D-Allulose Production from D-Fructose by Permeabilized Recombinant Cells of Corynebacterium glutamicum Cells Expressing D-Allulose 3-Epimerase Flavonifractor plautii. [PDF]
A d-allulose 3-epimerase from Flavonifractor plautii was cloned and expressed in Escherichia coli and Corynebacterium glutamicum. The maximum activity of the enzyme purified from recombinant E.
Chul-Soon Park +5 more
doaj +7 more sources
Production of recombinant D-allulose 3-epimerase utilizing an auto-induction approach in fermentor cultures suitable for industrial application. [PDF]
D-Allulose 3-epimerase (DAEase) is the key enzyme catalyzing D-fructose to catalyze into D-allulose, a rare sugar in foods, which has lately drawn increasing worldwide attention owing to its possible health advantages and application as a substitute ...
Kenny Lischer +10 more
doaj +7 more sources
Optimization of Ultrahigh-Throughput Screening Assay for Protein Engineering of d-Allulose 3-Epimerase [PDF]
d-Allulose is the corresponding epimer of d-fructose at the C-3 position, which exhibits a similar taste and sweetness to sucrose. As a low-calorie sweetener, d-allulose has broad application prospects in the fields of medicine, food, and so on ...
Zhanzhi Liu +7 more
doaj +3 more sources
Efficient D-allulose synthesis under acidic conditions by auto-inducing expression of the tandem D-allulose 3-epimerase genes in Bacillus subtilis [PDF]
Background D-allulose, a hexulose monosaccharide with low calorie content and high sweetness, is commonly used as a functional sugar in food and nutrition.
Mengkai Hu +7 more
doaj +4 more sources
Optimization of fermentation conditions for whole cell catalytic synthesis of D-allulose by engineering Escherichia coli [PDF]
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 +3 more sources
Safety evaluation of the food enzyme d‐psicose 3‐epimerase from the genetically modified Corynebacterium glutamicum strain FIS002 [PDF]
This assessment addresses a food enzyme preparation consisting of the immobilised intact but non‐viable cells of the genetically modified Corynebacterium glutamicum strain FIS002 by CJ‐Tereos Sweeteners Europe SAS. The production strain produces the food
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP) +22 more
doaj +3 more sources
Biochemical characterization, structure-guided mutagenesis, and application of a recombinant D-allulose 3-epimerase from Christensenellaceae bacterium for the biocatalytic production of D-allulose [PDF]
D-Allulose has become a promising alternative sweetener due to its unique properties of low caloric content, moderate sweetness, and physiological effects. D-Allulose 3-epimerase (DAEase) is a promising enzyme for D-Allulose production.
Lijun Guan +22 more
doaj +4 more sources
Efficient Utilization of Fruit Peels for the Bioproduction of D-Allulose and D-Mannitol [PDF]
Currently, the demand for low-calorie sweeteners has grown dramatically because consumers are more mindful of their health than they used to be. Therefore, bioproduction of low-calorie sweeteners from low-cost raw materials becomes a hot spot.
Jin Li +5 more
doaj +3 more sources
Safety evaluation of the food enzyme d‐psicose 3‐epimerase from the genetically modified Escherichia coli strain K‐12 W3110 (pWKLP) [PDF]
The food enzyme d‐psicose 3‐epimerase (EC 5.1.3.30) is produced with the genetically modified Escherichia coli strain K‐12 W3110 (pWKLP) by Matsutani Chemical Industry Co., Ltd.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP) +24 more
doaj +3 more sources
Comprehensive Analysis of Allulose Production: A Review and Update [PDF]
Advancements in D-allulose production have seen significant strides in recent years, focusing on enzymatic conversion methods. Key developments include traditional immobilization techniques, the discovery of novel enzymes, directed evolution studies, and
Lei Wang +3 more
doaj +3 more sources

