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28
D-fructose

pH 8.0, 45°C, mutant enzyme I66G
100
D-fructose
pH 8.0, 45°C, mutant enzyme D183E
67
D-fructose
pH 8.0, 45°C, mutant enzyme A107I
139
D-fructose
pH 8.0, 45°C, mutant enzyme E156D
44
D-fructose
pH 8.0, 50°C, wild-type enzyme
42
D-fructose
pH 8.0, 50°C, mutant enzyme S213C
40
D-fructose
pH 8.0, 50°C, mutant enzyme I33L
140
D-fructose
pH 8.0, 45°C, mutant enzyme A107P
36
D-fructose
pH 8.0, 45°C, mutant enzyme A107V
33
D-fructose
pH 8.0, 45°C, wild-type enzyme
31
D-fructose
pH 8.0, 50°C, mutant enzyme I33L/S213C
22
D-fructose
pH 8.0, 45°C, mutant enzyme I66Y
22
D-fructose
pH 8.0, 45°C, mutant enzyme I66A
19
D-fructose
pH 8.0, 45°C, mutant enzyme I66C
16
D-fructose
pH 8.0, 45°C, mutant enzyme I66W
11
D-fructose
pH 8.0, 45°C, mutant enzyme I66L
270
D-fructose
pH 8.0, 45°C, mutant enzyme W112F
3 - 5
D-fructose
pH 8.0, 45°C, mutant enzyme I66F
2 - 4
D-fructose
pH 8.0, 50°C
309
D-fructose
pH 8.0, 45°C, mutant enzyme R215K
1 - 7
D-fructose
pH 8.0, 45°C, mutant enzyme I66V
427
D-fructose
pH 8.0, 45°C, mutant enzyme H209A
1 - 2
D-psicose

-
pH 8.0, 50°C
100
D-psicose
pH 8.0, 45°C, mutant enzyme W112F
48
D-psicose
pH 8.0, 45°C, mutant enzyme E156D
37
D-psicose
pH 8.0, 45°C, mutant enzyme R215K
1 - 3
D-psicose
pH 8.0, 45°C, wild-type enzyme
1 - 2
D-psicose
pH 8.0, 50°C
91
D-tagatose

pH 8.0, 45°C, wild-type enzyme
213
D-tagatose
pH 8.0, 45°C, mutant enzyme I66W
6 - 11
D-tagatose
pH 8.0, 45°C, mutant enzyme I66C
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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168
D-fructose

pH 8.0, 45°C, mutant enzyme I66F
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
4.9
D-fructose
pH 8.0, 45°C, mutant enzyme R215K
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
68.3
D-fructose
pH 8.0, 50°C, mutant enzyme I33L/S213C
62
D-fructose
pH 8.0, 45°C, mutant enzyme I66C
0.029
D-fructose
pH 8.0, 45°C, mutant enzyme D183E
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
2381
D-psicose

pH 8.0, 50°C
478
D-psicose
pH 8.0, 45°C, wild-type enzyme
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
33
D-tagatose

pH 8.0, 45°C, mutant enzyme I66G
136
D-tagatose
pH 8.0, 45°C, mutant enzyme A107P
194
D-tagatose
pH 8.0, 45°C, wild-type enzyme
44
D-tagatose
pH 8.0, 45°C, mutant enzyme I66C
23
D-tagatose
pH 8.0, 45°C, mutant enzyme I66A
100
D-tagatose
pH 8.0, 45°C, mutant enzyme I66V
11
D-tagatose
pH 8.0, 45°C, mutant enzyme I66W
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
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10
D-fructose

pH 8.0, 45°C, wild-type enzyme
4.8
D-fructose
pH 8.0, 45°C, mutant enzyme I66F
3.3
D-fructose
pH 8.0, 45°C, mutant enzyme I66Y
3.3
D-fructose
pH 8.0, 45°C, mutant enzyme I66C
2.23
D-fructose
pH 8.0, 50°C, mutant enzyme I33L/S213C
5.2
D-fructose
pH 8.0, 45°C, mutant enzyme I66V
1.75
D-fructose
pH 8.0, 50°C, mutant enzyme I33L
1.68
D-fructose
pH 8.0, 50°C, mutant enzyme S213C
1.65
D-fructose
pH 8.0, 50°C, wild-type enzyme
1.3
D-fructose
pH 8.0, 45°C, mutant enzyme A107I
5.4
D-fructose
pH 8.0, 45°C, mutant enzyme I66G
0.72
D-fructose
pH 8.0, 45°C, mutant enzyme A107V
7
D-fructose
pH 8.0, 45°C, mutant enzyme A107P
7.3
D-fructose
pH 8.0, 45°C, mutant enzyme I66W
0.12
D-fructose
pH 8.0, 45°C, mutant enzyme E156D
0.1
D-fructose
pH 8.0, 45°C, mutant enzyme W112F
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
0.018
D-fructose
pH 8.0, 45°C, mutant enzyme H209A
0.015
D-fructose
pH 8.0, 45°C, mutant enzyme R215K
0.00029
D-fructose
pH 8.0, 45°C, mutant enzyme D183E
205
D-psicose

-
pH 8.0, 50°C
37
D-psicose
pH 8.0, 45°C, wild-type enzyme
205
D-psicose
pH 8.0, 50°C
0.96
D-psicose
pH 8.0, 45°C, mutant enzyme E156D
0.62
D-psicose
pH 8.0, 45°C, mutant enzyme R215K
0.44
D-psicose
pH 8.0, 45°C, mutant enzyme W112F
2.1
D-tagatose

pH 8.0, 45°C, wild-type enzyme
0.32
D-tagatose
pH 8.0, 45°C, mutant enzyme A107P
0.09
D-tagatose
pH 8.0, 45°C, mutant enzyme I66F
0.087
D-tagatose
pH 8.0, 45°C, mutant enzyme I66V
0.08
D-tagatose
pH 8.0, 45°C, mutant enzyme I66Y
0.072
D-tagatose
pH 8.0, 45°C, mutant enzyme I66C
0.05
D-tagatose
pH 8.0, 45°C, mutant enzyme I66W
0.036
D-tagatose
pH 8.0, 45°C, mutant enzyme I66L
0.024
D-tagatose
pH 8.0, 45°C, mutant enzyme I66G
0.014
D-tagatose
pH 8.0, 45°C, mutant enzyme I66A
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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
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
A107P
1.4fold decrease in kcat/Km for D-fructose, 6.6fold decrease in kcat/Km for D-tagatose
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
I33P
the enzyme variant shows no activity
G67C
the variant shows remarkably decreased specific activity
E244Q
inactive mutant enzyme
I66F
2.1fold decrease in kcat/Km for D-fructose, 23.3fold decrease in kcat/Km for D-tagatose
E156D
mutant exhibits 63% of the wild-type 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
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
E150Q
inactive mutant enzyme
I66A
1.4fold increase in kcat/Km for D-fructose, 150fold decrease in kcat/Km for D-tagatose
A107V
13.9fold decrease in kcat/Km for D-fructose, no activity detected with D-tagatose
I66C
3fold decrease in kcat/Km for D-fructose, 29.2fold decrease in kcat/Km for D-tagatose
I33K
the enzyme variant shows no activity
A107I
7.7fold decrease in kcat/Km for D-fructose, no activity detected with D-tagatose
I33E
the enzyme variant shows no activity
E150Q
-
inactive mutant enzyme
-
S213K
-
the variant shows no activity
-
E244Q
-
inactive mutant enzyme
-
E156D
-
mutant exhibits 63% of the wild-type activity
-
R215K
-
mutant exhibits 25% of the wild-type 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
-
S213E
-
decrease of 7.2°C in half-life at 55°C
-
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
-
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
-
I66V
-
1.9fold decrease in kcat/Km for D-fructose, 24fold 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
-
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
-
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
-
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
-
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
-
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.
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2011
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
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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
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2013
Agrobacterium tumefaciens, Agrobacterium tumefaciens C58 / ATCC 33970
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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
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2009
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
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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.
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2010
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
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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.
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Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
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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.
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2016
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens EHA 105 / NCIM 2942 (A9CH28)
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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.
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2017
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens CGMCC 1.1488 / C58 / ATCC 33970 (A9CH28)
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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.
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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.
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186-190
2016
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens C58 / ATCC 33970 (A9CH28)
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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)
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