Results 11 to 20 of about 29,402,319 (134)

Safety evaluation of the food enzyme d‐psicose 3‐epimerase from the genetically modified Escherichia coli strain K‐12 W3110‐TKO CDX‐088 [PDF]

open access: yesEFSA Journal
The food enzyme d‐psicose 3‐epimerase (EC 5.1.3.30) is produced with the genetically modified Escherichia coli strain K‐12 W3110‐TKO CDX‐088 by Tate & Lyle Ingredients France SAS.
EFSA Panel on Food Enzymes (FEZ)   +16 more
doaj   +3 more sources

Safety evaluation of the food enzyme preparation D‐psicose 3‐epimerase from the non‐genetically modified Microbacterium foliorum strain SYG27B [PDF]

open access: yesEFSA Journal
This assessment addresses a food enzyme preparation consisting of the immobilised non‐viable cells of the non‐genetically modified bacterium identified by the applicant (Samyang Corporation) as Microbacterium foliorum strain SYG27B.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +24 more
doaj   +3 more sources

Enhanced Thermostability of D-Psicose 3-Epimerase from Clostridium bolteae through Rational Design and Engineering of New Disulfide Bridges. [PDF]

open access: yesInt J Mol Sci, 2021
D-psicose 3-epimerase (DPEase) catalyzes the isomerization of D-fructose to D-psicose (aka D-allulose, a low-calorie sweetener), but its industrial application has been restricted by the poor thermostability of the naturally available enzymes. Computational rational design of disulfide bridges was used to select potential sites in the protein structure
Zhao J   +5 more
europepmc   +5 more sources

A Possible Mechanism of Graphene Oxide to Enhance Thermostability of D-Psicose 3-Epimerase Revealed by Molecular Dynamics Simulations. [PDF]

open access: yesInt J Mol Sci, 2021
Thermal stability is a limiting factor for effective application of D-psicose 3-epimerase (DPEase) enzyme. Recently, it was reported that the thermal stability of DPEase was improved by immobilizing enzymes on graphene oxide (GO) nanoparticles. However, the detailed mechanism is not known.
Li C   +5 more
europepmc   +5 more sources

Safety evaluation of the food enzyme d‐tagatose 3‐epimerase from the genetically modified Escherichia coli strain PS‐Sav‐001 [PDF]

open access: yesEFSA Journal, 2023
The food enzyme d‐tagatose 3‐epimerase (EC 5.1.3.31) is produced with the genetically modified Escherichia coli strain PS‐Sav‐001 by SAVANNA Ingredients GmbH. The genetic modifications do not give rise to safety concerns.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +23 more
doaj   +3 more sources

Adaptive Steered Molecular Dynamics Combined With Protein Structure Networks Revealing the Mechanism of Y68I/G109P Mutations That Enhance the Catalytic Activity of D-psicose 3-Epimerase From Clostridium Bolteae [PDF]

open access: yesFrontiers in Chemistry, 2018
The scarcity, richness, and other important physiological functions of D-psicose make it crucial to increase the yield of D-psicose. The production of D-psicose can be accomplished by D-psicose 3-epimerase (DPEase) from Clostridium bolteae (CbDPEase ...
Jingxuan Zhu   +6 more
doaj   +4 more sources

Biochemical analysis and the preliminary crystallographic characterization of d-tagatose 3-epimerase from Rhodobacter sphaeroides

open access: yesMicrobial Cell Factories, 2017
Background d-Tagatose 3-epimerase epimerizes d-fructose to yield d-psicose, which is a rare sugar that exists in small quantities in nature and is difficult to synthesize chemically.
Zhengliang Qi   +7 more
doaj   +2 more sources

Preparation of a Flower-Like Immobilized D-Psicose 3-Epimerase with Enhanced Catalytic Performance [PDF]

open access: yesCatalysts, 2018
In this present study, we proposed a smart biomineralization method for creating hybrid organic–inorganic nanoflowers using a Co2+-dependent enzyme (D-psicose 3-epimerase; DPEase) as the organic component and cobalt phosphate as the inorganic component. The prepared nanoflowers have many separated petals that have a nanometer size.
Zheng, Lu   +6 more
openaire   +2 more sources

Correction: Characterization of a Novel Metal-Dependent D-Psicose 3-Epimerase from 35704.

open access: yesPLoS ONE, 2014
Figure 2 in the article, which reports the overexpression and purification of Clostridium scindens DPEase (previously named D-tagatose 3-epimerase) is duplicate from the authors' publication in Food and Fermentation Industries below: Xing Q, Mu W, Jiang B, Zhou L, Zhang T (2011) Cloning, expression, purification and characterization of D-tagatose 3 ...
Wenli Zhang   +5 more
doaj   +3 more sources

Optimization of fermentation conditions for whole cell catalytic synthesis of D-allulose by engineering Escherichia coli [PDF]

open access: yesScientific Reports
D-allulose/D-psicose is a significant rare sugar with broad applications in the pharmaceutical, food, and other industries. In this study, we cloned the D-allulose 3-epimerase (DPEase) gene from Arthrobacter globiformis M30, using pET22b as the vector ...
Haoran Liu   +12 more
doaj   +2 more sources

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