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Biotechnology Letters, 2009 D-Psicose 3-epimerase from Agrobacterium tumefacience catalyzes the conversion of D: -fructose to D-psicose. According to mutational analysis, the ring at position 112, the negative charge at position 156, and the positive charge at position 215 were essential components for enzyme activity and for binding fructose and psicose. The surface contact area
Hye-Jung, Kim +5 more
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Characterization of a d-psicose-producing enzyme, d-psicose 3-epimerase, from Clostridium sp.
Biotechnology Letters, 2013The gene coding for D-psicose 3-epimerase (DPEase) from Clostridium sp. BNL1100 was cloned and expressed in Escherichia coli. The recombinant enzyme was purified by Ni-affinity chromatography. It was a metal-dependent enzyme and required Co(2+) as optimum cofactor.
Wanmeng Mu, Bo Jiang, Wenli Zhang
exaly +3 more sources
Enzyme and Microbial Technology, 2020 d-Psicose, as important rare sugar and epimer of d-fructose on the C-3 position, displays unique health benefits and physiological functions in various fields. The production of d-psicose is currently obtained via enzymatic bioconversion, mostly with of d-tagatose 3-epimerase.
Jun Zhang +9 more
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Biotechnology Letters, 2012
The D-psicose 3-epimerase (DPE) gene from Ruminococcus sp. was cloned and overexpressed in Escherichia coli. The recombinant protein was purified and characterized. It was optimally active at pH 7.5-8.0 and 60 °C. Activity was not dependent on the presence of metal ions; however, it became more thermostable with added Mn(2+).
Yueming Zhu
exaly +3 more sources
The D-psicose 3-epimerase (DPE) gene from Ruminococcus sp. was cloned and overexpressed in Escherichia coli. The recombinant protein was purified and characterized. It was optimally active at pH 7.5-8.0 and 60 °C. Activity was not dependent on the presence of metal ions; however, it became more thermostable with added Mn(2+).
Yueming Zhu
exaly +3 more sources
Applied Microbiology and Biotechnology, 2013
D-Tagatose 3-epimerase family enzymes can efficiently catalyze the epimerization of free keto-sugars, which could be used for D-psicose production from D-fructose. In previous studies, all optimum pH values of these enzymes were found to be alkaline. In this study, a D-psicose 3-epimerase (DPEase) with neutral pH optimum from Clostridium bolteae (ATCC ...
Wanmeng Mu, Bo Jiang
exaly +3 more sources
D-Tagatose 3-epimerase family enzymes can efficiently catalyze the epimerization of free keto-sugars, which could be used for D-psicose production from D-fructose. In previous studies, all optimum pH values of these enzymes were found to be alkaline. In this study, a D-psicose 3-epimerase (DPEase) with neutral pH optimum from Clostridium bolteae (ATCC ...
Wanmeng Mu, Bo Jiang
exaly +3 more sources
Biotechnology Letters, 2009 Using site-directed mutagenesis, we investigated the roles of Ile66 and Ala107 of D: -psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its true substrate, D: -fructose. When Ile66 was substituted with alanine, glycine, cysteine, leucine, phenylalanine, tryptophan, tyrosine or valine, all the mutants dramatically increased the K (m ...
Hye-Jung, Kim +5 more
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Journal of Bioscience and Bioengineering, 2000
An improved process for the mass production of D-psicose from D-fructose was developed. A D-fructose solution (60%, pH 7.0) was passed at 45 degrees C through a column filled with immobilized D-tagatose 3-epimerase (D-TE) which was produced using recombinant Escherichia coli, and 25% of the substrate was converted to D-psicose. After epimerization, the
Kei Takeshita
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An improved process for the mass production of D-psicose from D-fructose was developed. A D-fructose solution (60%, pH 7.0) was passed at 45 degrees C through a column filled with immobilized D-tagatose 3-epimerase (D-TE) which was produced using recombinant Escherichia coli, and 25% of the substrate was converted to D-psicose. After epimerization, the
Kei Takeshita
exaly +3 more sources
A stable immobilized d-psicose 3-epimerase for the production of d-psicose in the presence of borate
Process Biochemistry, 2009Abstract Maximal activity of the immobilized d -psicose 3-epimerase from Agrobacterium tumefaciens on Duolite A568 beads was achieved at pH 9.0 and 55 °C with borate, and at pH 8.5 and 50 °C without borate. The half-lives of the immobilized enzyme at 50 °C with and without borate were increased 4.2- and 128-fold compared to that of the free enzyme ...
Byung-Chul Lim +2 more
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Journal of Chemical Technology & Biotechnology, 2017
AbstractBACKGROUNDD‐psicose is a rare sugar and exists in extremely small quantities in nature. It has important physiological functions and is allowed to be used as an ingredient in foods and dietary supplements. The aim of this study is to develop the biotransformation, separation and purification methods for highly efficient mass production of d ...
Can Li +6 more
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AbstractBACKGROUNDD‐psicose is a rare sugar and exists in extremely small quantities in nature. It has important physiological functions and is allowed to be used as an ingredient in foods and dietary supplements. The aim of this study is to develop the biotransformation, separation and purification methods for highly efficient mass production of d ...
Can Li +6 more
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Enzyme and Microbial Technology, 2017
d-Psicose has been drawing increasing attention in recent years because of its medical and health applications. The production of d-psicose from d-glucose requires the co-expression and synergistic action of xylose isomerase and d-psicose 3-epimerase.
Xiaoyan, Chen +8 more
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d-Psicose has been drawing increasing attention in recent years because of its medical and health applications. The production of d-psicose from d-glucose requires the co-expression and synergistic action of xylose isomerase and d-psicose 3-epimerase.
Xiaoyan, Chen +8 more
openaire +2 more sources