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1 - 7
D-fructose
pH 8.0, 45°C, mutant enzyme I66V
2 - 4
D-fructose
pH 8.0, 50°C
3 - 5
D-fructose
pH 8.0, 45°C, mutant enzyme I66F
11
D-fructose
pH 8.0, 45°C, mutant enzyme I66L
16
D-fructose
pH 8.0, 45°C, mutant enzyme I66W
19
D-fructose
pH 8.0, 45°C, mutant enzyme I66C
22
D-fructose
pH 8.0, 45°C, mutant enzyme I66A
22
D-fructose
pH 8.0, 45°C, mutant enzyme I66Y
28
D-fructose
pH 8.0, 45°C, mutant enzyme I66G
31
D-fructose
pH 8.0, 50°C, mutant enzyme I33L/S213C
33
D-fructose
pH 8.0, 45°C, wild-type enzyme
36
D-fructose
pH 8.0, 45°C, mutant enzyme A107V
40
D-fructose
pH 8.0, 50°C, mutant enzyme I33L
42
D-fructose
pH 8.0, 50°C, mutant enzyme S213C
44
D-fructose
pH 8.0, 50°C, wild-type enzyme
67
D-fructose
pH 8.0, 45°C, mutant enzyme A107I
100
D-fructose
pH 8.0, 45°C, mutant enzyme D183E
139
D-fructose
pH 8.0, 45°C, mutant enzyme E156D
140
D-fructose
pH 8.0, 45°C, mutant enzyme A107P
270
D-fructose
pH 8.0, 45°C, mutant enzyme W112F
309
D-fructose
pH 8.0, 45°C, mutant enzyme R215K
427
D-fructose
pH 8.0, 45°C, mutant enzyme H209A
1 - 2
D-psicose
pH 8.0, 50°C
1 - 3
D-psicose
pH 8.0, 45°C, wild-type enzyme
37
D-psicose
pH 8.0, 45°C, mutant enzyme R215K
48
D-psicose
pH 8.0, 45°C, mutant enzyme E156D
100
D-psicose
pH 8.0, 45°C, mutant enzyme W112F
6 - 11
D-tagatose
pH 8.0, 45°C, mutant enzyme I66C
91
D-tagatose
pH 8.0, 45°C, wild-type enzyme
213
D-tagatose
pH 8.0, 45°C, mutant enzyme I66W
429
D-tagatose
pH 8.0, 45°C, mutant enzyme A107P
694
D-tagatose
pH 8.0, 45°C, mutant enzyme I66F
696
D-tagatose
pH 8.0, 45°C, mutant enzyme I66Y
1146
D-tagatose
pH 8.0, 45°C, mutant enzyme I66V
1369
D-tagatose
pH 8.0, 45°C, mutant enzyme I66G
1408
D-tagatose
pH 8.0, 45°C, mutant enzyme I66L
1640
D-tagatose
pH 8.0, 45°C, mutant enzyme I66A
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0.029
D-fructose
pH 8.0, 45°C, mutant enzyme D183E
4.9
D-fructose
pH 8.0, 45°C, mutant enzyme R215K
7.7
D-fructose
pH 8.0, 45°C, mutant enzyme H209A
17
D-fructose
pH 8.0, 45°C, mutant enzyme E156D
26
D-fructose
pH 8.0, 45°C, mutant enzyme A107V
26
D-fructose
pH 8.0, 45°C, mutant enzyme W112F
62
D-fructose
pH 8.0, 45°C, mutant enzyme I66C
68.3
D-fructose
pH 8.0, 50°C, mutant enzyme I33L/S213C
70
D-fructose
pH 8.0, 50°C, mutant enzyme I33L
70
D-fructose
pH 8.0, 50°C, mutant enzyme S213C
71.6
D-fructose
pH 8.0, 50°C, wild-type enzyme
72
D-fructose
pH 8.0, 45°C, mutant enzyme I66Y
88
D-fructose
pH 8.0, 45°C, mutant enzyme A107I
88
D-fructose
pH 8.0, 45°C, mutant enzyme I66V
116
D-fructose
pH 8.0, 45°C, mutant enzyme I66W
152
D-fructose
pH 8.0, 45°C, mutant enzyme I66G
168
D-fructose
pH 8.0, 45°C, mutant enzyme I66F
176
D-fructose
pH 8.0, 45°C, mutant enzyme I66L
308
D-fructose
pH 8.0, 45°C, mutant enzyme I66A
341
D-fructose
pH 8.0, 45°C, wild-type enzyme
996
D-fructose
pH 8.0, 45°C, mutant enzyme A107P
2068
D-fructose
pH 8.0, 50°C
23
D-psicose
pH 8.0, 45°C, mutant enzyme R215K
44
D-psicose
pH 8.0, 45°C, mutant enzyme W112F
46
D-psicose
pH 8.0, 45°C, mutant enzyme E156D
478
D-psicose
pH 8.0, 45°C, wild-type enzyme
2381
D-psicose
pH 8.0, 50°C
11
D-tagatose
pH 8.0, 45°C, mutant enzyme I66W
23
D-tagatose
pH 8.0, 45°C, mutant enzyme I66A
33
D-tagatose
pH 8.0, 45°C, mutant enzyme I66G
44
D-tagatose
pH 8.0, 45°C, mutant enzyme I66C
50
D-tagatose
pH 8.0, 45°C, mutant enzyme I66L
56
D-tagatose
pH 8.0, 45°C, mutant enzyme I66Y
64
D-tagatose
pH 8.0, 45°C, mutant enzyme I66F
100
D-tagatose
pH 8.0, 45°C, mutant enzyme I66V
136
D-tagatose
pH 8.0, 45°C, mutant enzyme A107P
194
D-tagatose
pH 8.0, 45°C, wild-type enzyme
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0.00029
D-fructose
pH 8.0, 45°C, mutant enzyme D183E
0.015
D-fructose
pH 8.0, 45°C, mutant enzyme R215K
0.018
D-fructose
pH 8.0, 45°C, mutant enzyme H209A
0.1
D-fructose
pH 8.0, 45°C, mutant enzyme W112F
0.12
D-fructose
pH 8.0, 45°C, mutant enzyme E156D
0.72
D-fructose
pH 8.0, 45°C, mutant enzyme A107V
1.3
D-fructose
pH 8.0, 45°C, mutant enzyme A107I
1.65
D-fructose
pH 8.0, 50°C, wild-type enzyme
1.68
D-fructose
pH 8.0, 50°C, mutant enzyme S213C
1.75
D-fructose
pH 8.0, 50°C, mutant enzyme I33L
2.23
D-fructose
pH 8.0, 50°C, mutant enzyme I33L/S213C
3.3
D-fructose
pH 8.0, 45°C, mutant enzyme I66C
3.3
D-fructose
pH 8.0, 45°C, mutant enzyme I66Y
4.8
D-fructose
pH 8.0, 45°C, mutant enzyme I66F
5.2
D-fructose
pH 8.0, 45°C, mutant enzyme I66V
5.4
D-fructose
pH 8.0, 45°C, mutant enzyme I66G
7
D-fructose
pH 8.0, 45°C, mutant enzyme A107P
7.3
D-fructose
pH 8.0, 45°C, mutant enzyme I66W
10
D-fructose
pH 8.0, 45°C, wild-type enzyme
14
D-fructose
pH 8.0, 45°C, mutant enzyme I66A
16
D-fructose
pH 8.0, 45°C, mutant enzyme I66L
85
D-fructose
pH 8.0, 50°C
0.44
D-psicose
pH 8.0, 45°C, mutant enzyme W112F
0.62
D-psicose
pH 8.0, 45°C, mutant enzyme R215K
0.96
D-psicose
pH 8.0, 45°C, mutant enzyme E156D
37
D-psicose
pH 8.0, 45°C, wild-type enzyme
205
D-psicose
pH 8.0, 50°C
0.014
D-tagatose
pH 8.0, 45°C, mutant enzyme I66A
0.024
D-tagatose
pH 8.0, 45°C, mutant enzyme I66G
0.036
D-tagatose
pH 8.0, 45°C, mutant enzyme I66L
0.05
D-tagatose
pH 8.0, 45°C, mutant enzyme I66W
0.072
D-tagatose
pH 8.0, 45°C, mutant enzyme I66C
0.08
D-tagatose
pH 8.0, 45°C, mutant enzyme I66Y
0.087
D-tagatose
pH 8.0, 45°C, mutant enzyme I66V
0.09
D-tagatose
pH 8.0, 45°C, mutant enzyme I66F
0.32
D-tagatose
pH 8.0, 45°C, mutant enzyme A107P
2.1
D-tagatose
pH 8.0, 45°C, wild-type enzyme
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A107I
7.7fold decrease in kcat/Km for D-fructose, no activity detected with D-tagatose
A107P
1.4fold decrease in kcat/Km for D-fructose, 6.6fold decrease in kcat/Km for D-tagatose
A107V
13.9fold decrease in kcat/Km for D-fructose, no activity detected with D-tagatose
E150Q
inactive mutant enzyme
E156D
mutant exhibits 63% of the wild-type activity
E244Q
inactive mutant enzyme
G67C
the variant shows remarkably decreased specific activity
I33E
the enzyme variant shows no activity
I33K
the enzyme variant shows no activity
I33L
increase of 5°C in the temperature for maximal enzyme activity, increase of 7.2-fold in the half-life at 50°C, and increase of 4.3°C in apparent melting temperature, respectively, compared with the wild-type enzyme
I33L-S213C
site-directed mutagenesis, structure homology modeling and substrate docking the double-site variant I33L-S213C DPEase on the crystal structure of DPEase from Agrobacterium tumefaciens, PDB Id 2HK0, as a template. Production of D-psicose from D-fructose by whole recombinant cells and its crude enzyme under optimized conditions, overview
I33L/S213C
increase of 7.5°C in the temperature for maximal enzyme activity, increase of 29.9-fold in the half-life at 50°C, and increase of 7.6°C in apparent melting temperature, respectively, compared with the wild-type enzyme. After 8 or 16 days, the enzyme activity gradually decreases, and the conversion yields with and without borate are reduced to 22 and 9.6%, respectively, at 30 days. In contrast, the activity of the immobilized I33L/S213C variant with and without borate does not decrease during the operation time of 30 days
I33P
the enzyme variant shows no activity
I66A
1.4fold increase in kcat/Km for D-fructose, 150fold decrease in kcat/Km for D-tagatose
I66C
3fold decrease in kcat/Km for D-fructose, 29.2fold decrease in kcat/Km for D-tagatose
I66F
2.1fold decrease in kcat/Km for D-fructose, 23.3fold decrease in kcat/Km for D-tagatose
I66G
1.9fold decrease in kcat/Km for D-fructose, 87.5fold decrease in kcat/Km for D-tagatose
I66L
1.6fold increase in kcat/Km for D-fructose, 58,3fold decrease in kcat/Km for D-tagatose
I66V
1.9fold decrease in kcat/Km for D-fructose, 24fold decrease in kcat/Km for D-tagatose
I66W
1.4fold decrease in kcat/Km for D-fructose, 42fold decrease in kcat/Km for D-tagatose
I66Y
3fold decrease in kcat/Km for D-fructose, 26fold decrease in kcat/Km for D-tagatose
R215K
mutant exhibits 25% of the wild-type activity
S213C
increase of 2.5°C in the temperature for maximal enzyme activity, increase of 3.3-fold in the half-life at 50°C, and increase of 3.1°C in apparent melting temperature, respectively, compared with the wild-type enzyme. Immobilized wild-type enzyme with and without borate maintains activity for 8 days at a conversion yield of 70% (350 g/l psicose) and for 16 days at a conversion yield of 30% (150 g/l psicose), respectively
S213E
decrease of 7.2°C in half-life at 55°C
S213K
the variant shows no activity
S213M
decrease of 6.8°C in half-life at 55°C
S213P
decrease of 6°C in half-life at 55°C
S213T
decrease of 5°C in half-life at 55°C
S8T
the variant displays 29% of the wild-type activity
V96A
the variant displays 51% of the wild-type activity
W112A
mutant enzyme exhibits no detectable activity
W112F
mutant enzyme displays 19% of the wild type enzyme activity. kcat/Km for D-fructose is 100fold lower than wild-type value, kcat/Km fur D-psicose is 84fold lower than wild-type value
W112H
mutant enzyme displays 65% of the wild type enzyme activity
W112Y
mutant enzyme displays 54% of the wild type enzyme activity
E150Q
-
inactive mutant enzyme
-
E156D
-
mutant exhibits 63% of the wild-type activity
-
E244Q
-
inactive mutant enzyme
-
I33L
-
increase of 5°C in the temperature for maximal enzyme activity, increase of 7.2-fold in the half-life at 50°C, and increase of 4.3°C in apparent melting temperature, respectively, compared with the wild-type enzyme
-
I33L/S213C
-
increase of 7.5°C in the temperature for maximal enzyme activity, increase of 29.9-fold in the half-life at 50°C, and increase of 7.6°C in apparent melting temperature, respectively, compared with the wild-type enzyme. After 8 or 16 days, the enzyme activity gradually decreases, and the conversion yields with and without borate are reduced to 22 and 9.6%, respectively, at 30 days. In contrast, the activity of the immobilized I33L/S213C variant with and without borate does not decrease during the operation time of 30 days
-
I66A
-
1.4fold increase in kcat/Km for D-fructose, 150fold decrease in kcat/Km for D-tagatose
-
I66C
-
3fold decrease in kcat/Km for D-fructose, 29.2fold decrease in kcat/Km for D-tagatose
-
I66G
-
1.9fold decrease in kcat/Km for D-fructose, 87.5fold decrease in kcat/Km for D-tagatose
-
I66L
-
1.6fold increase in kcat/Km for D-fructose, 58,3fold decrease in kcat/Km for D-tagatose
-
I66V
-
1.9fold decrease in kcat/Km for D-fructose, 24fold decrease in kcat/Km for D-tagatose
-
R215K
-
mutant exhibits 25% of the wild-type activity
-
S213C
-
increase of 2.5°C in the temperature for maximal enzyme activity, increase of 3.3-fold in the half-life at 50°C, and increase of 3.1°C in apparent melting temperature, respectively, compared with the wild-type enzyme. Immobilized wild-type enzyme with and without borate maintains activity for 8 days at a conversion yield of 70% (350 g/l psicose) and for 16 days at a conversion yield of 30% (150 g/l psicose), respectively
-
S213E
-
decrease of 7.2°C in half-life at 55°C
-
S213K
-
the variant shows no activity
-
W112F
-
mutant enzyme displays 19% of the wild type enzyme activity. kcat/Km for D-fructose is 100fold lower than wild-type value, kcat/Km fur D-psicose is 84fold lower than wild-type value
-
W112H
-
mutant enzyme displays 65% of the wild type enzyme activity
-
W112Y
-
mutant enzyme displays 54% of the wild type enzyme activity
-
I33L-S213C
-
site-directed mutagenesis, structure homology modeling and substrate docking the double-site variant I33L-S213C DPEase on the crystal structure of DPEase from Agrobacterium tumefaciens, PDB Id 2HK0, as a template. Production of D-psicose from D-fructose by whole recombinant cells and its crude enzyme under optimized conditions, overview
-
additional information
for production of D-psicose from D-glucose in an enzymatic process, the xylose isomerase gene from Escherichia coli strain MG1665 and the D-psicose 3-epimerase gene from Agrobacterium tumefaciens CGMCC 1.1488 are coexpressed in Escherichia coli strain BL21(DE3). After 24 h incubation with the dual enzyme system at 40°C, the sugar conversion ratio from D-glucose to D-psicose reaches 10%. The optimal conditions are 50°C, pH 7.5 with Co2+ and Mg2+. The D-psicose yields from sugarcane bagasse and microalgae hydrolysate are 1.42 and 1.69 g/L, respectively. Co2+ is strictly required. Method optimization and evaluation, overview
additional information
immobilization of Agrobacterium tumefaciens DPEase (agtu-DPEase) on graphene oxide particles (GO-agtu-DPEase). Immobilization on graphene oxide improves the thermal stability and bioconversion efficiency of D-psicose 3-epimerase for rare sugar production. Graphene oxide immobilized agtu-DPEase (GO-agtu-DPEase) shows optima at pH 7.5 and 60°C. Significant improvement in thermal stability is observed with half-life of 720 min at 60°C while unbound (agtu) DPEase is stable for 3.99 min at 60°C. At equilibrium, the bioconversion efficiency is accounted 40:60 (D-psicose: D-fructose) for graphene oxide-immobilized DPEase which is higher than for the free agtu-DPEase (32:68). Graphene oxide immobilized DPEase shows bioconversion efficiency up to 10 cycles of reusability
additional information
improved operational stability of D-psicose 3-epimerase by a protein engineering strategy by introduction of a SUMO fusion system, using Saccharomyces cerevisiae Smt3, as the N-terminal tag, which can significantly enhance operational stability and bioconversion efficiency of D-psicose 3-epimerase. The Smt3-D-psicose 3-epimerase conjugate system exhibits relatively better catalytic efficiency, and improved productivity in terms of space-time yields of about 8.5 kg/l/day, it can serve as a catalytic tool for the pilot scale production of the functional sugar, D-psicose, D-psicose production from fruit and vegetable remains and agro-industrial by-products, overview. The bioprocessing leads to achievement of D-psicose production to the extent of 25-35% conversion w/w of D-fructose contained in the sample
additional information
the engineered Kluyveromyces marxianus strain CICC1911 expressing gene dpe produces 190 g/l D-allulose with 750 g/l D-fructose as a substrate at 55°C within 12 h. Approximately 100 g of residual D-fructose are converted into 34 g of ethanol, and 15 g of the engineered Kluyveromyces marxianus cells are regenerated after fermentation at 37°C for 21 h. A purity of D-allulose of more than 90% can be obtained without isolating it from D-allulose and D-fructose mixture through residual D-fructose consumption, method development and evaluation of a valuable pathway to regenerate engineered cells and achieve cyclic catalysis for D-allulose production, overview
additional information
-
the engineered Kluyveromyces marxianus strain CICC1911 expressing gene dpe produces 190 g/l D-allulose with 750 g/l D-fructose as a substrate at 55°C within 12 h. Approximately 100 g of residual D-fructose are converted into 34 g of ethanol, and 15 g of the engineered Kluyveromyces marxianus cells are regenerated after fermentation at 37°C for 21 h. A purity of D-allulose of more than 90% can be obtained without isolating it from D-allulose and D-fructose mixture through residual D-fructose consumption, method development and evaluation of a valuable pathway to regenerate engineered cells and achieve cyclic catalysis for D-allulose production, overview
additional information
-
for production of D-psicose from D-glucose in an enzymatic process, the xylose isomerase gene from Escherichia coli strain MG1665 and the D-psicose 3-epimerase gene from Agrobacterium tumefaciens CGMCC 1.1488 are coexpressed in Escherichia coli strain BL21(DE3). After 24 h incubation with the dual enzyme system at 40°C, the sugar conversion ratio from D-glucose to D-psicose reaches 10%. The optimal conditions are 50°C, pH 7.5 with Co2+ and Mg2+. The D-psicose yields from sugarcane bagasse and microalgae hydrolysate are 1.42 and 1.69 g/L, respectively. Co2+ is strictly required. Method optimization and evaluation, overview
-
additional information
-
improved operational stability of D-psicose 3-epimerase by a protein engineering strategy by introduction of a SUMO fusion system, using Saccharomyces cerevisiae Smt3, as the N-terminal tag, which can significantly enhance operational stability and bioconversion efficiency of D-psicose 3-epimerase. The Smt3-D-psicose 3-epimerase conjugate system exhibits relatively better catalytic efficiency, and improved productivity in terms of space-time yields of about 8.5 kg/l/day, it can serve as a catalytic tool for the pilot scale production of the functional sugar, D-psicose, D-psicose production from fruit and vegetable remains and agro-industrial by-products, overview. The bioprocessing leads to achievement of D-psicose production to the extent of 25-35% conversion w/w of D-fructose contained in the sample
-
additional information
-
the engineered Kluyveromyces marxianus strain CICC1911 expressing gene dpe produces 190 g/l D-allulose with 750 g/l D-fructose as a substrate at 55°C within 12 h. Approximately 100 g of residual D-fructose are converted into 34 g of ethanol, and 15 g of the engineered Kluyveromyces marxianus cells are regenerated after fermentation at 37°C for 21 h. A purity of D-allulose of more than 90% can be obtained without isolating it from D-allulose and D-fructose mixture through residual D-fructose consumption, method development and evaluation of a valuable pathway to regenerate engineered cells and achieve cyclic catalysis for D-allulose production, overview
-
additional information
-
immobilization of Agrobacterium tumefaciens DPEase (agtu-DPEase) on graphene oxide particles (GO-agtu-DPEase). Immobilization on graphene oxide improves the thermal stability and bioconversion efficiency of D-psicose 3-epimerase for rare sugar production. Graphene oxide immobilized agtu-DPEase (GO-agtu-DPEase) shows optima at pH 7.5 and 60°C. Significant improvement in thermal stability is observed with half-life of 720 min at 60°C while unbound (agtu) DPEase is stable for 3.99 min at 60°C. At equilibrium, the bioconversion efficiency is accounted 40:60 (D-psicose: D-fructose) for graphene oxide-immobilized DPEase which is higher than for the free agtu-DPEase (32:68). Graphene oxide immobilized DPEase shows bioconversion efficiency up to 10 cycles of reusability
-
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medicine
D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar. It is regarded as a low calorie sweetener, an inhibitor of hepatic lipogenic enzymes, an activator of abdominal lipolysis and intestinal alpha-glycosidase enzymes D-psicose reduces the hyperglycemia, obesity, and hyperlipidemia and decrease the blood glucose level in type-2 diabetes
medicine
-
D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar. It is regarded as a low calorie sweetener, an inhibitor of hepatic lipogenic enzymes, an activator of abdominal lipolysis and intestinal alpha-glycosidase enzymes D-psicose reduces the hyperglycemia, obesity, and hyperlipidemia and decrease the blood glucose level in type-2 diabetes
-
nutrition
D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar. It is regarded as a low calorie sweetener, an inhibitor of hepatic lipogenic enzymes, an activator of abdominal lipolysis and intestinal alpha-glycosidase enzymes D-psicose reduces the hyperglycemia, obesity, and hyperlipidemia and decrease the blood glucose level in type-2 diabetes
nutrition
-
D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar. It is regarded as a low calorie sweetener, an inhibitor of hepatic lipogenic enzymes, an activator of abdominal lipolysis and intestinal alpha-glycosidase enzymes D-psicose reduces the hyperglycemia, obesity, and hyperlipidemia and decrease the blood glucose level in type-2 diabetes
-
synthesis
the enzyme can be used for synthesis of D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar
synthesis
the enzyme from Agrobacterium tumefaciens can be used for production of D-psicose in a coexpression system with xylose isomerase gene from Escherichia coli. Method optimization and evaluation, overview
synthesis
-
the enzyme can be used for synthesis of D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar
-
synthesis
-
the enzyme from Agrobacterium tumefaciens can be used for production of D-psicose in a coexpression system with xylose isomerase gene from Escherichia coli. Method optimization and evaluation, overview
-
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Kim, H.J.; Hyun, E.K.; Kim, Y.S.; Lee, Y.J.; Oh, D.K.
Characterization of an Agrobacterium tumefaciens D-psicose 3-epimerase that converts D-fructose to D-psicose
Appl. Environ. Microbiol.
72
981-985
2006
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens, Agrobacterium tumefaciens ATCC 33970 (A9CH28)
brenda
Choi, J.G.; Ju, Y.H.; Yeom, S.J.; Oh, D.K.
Improvement in the thermostability of D-psicose 3-epimerase from Agrobacterium tumefaciens by random and site-directed mutagenesis
Appl. Environ. Microbiol.
77
7316-7320
2011
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
brenda
Gu, L.; Zhang, J.; Liu, B.; Wu, C.; Du, G.; Chen, J.
High-level extracellular production of D-psicose-3-epimerase with recombinant Escherichia coli by a two-stage glycerol feeding approach
Bioprocess Biosyst. Eng.
36
1767-1777
2013
Agrobacterium tumefaciens, Agrobacterium tumefaciens C58 / ATCC 33970
brenda
Kim, H.J.; Lim, B.C.; Yeom, S.J.; Kim, Y.S.; Kim, D.; Oh, D.K.
Roles of Ile66 and Ala107 of D-psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its substrate, D-fructose
Biotechnol. Lett.
32
113-118
2009
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
brenda
Kim, H.J.; Yeom, S.J.; Kim, K.; Rhee, S.; Kim, D.; Oh, D.K.
Mutational analysis of the active site residues of a D-psicose 3-epimerase from Agrobacterium tumefaciens
Biotechnol. Lett.
32
261-268
2010
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
brenda
Kim, K.; Kim, H.J.; Oh, D.K.; Cha, S.S.; Rhee, S.
Crystal structure of D-psicose 3-epimerase from Agrobacterium tumefaciens and its complex with true substrate D-fructose: a pivotal role of metal in catalysis, an active site for the non-phosphorylated substrate, and its conformational changes
J. Mol. Biol.
361
920-931
2006
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
brenda
Patel, S.N.; Sharma, M.; Lata, K.; Singh, U.; Kumar, V.; Sangwan, R.S.; Singh, S.P.
Improved operational stability of D-psicose 3-epimerase by a novel protein engineering strategy, and D-psicose production from fruit and vegetable residues
Biores. Technol.
216
121-127
2016
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens EHA 105 / NCIM 2942 (A9CH28)
brenda
Chen, X.; Wang, W.; Xu, J.; Yuan, Z.; Yuan, T.; Zhang, Y.; Liang, C.; He, M.; Guo, Y.
Production of D-psicose from D-glucose by co-expression of D-psicose 3-epimerase and xylose isomerase
Enzyme Microb. Technol.
105
18-23
2017
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens CGMCC 1.1488 / C58 / ATCC 33970 (A9CH28)
brenda
Dedania, S.R.; Patel, M.J.; Patel, D.M.; Akhani, R.C.; Patel, D.H.
Immobilization on graphene oxide improves the thermal stability and bioconversion efficiency of D-psicose 3-epimerase for rare sugar production
Enzyme Microb. Technol.
107
49-56
2017
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens MTCC 609 / C58 / ATCC 33970 (A9CH28)
brenda
Park, C.S.; Park, C.S.; Shin, K.C.; Oh, D.K.
Production of d-psicose from D-fructose by whole recombinant cells with high-level expression of D-psicose 3-epimerase from Agrobacterium tumefaciens
J. Biosci. Bioeng.
121
186-190
2016
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens C58 / ATCC 33970 (A9CH28)
brenda
Yang, P.; Zhu, X.; Zheng, Z.; Mu, D.; Jiang, S.; Luo, S.; Wu, Y.; Du, M.
Cell regeneration and cyclic catalysis of engineered Kluyveromyces marxianus of a D-psicose-3-epimerase gene from Agrobacterium tumefaciens for D-allulose production
World J. Microbiol. Biotechnol.
34
65
2018
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens, Agrobacterium tumefaciens EHA 105 / NCIM 2942 (A9CH28)
brenda