5.1.3.11: cellobiose epimerase
This is an abbreviated version!
For detailed information about cellobiose epimerase, go to the full flat file.
Word Map on EC 5.1.3.11
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5.1.3.11
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synthesis
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epimerization
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lactulose
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caldicellulosiruptor
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saccharolyticus
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isomerization
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d-glucose
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ruminococcus
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albus
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prebiotic
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d-mannose
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marinus
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turgidum
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rhodothermus
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nutrition
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dictyoglomus
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mannans
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food industry
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n-acyl-d-glucosamine
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epimerizes
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isomerizes
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cello-oligosaccharides
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spirochaeta
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pharmacology
- 5.1.3.11
- synthesis
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epimerization
- lactulose
- caldicellulosiruptor
- saccharolyticus
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isomerization
- d-glucose
- ruminococcus
- albus
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prebiotic
- d-mannose
- marinus
- turgidum
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rhodothermus
- nutrition
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dictyoglomus
- mannans
- food industry
- n-acyl-d-glucosamine
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epimerizes
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isomerizes
- cello-oligosaccharides
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spirochaeta
- pharmacology
Reaction
Synonyms
B15CE, BfCE, BN699_02313, Caob-CE, CE-NE1, ce13, cellobiose 2-epimerase, CS-HRCE, Csac_0294, CsCE, CvCE, DfCE, Dfer_1975, DsCE, DtCE, Dtur_0652, EcCE, EpiA, epilactose-producing cellobiose 2-epimerase, Epimerase, cellobiose, FbCE, FjCE, Fjoh_4956, HaCE, Haur_0887, mannobiose 2-epimerase, md1, md2, PhCE, Phep_3983, RACE, Rmar_2439, RmCE, SdCE, Sde_0508, SlCE, Slin_0271, Spith_0082, StCE, STHERM_c00950, TERTU_4095, Thsa-CE, TtCE
ECTree
5.1.3.11 cellobiose epimeraseAdvanced search results
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results (Engineering
Engineering on EC 5.1.3.11 - cellobiose epimerase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A12S
A12S/K328I
E161D
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
E161D/N365P
E161D/S180P/S351G
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/F231L/K328I
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
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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
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Y114F
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
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site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
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Y114L
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
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site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
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Y114T
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
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site-directed mutagenesis, the mutant shows reduced activity at 37°C compared to wild-type and inactivation at 65°C
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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
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
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
additional information
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
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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
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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
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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
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additional information
Caldicellulosiruptor saccharolyticus ATCC 43494 / DSM 8903 / Tp8T 6331
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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
Cellulosilyticum lentocellum ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
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enzyme production evaluation for large-sclae production, parameters, overview
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additional information
enzyme production evaluation for large-sclae production, parameters, overview
additional information
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enzyme production evaluation for large-sclae production, parameters, overview
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additional information
enzyme production evaluation for large-sclae production, parameters, overview
additional information
Flavobacterium johnsoniae ATCC 17061 / DSM 2064 / UW101
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enzyme production evaluation for large-sclae production, parameters, overview
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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
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enzyme production evaluation for large-sclae production, parameters, overview
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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
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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
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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
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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
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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
