Results 101 to 110 of about 1,864,743 (129)
Some of the next articles are maybe not open access.
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.
Yan Men, Yueming Zhu, Yan Zeng
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.
Yan Men, Yueming Zhu, Yan Zeng
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.
Satya Narayan Patel, Sudhir P Singh
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.
Satya Narayan Patel, Sudhir P Singh
exaly +3 more sources
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, Yan Men, Yuanxia Sun
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, Yan Men, Yuanxia Sun
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.
Xiaoyan Chen, Wen Wang, Jingliang Xu
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.
Xiaoyan Chen, Wen Wang, Jingliang Xu
exaly +3 more sources
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, Wenli Zhang, Leon Zhou
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
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