Results 71 to 80 of about 277 (107)
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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, Ma Yanhe
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, Ma Yanhe
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 ...
Deok-Kun Oh
exaly +2 more sources
Enzyme and Microbial Technology, 2014
D-Psicose has been attracting attention in recent years because of its alimentary activities and is used as an ingredient in a range of foods and dietary supplements. To develop a one-step enzymatic process of D-psicose production, thermoactive D-glucose isomerase and the D-psicose 3-epimerase obtained from Bacillus sp.
Ken Izumori, Yan Zeng, Yueming Zhu
exaly +3 more sources
D-Psicose has been attracting attention in recent years because of its alimentary activities and is used as an ingredient in a range of foods and dietary supplements. To develop a one-step enzymatic process of D-psicose production, thermoactive D-glucose isomerase and the D-psicose 3-epimerase obtained from Bacillus sp.
Ken Izumori, Yan Zeng, Yueming Zhu
exaly +3 more sources
Bioresource Technology, 2016
The aim of the present work was to improve stability of d-psicose 3-epimerase and biotransformation of fruit and vegetable residues for d-psicose production. The study established that N-terminal fusion of a yeast homolog of SUMO protein - Smt3 - can confer elevated optimal temperature and improved operational stability to d-psicose 3-epimerase.
Sudhir P Singh, Satya Narayan Patel
exaly +3 more sources
The aim of the present work was to improve stability of d-psicose 3-epimerase and biotransformation of fruit and vegetable residues for d-psicose production. The study established that N-terminal fusion of a yeast homolog of SUMO protein - Smt3 - can confer elevated optimal temperature and improved operational stability to d-psicose 3-epimerase.
Sudhir P Singh, Satya Narayan Patel
exaly +3 more sources
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.
Zhenhong Yuan, Cuiyi Liang, Tao Yuan
exaly +3 more sources
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.
Zhenhong Yuan, Cuiyi Liang, Tao Yuan
exaly +3 more sources
Journal of Bioscience and Bioengineering, 2016
The specific activity of recombinant Escherichia coli cells expressing the double-site variant (I33L-S213C) d-psicose 3-epimerase (DPEase) from Agrobacterium tumefaciens was highest at 24 h of cultivation time in Terrific Broth (TB) medium among the media tested.
Chang-Su Park +2 more
exaly +3 more sources
The specific activity of recombinant Escherichia coli cells expressing the double-site variant (I33L-S213C) d-psicose 3-epimerase (DPEase) from Agrobacterium tumefaciens was highest at 24 h of cultivation time in Terrific Broth (TB) medium among the media tested.
Chang-Su Park +2 more
exaly +3 more sources
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
openaire +1 more source
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
openaire +1 more source
International Journal of Biological Macromolecules, 2021
The combined catalysis of glucose isomerase (GI) and D-psicose 3-epimerase (DPEase) provided a convenient route for the direct synthesis of D-allulose from d-glucose, whose cost is lower than d-fructose. In the present research, the weak activity of DPEase was the key rate-limiting step and resulted in the accumulation of d-fructose in engineered ...
Jingyi, Zhao +5 more
openaire +2 more sources
The combined catalysis of glucose isomerase (GI) and D-psicose 3-epimerase (DPEase) provided a convenient route for the direct synthesis of D-allulose from d-glucose, whose cost is lower than d-fructose. In the present research, the weak activity of DPEase was the key rate-limiting step and resulted in the accumulation of d-fructose in engineered ...
Jingyi, Zhao +5 more
openaire +2 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, Mu Wanmeng
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, Mu Wanmeng
exaly +3 more sources
Process Biochemistry, 2021
Abstract Functional mature proteins usually undergo folding, and in vivo folding is often affected by factors such as translation ratio, intracellular environment, and chaperones. d -psicose 3-epimerase (DPEase) derived from Dorea sp. has excellent properties in catalytic production of d -allulose; a rare sugar with unique biological functions ...
Jing Chen +5 more
openaire +1 more source
Abstract Functional mature proteins usually undergo folding, and in vivo folding is often affected by factors such as translation ratio, intracellular environment, and chaperones. d -psicose 3-epimerase (DPEase) derived from Dorea sp. has excellent properties in catalytic production of d -allulose; a rare sugar with unique biological functions ...
Jing Chen +5 more
openaire +1 more source