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Chaperone-mediated protein folding enhanced D-psicose 3-epimerase expression in engineered Bacillus subtilis

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
semanticscholar   +2 more sources

Production of d-psicose from d-glucose by co-expression of d-psicose 3-epimerase and xylose isomerase.

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
semanticscholar   +3 more sources

Production of d-allose from d-fructose using immobilized l-rhamnose isomerase and d-psicose 3-epimerase

Bioprocess and Biosystems Engineering, 2019
D-Allose is a rare sugar, can be used as an ingredient in a range of foods and dietary supplements, has alimentary activities, especially excellent anti-cancer effects and used in assisting cancer chemotherapy and radiotherapy, etc. To develop a simple and low-cost process for D-allose production, a one-pot enzymatic process using the substrate of D ...
Can Li   +6 more
semanticscholar   +3 more sources

Cloning, expression, and characterization of a D-psicose 3-epimerase from Clostridium cellulolyticum H10.

Journal of Agricultural and Food Chemistry, 2011
The noncharacterized protein ACL75304 encoded by the gene Ccel_0941 from Clostridium cellulolyticum H10 (ATCC 35319), previously proposed as the xylose isomerase domain protein TIM barrel, was cloned and expressed in Escherichia coli . The expressed enzyme was purified by nickel-affinity chromatography with electrophoretic homogeneity and then ...
W. Mu   +5 more
semanticscholar   +3 more sources

Improved operational stability of d-psicose 3-epimerase by a novel protein engineering strategy, and d-psicose production from fruit and vegetable residues.

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.
S. Patel   +6 more
semanticscholar   +3 more sources

A stable immobilized d-psicose 3-epimerase for the production of d-psicose in the presence of borate

Process Biochemistry, 2009
Abstract 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 ...
B. Lim, Hye‐Jung Kim, D. Oh
semanticscholar   +2 more sources

Co-expression of D-glucose isomerase and D-psicose 3-epimerase: development of an efficient one-step production of D-psicose.

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   +5 more
semanticscholar   +3 more sources

Production of d-psicose from d-fructose by whole recombinant cells with high-level expression of d-psicose 3-epimerase from Agrobacterium tumefaciens.

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   +3 more
semanticscholar   +3 more sources

Mutational analysis of the active site residues of a d-psicose 3-epimerase from Agrobacterium tumefaciens

Biotechnology Letters, 2010
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
semanticscholar   +3 more sources

Immobilization on graphene oxide improves the thermal stability and bioconversion efficiency of D-psicose 3-epimerase for rare sugar production.

Enzyme and Microbial Technology, 2017
D-Psicose (D-ribo-2-hexulose or D-allulose), an epimer of D-fructose is considered as a rare low-calorie sugar displaying important physiological functions. Enzymatic production using ketose 3-epimerases is the feasible process for the production of D-Psicose.
Samir R. Dedania   +4 more
semanticscholar   +3 more sources

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