.0fold increases in specific activity and kcat/Km for lactulose production, respectively, without compromising thermostability. The yield of lactulose catalyzed by mutant G4-C5 increases to approximately 76% with no obvious epilactose detected, indicating that mutant G4-C5 is more suitable for lactulose production than the wild-type enzyme
S180P
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
S304G
site-directed mutagenesis, the mutant shows reduced thermostability compared to the wild-type enzyme
S351G
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
S99P
site-directed mutagenesis, the mutant shows highly reduced thermostability compared to the wild-type enzyme
T110G
site-directed mutagenesis, the mutant shows reduced thermostability compared to the wild-type enzyme
Y114A
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114C
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114D
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114E
site-directed mutagenesis, the mutation leads to increased release of a byproduct, lactulose, from lactose at 65°C, while its activity is low at 37°C. The Y114E mutation increases isomerization of lactose, while decreasing the epimerization of lactose
Y114F
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114G
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114H
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114I
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114K
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114L
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114M
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114N
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114P
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114Q
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114R
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114S
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114T
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114V
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114W
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
Y114E
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
site-directed mutagenesis, the mutation leads to increased release of a byproduct, lactulose, from lactose at 65°C, while its activity is low at 37°C. The Y114E mutation increases isomerization of lactose, while decreasing the epimerization of lactose
-
Y114F
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
-
Y114L
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
-
Y114T
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
-
E246A
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
E246Q
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
E308A
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
E308D
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
E308Q
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
F114A
production by site-directed mutagenesis, mutant has a very low specific activity toward cellobiose and lactose, residue protrudes into the active-site cleft in the model core barrel structure
H184A
-
site-directed mutagenesis
H184N
-
site-directed mutagenesis
H243A
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
H243K
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
H243R
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
H374A
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
H374K
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
H374R
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
R377A
production by site-directed mutagenesis, mutant retains 43% of the activity toward cellobiose and 23% activity toward lactose, compaired to the wild type
R377H
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
R52A
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
R52H
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
R52K
production by site-directed mutagenesis, complete loss of activity towards cellobiose and lactose
W249F
mutant completely loses acitivity toward cellobiose and lactose
W303F
11% and 1.9% activity toward cellobiose and lactose, compared to the wild type, contributes to catalysis, residue protrudes into the active-site cleft in the model core barrel structure
W304F
mutant completely loses acitivity toward cellobiose and lactose
W369A
-
site-directed mutagenesis
W55F
mutant is active, the specific activities toward cellobiose and lactose of the mutant retains more than 80% of those of the wild type enzyme although their Km values are increase greatly
A12S
random mutagenesis, the mutant shows increased activity compared to the wild-type
A12S
t1/2 at 80°C increases approximately 20 min compared with that of the wild-type enzyme
A12S/K328I
random mutagenesis, the mutant shows increased activity compared to the wild-type
A12S/K328I
t1/2 at 80°C decreases approximately 8 min compared with that of the wild-type enzyme
E161D/N365P
compared to the wild-type enzyme the mutant enzyme shows approximately 4fold increase in the t1/2 value at 80°C and a 1.3fold increase in catalytic efficiency for lactulose production. Its reaction temperature for maximum activity increases from 80°C to 87.5°C, and half denaturating guanidine-HCl concentration increased from 3.16 M to 3.55 M
E161D/N365P
site-directed mutagenesis, the mutant's half-life is approximately 4fold higher than that of the wild-type enzyme. The reaction temperature for maximum activity increased from 80°C to 87.5°C, and catalytic efficiency (kcat/Km) for lactulose production is increased 29%. The mutant E161D/N365P is more stable against chemical denaturation and shows also a broader pH profile than the wild-type. The most thermostable mutant E161D/N365P displays a 1.12 and 1.32fold increase in isomerization activity and epimerization activity, respectively
E161D/S180P/S351G
compared to the wild-type enzyme the mutant enzyme shows approximately 3.3fold increase in the t1/2 value at 80°C. Catalytic efficiency (kcat/Km) of mutant E161D/S180P/S351G decreases to approximately 56% of the wild type enzyme with a 1.6fold increase in apparent Km value
E161D/S180P/S351G
site-directed mutagenesis, the mutant shows a 3.3fold increase in half-life compared to wild-type, the mutant has both decreased isomerization activity and epimerization activity compared to the wild-type
R5M/A12S/F231L/K328I
random mutagenesis, the mutant shows increased activity compared to the wild-type
R5M/A12S/F231L/K328I
t1/2 at 80°C decreases approximately 24 min compared with that of the wild-type enzyme
additional information
efficient production of lactulose from whey powder, a by-product of cheese industry, by cellobiose 2-epimerase in an enzymatic membrane reactor using the recombinant enzyme, expressed in Bacillus subtilis, with great operational stability, method optimization and evaluation, overview. Optimal pH stability is displayed between pH 7.0 and 8.0. The transformation of whey powder solution into lactulose is conducted by 7.5 U/mg enzyme CsCE at 70°C in 50 mL 50 mM PBS, pH 7.0, with different concentration whey powder (lactose), 58.5% lactose is obtained from whey powder compared to 29.6% by the chemical method
additional information
-
efficient production of lactulose from whey powder, a by-product of cheese industry, by cellobiose 2-epimerase in an enzymatic membrane reactor using the recombinant enzyme, expressed in Bacillus subtilis, with great operational stability, method optimization and evaluation, overview. Optimal pH stability is displayed between pH 7.0 and 8.0. The transformation of whey powder solution into lactulose is conducted by 7.5 U/mg enzyme CsCE at 70°C in 50 mL 50 mM PBS, pH 7.0, with different concentration whey powder (lactose), 58.5% lactose is obtained from whey powder compared to 29.6% by the chemical method
additional information
isolation of an enzyme mutant with 1.3fold increased lactulose production acctivity and increased thermostability (over 75°C) compared to the wild-type. Lactulose production using cells immobilized on calcium-alginate and expressing thermostable cellobiose 2-epimerase, method development and evaluation, overview. The immobilized enzyme shows increased stability and retains 80% activity after 4 reaction cycles
additional information
lactulose production from lactose by recombinant cellobiose 2-epimerase in permeabilised Escherichia coli ethanol-permeabilised cells. The reaction conditions for maximum lactulose production are optimised to be 600 g/l lactose, pH 7.5, 80°C and 12.5 U ml of whole-cell biocatalyst. After incubated at Na2HPO4-NaH2PO4 buffer for 2 h, approximately 390.59 g/l lactulose is obtained with a conversion yield of 65.1%. Method optimization, detailed overview. A Na2HPO4-NaH2PO4 buffer system results in the highest lactulose conversion yield and the lowest epilactose production
additional information
Y114X mutants are found to lose activity entirely, while the parental enzyme and the Y114E mutant enzyme show increased isomerization activity from lactose to lactulose at 65°C. Isomerase and epimerase activities of wild-type and mutant enzymes, overview
additional information
-
Y114X mutants are found to lose activity entirely, while the parental enzyme and the Y114E mutant enzyme show increased isomerization activity from lactose to lactulose at 65°C. Isomerase and epimerase activities of wild-type and mutant enzymes, overview
additional information
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
efficient production of lactulose from whey powder, a by-product of cheese industry, by cellobiose 2-epimerase in an enzymatic membrane reactor using the recombinant enzyme, expressed in Bacillus subtilis, with great operational stability, method optimization and evaluation, overview. Optimal pH stability is displayed between pH 7.0 and 8.0. The transformation of whey powder solution into lactulose is conducted by 7.5 U/mg enzyme CsCE at 70°C in 50 mL 50 mM PBS, pH 7.0, with different concentration whey powder (lactose), 58.5% lactose is obtained from whey powder compared to 29.6% by the chemical method
-
additional information
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
lactulose production from lactose by recombinant cellobiose 2-epimerase in permeabilised Escherichia coli ethanol-permeabilised cells. The reaction conditions for maximum lactulose production are optimised to be 600 g/l lactose, pH 7.5, 80°C and 12.5 U ml of whole-cell biocatalyst. After incubated at Na2HPO4-NaH2PO4 buffer for 2 h, approximately 390.59 g/l lactulose is obtained with a conversion yield of 65.1%. Method optimization, detailed overview. A Na2HPO4-NaH2PO4 buffer system results in the highest lactulose conversion yield and the lowest epilactose production
-
additional information
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
Y114X mutants are found to lose activity entirely, while the parental enzyme and the Y114E mutant enzyme show increased isomerization activity from lactose to lactulose at 65°C. Isomerase and epimerase activities of wild-type and mutant enzymes, overview
-
additional information
enzyme production evaluation for large-sclae production, parameters, overview
additional information
-
enzyme production evaluation for large-sclae production, parameters, overview
-
additional information
enzyme production evaluation for large-sclae production, parameters, overview
additional information
-
enzyme production evaluation for large-sclae production, parameters, overview
-
additional information
enzyme production evaluation for large-sclae production, parameters, overview
additional information
-
enzyme production evaluation for large-sclae production, parameters, overview
-
additional information
enzyme production evaluation for large-sclae production, parameters, overview
additional information
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
-
enzyme production evaluation for large-sclae production, parameters, overview
-
additional information
immobilization of the purified recombinant enzyme on an anion exchange resin and conversion of lactose to epilactose in a chromatographic column, method development and evaluation, overview
additional information
-
immobilization of the purified recombinant enzyme on an anion exchange resin and conversion of lactose to epilactose in a chromatographic column, method development and evaluation, overview
additional information
-
immobilization of the purified recombinant enzyme on an anion exchange resin and conversion of lactose to epilactose in a chromatographic column, method development and evaluation, overview
-
additional information
sequence analysis shows that the gene shares a very low level of homology with N-acetyl-D-glucosamine 2-epimerases (EC 5.1.3.8), but no significant homology to any other epimerases reported to date
additional information
-
sequence analysis shows that the gene shares a very low level of homology with N-acetyl-D-glucosamine 2-epimerases (EC 5.1.3.8), but no significant homology to any other epimerases reported to date
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food industry
the enzyme can be used for production of the probiotic lactulose
food industry
the enzyme is of interest for the dairy industry due to their ability to convert lactose into epilactose and lactulose, rare disaccharides with prebiotic properties
food industry
the enzyme is of interest for the dairy industry due to their ability to convert lactose into epilactose and lactulose, rare disaccharides with prebiotic properties
food industry
the enzyme may introduce an added value for particular dairy products by in situ production of the prebiotic sugar epilactose
food industry
the enzyme may introduce an added value for particular dairy products by in situ production of the prebiotic sugar epilactose
food industry
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
-
the enzyme may introduce an added value for particular dairy products by in situ production of the prebiotic sugar epilactose
-
food industry
-
the enzyme is of interest for the dairy industry due to their ability to convert lactose into epilactose and lactulose, rare disaccharides with prebiotic properties
-
food industry
-
the enzyme may introduce an added value for particular dairy products by in situ production of the prebiotic sugar epilactose
-
nutrition
-
cellobiose 2-epimerase is an attractive enzyme to produce epilactose (4-O-beta-Dgalactosyl-D-mannose) from lactose. Epilactose is a non-digestible oligosaccharide, and enhances proliferation of bifidobacilli and lactobacilli in the human gut
nutrition
cellobiose 2-epimerases can be used for the production of epilactose from milk ultrafiltrate containing lactose
nutrition
cellobiose 2-epimerases can be used for the production of epilactose from milk ultrafiltrate containing lactose
nutrition
the enzyme may introduce an added value for particular dairy products by in situ production of the prebiotic sugar epilactose
nutrition
the enzyme may introduce an added value for particular dairy products by in situ production of the prebiotic sugar epilactose
nutrition
-
cellobiose 2-epimerases can be used for the production of epilactose from milk ultrafiltrate containing lactose
-
nutrition
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
-
the enzyme may introduce an added value for particular dairy products by in situ production of the prebiotic sugar epilactose
-
nutrition
-
cellobiose 2-epimerases can be used for the production of epilactose from milk ultrafiltrate containing lactose
-
nutrition
-
the enzyme may introduce an added value for particular dairy products by in situ production of the prebiotic sugar epilactose
-
pharmacology
synthesis of lactulose, which is used as a pharmaceutical against various illnesses, such as chronic constipation
pharmacology
synthesis of lactulose, which is used as a pharmaceutical against various illnesses, such as chronic constipation
pharmacology
-
synthesis of lactulose, which is used as a pharmaceutical against various illnesses, such as chronic constipation
-
synthesis
cellobiose 2-epimerase from Caldicellulosiruptor saccharolyticus is used in the presence of borate to increase the production of lactulose from lactose, method optimization, incubation at pH 7.5 and 80°C for 3 h, with a conversion yield of 88% and a productivity of 205 g/l/h, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
application of the enzyme for production of functional oligosaccharides, overview
synthesis
-
application of the enzyme for production of functional oligosaccharides, overview
synthesis
industrial application of Caldicellulosiruptor saccharolyticus cellobiose 2-epimerase (CsCE) for lactulose synthesis is limited by low enzyme activity and formation of epilactose as by-product, the mutant G4-C5, i.e. R5M/I52V/A12S/K328I/F231L, shows improved enzyme activity without compromised thermostability. The yield of lactulose catalyzed by mutant G4-C5 increases to approximately 76% with no obvious epilactose detected, indicating that mutant G4-C5 is more suitable for lactulose production than the wild-type enzyme. The mutant does not produc epilactose as side-product from lactose, in contrast to the wild-type enzyme. Although epilactose is also a bifidus factor, formation of epilactose can complicate lactulose purification
synthesis
industrial application of Caldicellulosiruptor saccharolyticus cellobiose 2-epimerase for lactulose synthesis is limited by low enzyme activity and formation of epilactose as by-product. The yield of lactulose catalyzed by mutant R5M/A12S/I52V/F231L/K328I increases to approximately 76% with no epilactose detected, indicating that the mutant is more suitable for lactulose production than the wild-type enzyme
synthesis
most efficient enzyme for the enzymatic synthesis of lactulose. Ethanol-permeabilised Escherichia coli cells containing the enzyme are used as biocatalysts for lactulose production. The reaction conditions for maximum lactulose production are optimised to be 600 g/l lactose, pH 7.5, 80°C and 12.5 U/ml of whole-cell biocatalyst. After incubated at Na2HPO4-NaH2PO4 buffer for 2 h, approximately 390.59 g/l lactulose is obtained with a conversion yield of 65.1%. The lowest production and conversion yield of epilactose are also found in Na2HPO4-NaH2PO4 buffer with a final concentration of 11.7 g/l and a conversion yield less than 2%. The results represent a promising technology to attain high production and conversion yield of lactulose with a high purity on industrial scale
synthesis
synthesis of lactulose, a non-digestible disaccharide widely used in food and pharmaceutical industries. Thermostability enhancement of cellobiose 2-epimerase from Caldicellulosiruptor saccharolyticus by site-directed mutagenesis. Compared to the wild-type enzyme the mutant enzyme E161D/N365P shows approximately 4fold increase in the t1/2 value at 80°C and a 1.3fold increase in catalytic efficiency for lactulose production
synthesis
the enzyme can be used for production of the probiotic lactulose
synthesis
the enzyme from Caldicellulosiruptor saccharolyticus is applied for epilactose and lactulose production in milk at lower temperatures
synthesis
the enzyme mutant Y114E can be used for production of lactulose for the nutritional industry. Using Y114E, isomerization of lactose to lactulose is optimnized, resulting in 86.9 g/l of lactulose and 4.6 g/l of epilactose for 2 h from 200 g/l of lactose
synthesis
the recombinant enzyme shows both epimerisation and isomerisation activities against lactose, making it an alternative promising biocatalyst candidate for lactulose production
synthesis
-
application of the enzyme for production of functional oligosaccharides, overview
-
synthesis
-
application of the enzyme for production of functional oligosaccharides, overview
-
synthesis
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
application of the enzyme for production of functional oligosaccharides, overview
-
synthesis
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
most efficient enzyme for the enzymatic synthesis of lactulose. Ethanol-permeabilised Escherichia coli cells containing the enzyme are used as biocatalysts for lactulose production. The reaction conditions for maximum lactulose production are optimised to be 600 g/l lactose, pH 7.5, 80°C and 12.5 U/ml of whole-cell biocatalyst. After incubated at Na2HPO4-NaH2PO4 buffer for 2 h, approximately 390.59 g/l lactulose is obtained with a conversion yield of 65.1%. The lowest production and conversion yield of epilactose are also found in Na2HPO4-NaH2PO4 buffer with a final concentration of 11.7 g/l and a conversion yield less than 2%. The results represent a promising technology to attain high production and conversion yield of lactulose with a high purity on industrial scale
-
synthesis
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
-
the enzyme mutant Y114E can be used for production of lactulose for the nutritional industry. Using Y114E, isomerization of lactose to lactulose is optimnized, resulting in 86.9 g/l of lactulose and 4.6 g/l of epilactose for 2 h from 200 g/l of lactose
-
synthesis
-
application of the enzyme for production of functional oligosaccharides, overview
-
synthesis
-
application of the enzyme for production of functional oligosaccharides, overview
-
synthesis
Pedobacter heparinus ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3
-
application of the enzyme for production of functional oligosaccharides, overview
-
synthesis
-
application of the enzyme for production of functional oligosaccharides, overview
-
synthesis
-
application of the enzyme for production of functional oligosaccharides, overview
-
synthesis
Caldicellulosiruptor obsidiansis ATCC BAA-2073 / strain OB47
-
the recombinant enzyme shows both epimerisation and isomerisation activities against lactose, making it an alternative promising biocatalyst candidate for lactulose production
-
synthesis
-
application of the enzyme for production of functional oligosaccharides, overview
-
synthesis
-
application of the enzyme for production of functional oligosaccharides, overview
-
synthesis
-
application of the enzyme for production of functional oligosaccharides, overview
-
synthesis
-
application of the enzyme for production of functional oligosaccharides, overview
-
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Amein, M.; Leatherwood, J.M.
Mechanism of cellobiose epimerase
Biochem. Biophys. Res. Commun.
36
223-227
1969
Ruminococcus albus
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Epimerization of disaccharides by enzyme preparations from Ruminococcus albus
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119
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1967
Ruminococcus albus
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Ito, S.; Hamada, S.; Yamaguchi, K.; Umene, S.; Ito, H.; Matsui, H.; Ozawa, T.; Taguchi, H.; Watanabe, J.; Wasaki, J.; Ito, S.
Cloning and sequencing of the cellobiose 2-epimerase gene from an obligatory anaerobe, Ruminococcus albus
Biochem. Biophys. Res. Commun.
360
640-645
2007
Ruminococcus albus (P0DKY4), Ruminococcus albus
brenda
Ito, S.; Taguchi, H.; Hamada, S.; Kawauchi, S.; Ito, H.; Senoura, T.; Watanabe, J.; Nishimukai, M.; Ito, S.; Matsui, H.
Enzymatic properties of cellobiose 2-epimerase from Ruminococcus albus and the synthesis of rare oligosaccharides by the enzyme
Appl. Microbiol. Biotechnol.
79
433-441
2008
Ruminococcus albus
brenda
Taguchi, H.; Senoura, T.; Hamada, S.; Matsui, H.; Kobayashi, Y.; Watanabe, J.; Wasaki, J.; Ito, S.
Cloning and sequencing of the gene for cellobiose 2-epimerase from a ruminal strain of Eubacterium cellulosolvens
FEMS Microbiol. Lett.
287
34-40
2008
[Eubacterium] cellulosolvens (B3XZI5), [Eubacterium] cellulosolvens
brenda
Senoura, T.; Taguchi, H.; Ito, S.; Hamada, S.; Matsui, H.; Fukiya, S.; Yokota, A.; Watanabe, J.; Wasaki, J.; Ito, S.
Identification of the cellobiose 2-epimerase gene in the genome of Bacteroides fragilis NCTC 9343
Biosci. Biotechnol. Biochem.
73
400-406
2009
Ruminococcus albus (P0DKY4), Bacteroides fragilis (Q5LH66), Bacteroides fragilis
brenda
Ito, S.; Hamada, S.; Ito, H.; Matsui, H.; Ozawa, T.; Taguchi, H.; Ito, S.
Site-directed mutagenesis of possible catalytic residues of cellobiose 2-epimerase from Ruminococcus albus
Biotechnol. Lett.
31
1065-1071
2009
Ruminococcus albus (P0DKY4), Ruminococcus albus
brenda
Park, C.S.; Kim, J.E.; Choi, J.G.; Oh, D.K.
Characterization of a recombinant cellobiose 2-epimerase from Caldicellulosiruptor saccharolyticus and its application in the production of mannose from glucose
Appl. Microbiol. Biotechnol.
92
1187-1196
2011
Caldicellulosiruptor saccharolyticus
brenda
Saburi, W.; Yamamoto, T.; Taguchi, H.; Hamada, S.; Matsui, H.
Practical preparation of epilactose produced with cellobiose 2-epimerase from Ruminococcus albus NE1
Biosci. Biotechnol. Biochem.
74
1736-1737
2010
Ruminococcus albus, Ruminococcus albus NE1
brenda
Kim, Y.S.; Oh, D.K.
Lactulose production from lactose as a single substrate by a thermostable cellobiose 2-epimerase from Caldicellulosiruptor saccharolyticus
Biores. Technol.
104
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2012
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Rhodothermus marinus (F8WRK9), Rhodothermus marinus, Rhodothermus marinus JCM 9785 (F8WRK9), Rhodothermus marinus JCM 9785
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Kim, J.E.; Kim, Y.S.; Kang, L.W.; Oh, D.K.
Characterization of a recombinant cellobiose 2-epimerase from Dictyoglomus turgidum that epimerizes and isomerizes beta-1,4- and alpha-1,4-gluco-oligosaccharides
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Dictyoglomus turgidum, Dictyoglomus turgidum DSM 6724
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Ruminococcus albus
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Structural insights into the epimerization of beta-1,4-linked oligosaccharides catalyzed by cellobiose 2-epimerase, the sole enzyme epimerizing non-anomeric hydroxyl groups of unmodified sugars
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uncultured bacterium (A0A0A1H8D7), uncultured bacterium (A0A0A1HAT7)
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Caldicellulosiruptor saccharolyticus (A4XGA6), Caldicellulosiruptor saccharolyticus, Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331 (A4XGA6)
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Saburi, W.; Tanaka, Y.; Muto, H.; Inoue, S.; Odaka, R.; Nishimoto, M.; Kitaoka, M.; Mori, H.
Functional reassignment of Cellvibrio vulgaris EpiA to cellobiose 2-epimerase and an evaluation of the biochemical functions of the 4-O-beta-D-mannosyl-D-glucose phosphorylase-like protein, UnkA
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Cellulosilyticum lentocellum (F2JR71), Dysgonomonas gadei (F5ITJ6), Cellulosilyticum lentocellum ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5 (F2JR71), Dysgonomonas gadei ATCC BAA-286 (F5ITJ6)
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Thermoanaerobacterium saccharolyticum (I3VXT6), Thermoanaerobacterium saccharolyticum JW/SL-YS485 / DSM 8691 (I3VXT6)
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Shen, Q.; Zhang, Y.; Yang, R.; Hua, X.; Zhang, W.; Zhao, W.
Thermostability enhancement of cellobiose 2-epimerase from Caldicellulosiruptor saccharolyticus by site-directed mutagenesis
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Caldicellulosiruptor saccharolyticus (A4XGA6)
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Kuschel, B.; Claaen, W.; Mu, W.; Jiang, B.; Stressler, T.; Fischer, L.
Reaction investigation of lactulose-producing cellobiose 2-epimerases under operational relevant conditions
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Caldicellulosiruptor saccharolyticus (A4XGA6), Dictyoglomus turgidum (B8DZK4), Dictyoglomus turgidum DSM 6724 (B8DZK4)
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brenda
Chen, Q.; Levin, R.; Zhang, W.; Zhang, T.; Jiang, B.; Stressler, T.; Fischer, L.; Mu, W.
Characterisation of a novel cellobiose 2-epimerase from thermophilic Caldicellulosiruptor obsidiansis for lactulose production
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Caldicellulosiruptor obsidiansis (D9TH31), Caldicellulosiruptor obsidiansis, Caldicellulosiruptor obsidiansis ATCC BAA-2073 / strain OB47 (D9TH31)
brenda
Park, A.R.; Kim, J.S.; Jang, S.W.; Park, Y.G.; Koo, B.S.; Lee, H.C.
Rational modification of substrate binding site by structure-based engineering of a cellobiose 2-epimerase in Caldicellulosiruptor saccharolyticus
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Caldicellulosiruptor saccharolyticus (A4XGA6), Caldicellulosiruptor saccharolyticus, Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331 (A4XGA6)
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Park, A.; Koo, B.; Kim, J.; Kim, E.; Lee, H.
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Caldicellulosiruptor saccharolyticus (A4XGA6)
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