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D-psicose + NADH + H+
allitol + NAD+
-
-
-
-
?
D-xylulose
D-ribulose
-
3.9% activity compared to the activity with D-psicose
-
-
r
additional information
?
-
D-fructose
D-psicose
-
the equilibrium ratio between D-psicose and D-fructose is 30:70
-
-
r
D-fructose
D-psicose
-
-
-
-
r
D-fructose
D-psicose
under the optimal conditions, the equilibrium ratio of D-fructose to D-psicose is 69:31, relative activity with D-fructose is 66.4% of the activity with D-psicose
-
-
r
D-fructose
D-psicose
66.4% activity compared to the activity with D-psicose
-
-
r
D-fructose
D-psicose
under the optimal conditions, the equilibrium ratio of D-fructose to D-psicose is 69:31, relative activity with D-fructose is 66.4% of the activity with D-psicose
-
-
r
D-fructose
D-psicose
66.4% activity compared to the activity with D-psicose
-
-
r
D-fructose
D-psicose
-
-
-
r
D-fructose
D-psicose
the enzyme carries out the epimerization of D-fructose to D-psicose with a conversion yield of 32% under optimal conditions
-
-
r
D-fructose
D-psicose
the enzyme carries out the epimerization of D-fructose to D-psicose with a conversion yield of 32% under optimal conditions
-
-
r
D-fructose
D-psicose
-
-
-
r
D-fructose
D-psicose
-
the equilibrium ratio between D-psicose and D-fructose is 28:72 at 60°C
-
-
r
D-fructose
D-psicose
-
59.8% activity compared to the activity with D-psicose
-
-
r
D-fructose
D-psicose
-
-
-
-
r
D-fructose
D-psicose
-
-
-
-
r
D-fructose
D-psicose
the catalytic efficiency for D-psicose is 7.4fold higher than that for D-tagatose. The equilibrium ratio between D-psicose and D-fructose is 28:72. The catalytic efficiency for D-psicose is 258fold higher than that for D-tagatose
-
-
r
D-fructose
D-psicose
the catalytic efficiency for D-psicose is 7.4fold higher than that for D-tagatose. The equilibrium ratio between D-psicose and D-fructose is 28:72. The catalytic efficiency for D-psicose is 258fold higher than that for D-tagatose
-
-
r
D-psicose
D-fructose
optimum substrate. Equilibrium ratio between D-psicose and D-fructose is 28:72 at 65°C
-
-
r
D-psicose
D-fructose
optimum substrate. Equilibrium ratio between D-psicose and D-fructose is 28:72 at 65°C
-
-
r
D-psicose
D-fructose
-
the equilibrium ratio between D-psicose and D-fructose is 30:70
-
-
r
D-psicose
D-fructose
-
-
-
-
r
D-psicose
D-fructose
-
i.e. D-allulose
-
-
r
D-psicose
D-fructose
-
-
-
r
D-psicose
D-fructose
under the optimal conditions, the equilibrium ratio of D-fructose to D-psicose is 69:31, relative activity with D-fructose is 66.4% of the activity with D-psicose
-
-
r
D-psicose
D-fructose
i.e. D-ribo-2-hexulose or D-allulose, best substrate
-
-
r
D-psicose
D-fructose
under the optimal conditions, the equilibrium ratio of D-fructose to D-psicose is 69:31, relative activity with D-fructose is 66.4% of the activity with D-psicose
-
-
r
D-psicose
D-fructose
-
-
-
r
D-psicose
D-fructose
i.e. D-ribo-2-hexulose or D-allulose, best substrate
-
-
r
D-psicose
D-fructose
the enzyme carries out the epimerization of D-fructose to D-psicose with a conversion yield of 32% under optimal conditions
-
-
r
D-psicose
D-fructose
the enzyme carries out the epimerization of D-fructose to D-psicose with a conversion yield of 32% under optimal conditions
-
-
r
D-psicose
D-fructose
-
the equilibrium ratio between D-psicose and D-fructose is 28:72 at 60°C
-
-
r
D-psicose
D-fructose
-
-
-
-
r
D-psicose
D-fructose
-
best substrate
-
-
r
D-psicose
D-fructose
-
-
-
-
r
D-psicose
D-fructose
-
-
-
-
r
D-psicose
D-fructose
-
-
-
-
r
D-psicose
D-fructose
the catalytic efficiency for D-psicose is 7.4fold higher than that for D-tagatose. The equilibrium ratio between D-psicose and D-fructose is 28:72. The catalytic efficiency for D-psicose is 258fold higher than that for D-tagatose
-
-
r
D-psicose
D-fructose
-
-
-
-
r
D-psicose
D-fructose
the catalytic efficiency for D-psicose is 7.4fold higher than that for D-tagatose. The equilibrium ratio between D-psicose and D-fructose is 28:72. The catalytic efficiency for D-psicose is 258fold higher than that for D-tagatose
-
-
r
D-sorbose
D-tagatose
1.2% activity compared to the activity with D-psicose
-
-
r
D-sorbose
D-tagatose
1.2% activity compared to the activity with D-psicose
-
-
r
D-sorbose
D-tagatose
-
2.9% activity compared to the activity with D-psicose
-
-
r
D-tagatose
D-sorbose
-
-
-
r
D-tagatose
D-sorbose
23.2% activity compared to the activity with D-psicose
-
-
r
D-tagatose
D-sorbose
-
-
-
r
D-tagatose
D-sorbose
23.2% activity compared to the activity with D-psicose
-
-
r
D-tagatose
D-sorbose
-
24.2% activity compared to the activity with D-psicose
-
-
r
additional information
?
-
-
the equilibrium ratio between D-fructose and D-psicose is approximately 30:70 for the recombinant enzyme, elevated temperature does not significantly shift the equilibrium toward D-psicose. The conversion ratio of D-fructose to D-psicose is calculated to be 30.1%, 31.5%, 31.8%, 31.4%, 31.1%, 31.0%, 30.4%, 29.2%, and 28.6% when the reaction temperature is 40°C, 45°C, 50°C, 55°C, 60°C, 65°C, 70°C, 75°C, and 80°C, respectively
-
-
?
additional information
?
-
-
when the reaction equilibrium is reached, the ratio of D-glucose, D-fructose and D-allulose is approximately 6.5:7:3, respectively
-
-
?
additional information
?
-
no activity with D-fructose 6-phosphate and D-ribulose 5-phosphate. Catalytic efficiency (kcat/KM) of D-tagatose is 127fold lower than catalytic efficiency of D-psicose
-
-
?
additional information
?
-
-
no activity with D-fructose 6-phosphate and D-ribulose 5-phosphate. Catalytic efficiency (kcat/KM) of D-tagatose is 127fold lower than catalytic efficiency of D-psicose
-
-
?
additional information
?
-
no activity with D-fructose 6-phosphate and D-ribulose 5-phosphate. Catalytic efficiency (kcat/KM) of D-tagatose is 127fold lower than catalytic efficiency of D-psicose
-
-
?
additional information
?
-
the relative activity with D-tagatose is 4.9% of the activity with D-psicose, the catalytic efficiency for D-tagatose is 249fold lower than the catalytic efficiency for D-fructose, the relative activity with D-sorbose is 0.9% of the activity wth D-psicose. No activity with D-fructose-6-phosphate or D-ribulose-5-phosphate
-
-
?
additional information
?
-
the relative activity with D-tagatose is 4.9% of the activity with D-psicose, the catalytic efficiency for D-tagatose is 249fold lower than the catalytic efficiency for D-fructose, the relative activity with D-sorbose is 0.9% of the activity wth D-psicose. No activity with D-fructose-6-phosphate or D-ribulose-5-phosphate
-
-
?
additional information
?
-
-
catalytic efficiency with D-tagatose is 108fold lower than cataltic efficiency with D-psicose
-
-
?
additional information
?
-
-
substrate specificity, overview. Poor activity with D-galactose, D-glucose, and D-arabinose, no activity with D-mannose
-
-
?
additional information
?
-
-
the D-psicose/D-fructose equilibrium ratio of Trpr-DPEase is 28:72. Recombinant enzyme produces D-psicose at a yield of 137.5 g/l from 500 g/l D-fructose
-
-
?
additional information
?
-
-
the D-psicose/D-fructose equilibrium ratio of Trpr-DPEase is 28:72. Recombinant enzyme produces D-psicose at a yield of 137.5 g/l from 500 g/l D-fructose
-
-
?
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Fe3+
-
at 1 mM increases enzymatic activity by 30%
Zn2+
-
1.75% of the activity with Co2+ at 1 mM
Co2+
the metal-dependent enzyme requires Co2+ as optimum cofactor. The relative activity is linearly increased when adding Co2+ from 0.005 mM to 0.035 mM. When adding greater concentrations of Co2+, the relative activity tends to be stable. The optimum Co2+ concentration is 0.2 mM for catalytic activity
Co2+
-
the enzyme is strictly metal-dependent and displays maximum activity in the presence of Co2+
Co2+
-
activates 10.8fold at 1 mM, best divalent cation, dependent on
Co2+
-
best metal cofactor, has no effect on pH stability and slightly imporves temperature
Co2+
metalloprotein that exhibits the highest activity in the presence of Co2+
Co2+
activates most highly at 0.5 mM, 80% of maximal activation at 1-5 mM, best divalent cation, dependent on
Co2+
the enzyme is strictly metal-dependent and shows a maximal activity in the presence of Co2+
Co2+
-
highly activating at 1 mM, essential for the activity of the recombinant enzyme
Fe2+
-
the enzyme is strictly metal-dependent and displays maximum activity in the presence of Co2+. When Co2+ is replaced with Fe2+ the enzyme activity is reduced to 49% of that in the presence of Co2+
Fe2+
-
26.59% of the activity with Co2+ at 1 mM
Fe2+
the enzyme is strictly metal-dependent and shows a maximal activity in the presence of Co2+. When Co2+ is replaced with Fe2+ the enzyme activity is reduced to 67% of that in presence of Co2+
Mg2+
the metal-dependent enzyme requires Co2+ as optimum cofactor. When Co2+ is replaced with Mg2+ the enzyme activity is reduced to 22% of that in presence of Co2+
Mg2+
the enzyme is strictly metal-dependent and shows a maximal activity in the presence of Co2+. When Co2+ is replaced with Mg2+ the enzyme activity is reduced to 38% of that in presence of Co2+
Mg2+
-
at 1 mM increases enzymatic activity by 10%
Mn2+
the metal-dependent enzyme requires Co2+ as optimum cofactor. When Co2+ is replaced with Mn2+ the enzyme activity is reduced to 66% of that in presence of Co2+
Mn2+
-
the enzyme is strictly metal-dependent and displays maximum activity in the presence of Co2+. When Co2+ is replaced with Mn2+ the enzyme activity is reduced to 80% of that in the presence of Co2+
Mn2+
-
81.24% of the activity with Co2+ at 1 mM
Mn2+
-
activates to 23.1% of the activity with Co2+ at 1 mM
Mn2+
the enzyme is strictly metal-dependent and shows a maximal activity in the presence of Co2+. When Co2+ is replaced with Mn2+ the enzyme activity is reduced to 92% of that in presence of Co2+
Mn2+
-
at 1 mM increases enzymatic activity by 60%
Mn2+
-
activates the recombinant free and immobilized enzyme, but does not affect the reaction equilibrium for both the free and the immobilized enzyme
Mn2+
-
highly activating at 1 mM
Mn2+
the enzyme is strictly metal-dependent and requires Mn2+ as optimum cofactor for activity
Ni2+
the metal-dependent enzyme requires Co2+ as optimum cofactor. When Co2+ is replaced with Ni2+ the enzyme activity is reduced to 31% of that in presence of Co2+
Ni2+
-
the enzyme is strictly metal-dependent and displays maximum activity in the presence of Co2+. When Co2+ is replaced with Ni2+, the enzyme activity is reduced to 14% of that in the presence of Co2+
Ni2+
-
7.96% of the activity with Co2+ at 1 mM
Ni2+
the enzyme is strictly metal-dependent and shows a maximal activity in the presence of Co2+. When Co2+ is replaced with Ni2+ the enzyme activity is reduced to 65% of that in presence of Co2+
additional information
-
Mg2+, Zn2+, and Cu2+ can not excite activity
additional information
-
metal-dependent enzyme, no activity without presence of divalent metal ion
additional information
-
no effect on activity by Mg2+
additional information
the CB-DPEase is a metalloprotein, that is inactive in absence of divalent metal ions
additional information
-
the CB-DPEase is a metalloprotein, that is inactive in absence of divalent metal ions
additional information
-
activity is not dependent on the presence of metal ions
additional information
-
the enzyme is metal-dependent
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additional information
-
on the basis of the Izumoring strategy, D-allulose can be obtained from D-glucose by coupling D-glucose isomerase (GIase) and DPEase, with D-fructose as the intermediate. In this reaction system, D-fructose is firstly converted from D-glucose by GIase, and immediately isomerised to D-allulose by DPEase. Recombinant co-expression with GIase from Acidothermus cellulolyticus from plasmid pETDuet-Dosp-DPE/Acce-GI, optimization of the biotransformation consitions, method, overview. When the reactions reaches equilibrium under optimal conditions,the equilibrium ratio of D-glucose, D-fructose and D-allulose is approximately 6.5:7:3, respectively. The transformation rate is about 18%. The optimum pH of the Acce-GI/Dosp-DPE co-expression system is lower than that of the BGI/RDPE co-expression system, while the optimum temperature is higher than that of the BGI/RDPE co-expression system
additional information
enzyme overexpression for heterologous production of D-psicose from D-fructose, under the optimal conditions, the equilibrium ratio of D-fructose to D-psicose is 69:31. For high production of D-psicose, 216 g/L D-psicose are produced with 28.8% turnover yield at pH 6.5 and 55°C. The recombinant DPEase exhibits weak acid stability and thermostability and has a high affinity and turnover for the substrate D-fructose
additional information
-
enzyme overexpression for heterologous production of D-psicose from D-fructose, under the optimal conditions, the equilibrium ratio of D-fructose to D-psicose is 69:31. For high production of D-psicose, 216 g/L D-psicose are produced with 28.8% turnover yield at pH 6.5 and 55°C. The recombinant DPEase exhibits weak acid stability and thermostability and has a high affinity and turnover for the substrate D-fructose
additional information
-
enzyme overexpression for heterologous production of D-psicose from D-fructose, under the optimal conditions, the equilibrium ratio of D-fructose to D-psicose is 69:31. For high production of D-psicose, 216 g/L D-psicose are produced with 28.8% turnover yield at pH 6.5 and 55°C. The recombinant DPEase exhibits weak acid stability and thermostability and has a high affinity and turnover for the substrate D-fructose
-
additional information
-
high-level intra- and extra-cellular production of D-psicose 3-epimerase via a modified xylose-inducible expression system in Bacillus subtilis, fed-batch fermentation in 7.5 l fermentor, overview
additional information
-
immobilization of recombinant extracellular enzyme DPE onto anion exchange resin D301, DPE immobilization yield is 90%. D-Psicose is produced using the immobilized enzyme, separated by simulated moving bed chromatography (SMB), and purified by crystallization. The purity of the D-psicose crystals reaches 99.1%, method optimization, overview
additional information
-
to improve the expression level of D-psicose 3-epimerase, the DPEase gene is fused with the promoter P43 to generate an expression cassette that introduced an identical cohesive end, and the resultant P43-DPE expression cassette is used as a monomeric fragment. The tandem repeats of the expression cassette are constructed by the isocaudamer method and integrated into the amyE gene locus of Bacillus subtilis by double-crossover. After DPEase is expressed in Bacillus subtilis, the antibiotic resistance gene is deleted via the Cre/lox system, thus generating food-grade strains. D-Psicose (D-allulose) production by freeze-dried enzyme powder, the optimal substrate concentration is 300 g/L of D-fructose, generating 26.67 g/l/h of D-allulose yield with an 8.89% conversion rate
additional information
-
to improve the expression level of D-psicose 3-epimerase, the DPEase gene is fused with the promoter P43 to generate an expression cassette that introduced an identical cohesive end, and the resultant P43-DPE expression cassette is used as a monomeric fragment. The tandem repeats of the expression cassette are constructed by the isocaudamer method and integrated into the amyE gene locus of Bacillus subtilis by double-crossover. After DPEase is expressed in Bacillus subtilis, the antibiotic resistance gene is deleted via the Cre/lox system, thus generating food-grade strains. D-Psicose (D-allulose) production by freeze-dried enzyme powder, the optimal substrate concentration is 300 g/L of D-fructose, generating 26.67 g/l/h of D-allulose yield with an 8.89% conversion rate
-
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5 - 9
purified recombinant enzyme, 80-100% of maximal activity within this range
746879
5.5
4°C, 2 h, about 30% loss of activity
728603
5.5 - 8.5
-
the purified recombinant enzyme retains more than 80% of initial activity when incubated for 2 h at pH values from pH 5.5 to pH 8.5
748412
6 - 7.5
after incubation at 4 °C for 2 h, more than 90% of the residual activity is retained at pH values ranging from of 6.07.5
726795
7.5
4°C, 2 h, less than 5% loss of activity
728603
7.5 - 8
4°C, 2 h, stable
727652
8
4°C, 2 h, about 10% loss of activity
728603
8.5
4°C, 2 h, about 10% loss of activity
728603
8.5 - 9
4°C, 2 h, 10% loss of activity
727652
9
4°C, 2 h, about 20% loss of activity
728603
6
4°C, 2 h, 15% loss of activity
727652
6
4°C, 2 h, about 15% loss of activity
728603
6 - 9
4°C, 2 h, more than 80% of initial activity remains
727229
6 - 9
-
purified recombinant enzyme, 4°C, 2 h, completely stable
748499
6.5
4°C, 2 h, 10% loss of activity
727652
6.5
4°C, 2 h, about 15% loss of activity
728603
7
purified recombinant enzyme, most stable at
746879
7
4°C, 2 h, 5% loss of activity
727652
7
4°C, 2 h, about 5% loss of activity
728603
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100
purified recombinant enzyme, 10 min, inactivation
20 - 60
-
activity of free DPE has small decreases after being maintained at 20-40°C, and has moderate decreases at 50-60°C, while the thermal stability of the immobilized DPE increases, particularly at 50°C
40 - 70
-
the purified recombinant enzyme retains 70% and 30% of its initial activity after 4 h of incubation at 40°C and 50°C, respectively, 55% activity remaining after 0.5 h at 60°C, complete inactivation after 0.5 h at 70°C
45
in the absence of Co2+, the activity is very stable below 45 °C but decreases at temperatures above 50 °C with increasing reaction times. When incubated with 0.4 mM Co2+, the half-lives (t1/2) of the enzyme are extended
64.4
apparent melting temperature
65
1 h, about 80% loss of activity
70
-
recombinant enzyme in overexpressing Escherichia coli cells, pH 6.5, 9.3% activity remaining after 30 min, inactivation after 4 h
40
4 h, stable
40
-
2 h, 46% loss of activity
40
-
recombinant enzyme in overexpressing Escherichia coli cells, pH 6.5, 64.7%, activity remaining after 18 h
40
-
purified recombinant His6-tagged enzyme, over 75% activity remaining after 4 h
50
4 h, about 50% loss of activity
50
-
2 h, 42% loss of activity, thermostability property is almost not affected by the addition of Co2+
50
-
recombinant enzyme in overexpressing Escherichia coli cells, pH 6.5, 58.4% activity remaining after 18 h
50
in the absence of Co2+, the activity is very stable below 45 °C but decreases at temperatures above 50 °C with increasing reaction times. When incubated with 0.4 mM Co2+, the half-lives (t1/2) of the enzyme are extended
50
-
purified recombinant His6-tagged enzyme, 7% activity remaining after 4 h
55
half-life: 156 min
55
purified recombinant enzyme, half-life is 156 min
55
the half-lives for the enzyme are 9.5 h and 24 min when incubated with and without Co2+ (0.1 mM)
55
1 h, about 40% loss of activity
60
half-life without metal: 15 min
60
-
the enzyme loses all of the initial activity after 0.5 h of exposure, thermostability property is almost not affected by the addition of Co2+
60
-
recombinant enzyme in overexpressing Escherichia coli cells, pH 6.5, 15.2% activity remaining after 18 h
60
the half-lives for the enzyme are 6.8 h and 10 min when incubated with and without Co2+ (0.1 mM)
60
1 h, about 55% loss of activity
additional information
-
Co2+ slightly improves the thermostability of the enzyme
additional information
-
the thermostability of the enzyme is enhanced by the addition of Mn2+
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DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant overexpression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli
expressed with a C-terminal 6His-tag in Escherichia coli
expression in Escherichia coli
gene CLOBOL_00069, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli
gene dpe, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene dpe, recombinant food-grade overexpression of His-tagged enzyme in Bacillus pumilus using the P2 promoter, derived from a cell wall protein promoter of the host bacterium, the recombinant protein is soluble and bioactive, and is secreted to a high leve, subcloning in Escherichis coli strain DH5alphal
-
gene rdpe, recombinant constitutive enzyme expression in Bacillus subtilis strains 1A751-SR, 1A751-GR, and 1A751S1-XR (from strain 1A751), in which two extracellular proteases (nprE, aprE) are deleted, Bacillus subtilis is transformed using the Paris method, screening and characterization of different inducible promoters, xylose-inducible expression system, method evaluation, detailed overview
-
gene rdpe, recombinant expression in and secretion from Bacillus subtilis alanine racemase knockout (deletion of gene dal using Cre/lox system) strains 1A751D2R and 1A751D2C, construction of food-grade expression plasmids with auxotrophic marker, the food-grade plasmids pMA5-DAL-RDPE and pMA5-DAL are transformed into the food-grade host strain 1A751D2 with the deficiency of alanine racemase gene to generate the recombinant strain 1A751D2R and 1A751D2C, respectively. The extracellular activity of enzyme RDPE is gradually increased with the fermentation process, and the highest activity reaches 46 U/ml at 72 h, fed-batch fermentation, method evaluation, overview
-
recombinant enzyme expression in Escherichia coli strain BL21(DE3), co-expression with D-glucose isomerase (GIase) from Acidothermus cellulolyticus from plasmid pETDuet-Dosp-DPE/Acce-GI
-
recombinant expression of D-psicose 3-epimerase and display on the surface of Bacillus subtilis spores. To improve the expression level of D-psicose 3-epimerase, the DPEase gene is fused with the promoter P43 to generate an expression cassette that introduced an identical cohesive end, and the resultant P43-DPE expression cassette is used as a monomeric fragment. The tandem repeats of the expression cassette are constructed by the isocaudamer method and integrated into the amyE gene locus of Bacillus subtilis by double-crossover. After DPEase is expressed in Bacillus subtilis, the antibiotic resistance gene is deleted via the Cre/lox system, thus generating food-grade strains
-
expressed in Escherichia coli
expressed in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
-
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synthesis
for the high production of D-psicose from D-fructose, the reaction reaches equilibrium after 160 min with the highest turnover yield (28.8%) observed at 55 °C
synthesis
-
suitable for the industrial production of D-psicose from fructose
synthesis
-
synthesis of the rare sugar D-psicose, that is an ideal sucrose substitute for food products, due to having 70% of the relative sweetness but 0.3% of the energy of sucrose. It also shows important physiological functions
synthesis
useful in the bioproduction of D-psicose, a rare hexose sugar, from D-fructose, found plenty in nature
synthesis
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D-psicose 3-epimerase is the key enzyme for producing D-allulose from inexpensive D-fructose sugar
synthesis
the enzyme is a potential D-psicose producer for industrial production
synthesis
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the recombinant Dorea sp. DPEase displays significantly higher specific activity at acidic pHs and remarkably higher productivity of D-psicose at pH 6.0, indicating that it is appropriate for use as a different source of D-psicose producing enzyme
synthesis
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Trpr-DPEase might be appropriate for the industrial production of D-psicose. Comparison of D-psicose productivity of various ketose 3-epimerases, overview
synthesis
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the recombinant Escherichia coli expressing D-psicose-3-epimerase (DPE), ribitol dehydrogenase (RDH) and formate dehydrogenase (FDH) is constructed and used together with immobilized GI for allitol bioproduction from D-glucose. The conditions of allitol biotransformation, the cell catalytic activity resistance, the cell cultivation medium, and fed-batch culture conditions are optimized
synthesis
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for the high production of D-psicose from D-fructose, the reaction reaches equilibrium after 160 min with the highest turnover yield (28.8%) observed at 55 °C
-
synthesis
-
the enzyme is a potential D-psicose producer for industrial production
-
synthesis
-
useful in the bioproduction of D-psicose, a rare hexose sugar, from D-fructose, found plenty in nature
-
synthesis
-
D-psicose 3-epimerase is the key enzyme for producing D-allulose from inexpensive D-fructose sugar
-
synthesis
-
Trpr-DPEase might be appropriate for the industrial production of D-psicose. Comparison of D-psicose productivity of various ketose 3-epimerases, overview
-
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Jia, M.; Mu, W.; Chu, F.; Zhang, X.; Jiang, B.; Zhou, L.L.; Zhang, T.
A D-psicose 3-epimerase with neutral pH optimum from Clostridium bolteae for D-psicose production: cloning, expression, purification, and characterization
Appl. Microbiol. Biotechnol.
98
717-725
2013
Enterocloster bolteae (A8RG82), Enterocloster bolteae, Enterocloster bolteae ATCC BAA-613 (A8RG82)
brenda
Zhu, Y.; Men, Y.; Bai, W.; Li, X.; Zhang, L.; Sun, Y.; Ma, Y.
Overexpression of D-psicose 3-epimerase from Ruminococcus sp. in Escherichia coli and its potential application in D-psicose production
Biotechnol. Lett.
34
1901-1906
2012
Ruminococcus sp.
brenda
Mu, W.; Zhang, W.; Fang, D.; Zhou, L.; Jiang, B.; Zhang, T.
Characterization of a D-psicose-producing enzyme, D-psicose 3-epimerase, from Clostridium sp.
Biotechnol. Lett.
35
1481-1486
2013
Clostridium sp. (H2JEN2), Clostridium sp. BNL1100 (H2JEN2)
brenda
Mu, W.; Chu, F.; Xing, Q.; Yu, S.; Zhou, L.; Jiang, B.
Cloning, expression, and characterization of a D-psicose 3-epimerase from Clostridium cellulolyticum H10
J. Agric. Food Chem.
59
7785-7792
2011
Ruminiclostridium cellulolyticum (B8I944), Ruminiclostridium cellulolyticum ATCC 35319 (B8I944)
brenda
Zhang, W.; Fang, D.; Zhang, T.; Zhou, L.; Jiang, B.; Mu, W.
Characterization of a metal-dependent D-psicose 3-epimerase from a novel strain, Desmospora sp. 8437
J. Agric. Food Chem.
61
11468-11476
2013
Desmospora sp. 8437
brenda
Zhang, W.; Fang, D.; Xing, Q.; Zhou, L.; Jiang, B.; Mu, W.
Characterization of a novel metal-dependent D-psicose 3-epimerase from Clostridium scindens 35704
PLoS One
8
e62987
2013
[Clostridium] scindens (B0NGC5), [Clostridium] scindens, [Clostridium] scindens ATCC 35704 (B0NGC5), [Clostridium] scindens ATCC 35704
brenda
Chan, H.C.; Zhu, Y.; Hu, Y.; Ko, T.P.; Huang, C.H.; Ren, F.; Chen, C.C.; Ma, Y.; Guo, R.T.; Sun, Y.
Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars
Protein Cell
3
123-131
2012
Ruminiclostridium cellulolyticum (B8I944), Ruminiclostridium cellulolyticum ATCC 35319 (B8I944)
brenda
Jia, M.; Mu, W.; Chu, F.; Zhang, X.; Jiang, B.; Zhou, L.; Zhang, T.
A D-psicose 3-epimerase with neutral pH optimum from Clostridium bolteae for D-psicose production Cloning, expression, purification, and characterization
Appl. Microbiol. Biotechnol.
98
717-725
2014
Enterocloster bolteae (A8RG82), Enterocloster bolteae, Enterocloster bolteae ATCC BAA-613 (A8RG82)
brenda
Chen, J.; Jin, Z.; Gai, Y.; Sun, J.; Zhang, D.
A food-grade expression system for D-psicose 3-epimerase production in Bacillus subtilis using an alanine racemase-encoding selection marker
Bioresour. Bioproc.
4
9
2017
Ruminococcus sp. 5_1_39BFAA
brenda
He, W.; Jiang, B.; Mu, W.; Zhang, T.
Production of D-allulose with D-psicose 3-epimerase expressed and displayed on the surface of Bacillus subtilis spores
J. Agric. Food Chem.
64
7201-7207
2016
[Clostridium] scindens, [Clostridium] scindens ATCC 35704
brenda
Li, C.; Lin, J.; Guo, Q.; Zhang, C.; Du, K.; Lin, H.; Lin, J.
D-Psicose 3-epimerase secretory overexpression, immobilization, and D-psicose biotransformation, separation and crystallization
J. Chem. Technol. Biotechnol.
93
350-357
2018
Ruminococcus sp. 5_1_39BFAA
-
brenda
Chen, J.; Zhu, Y.; Fu, G.; Song, Y.; Jin, Z.; Sun, Y.; Zhang, D.
High-level intra- and extra-cellular production of D-psicose 3-epimerase via a modified xylose-inducible expression system in Bacillus subtilis
J. Ind. Microbiol. Biotechnol.
43
1577-1591
2016
Ruminococcus sp. 5_1_39BFAA
brenda
Zhang, W.; Li, H.; Zhang, T.; Jiang, B.; Zhou, L.; Mu, W.
Characterization of a D-psicose 3-epimerase from Dorea sp. CAG317 with an acidic pH optimum and a high specific activity
J. Mol. Catal. B
120
68-74
2015
Dorea sp. CAG:317
-
brenda
Zhang, W.; Zhang, T.; Jiang, B.; Mu, W.
Biochemical characterization of a D-psicose 3-epimerase from Treponema primitia ZAS-1 and its application on enzymatic production of D-psicose
J. Sci. Food. Agric.
96
49-56
2016
Treponema primitia, Treponema primitia ZAS-1
brenda
Zhang, W.; Li, H.; Jiang, B.; Zhang, T.; Mu, W.
Production of D-allulose from D-glucose by Escherichia coli transformant cells co-expressing D-glucose isomerase and D-psicose 3-epimerase genes
J. Sci. Food. Agric.
97
3420-3426
2017
Dorea sp. CAG:317
brenda
Wen, X.; Lin, H.; Ren, Y.; Li, C.; Zhang, C.; Song, X.; Lin, J.; Lin, J.
Optimization for allitol production from D-glucose by using immobilized glucose isomerase and recombinant E. coli expressing D-psicose-3-epimerase, ribitol dehydrogenase and formate dehydrogenase
Biotechnol. Lett.
42
2135-2145
2020
Escherichia coli
brenda