Construction of hyperthermostable d‐allulose 3‐epimerase from Arthrobacter globiformis M30 using the sequence information from Arthrobacter psychrolactophilus [PDF]
d‐Allulose is one of the rare monosaccharides and is considered as a safe ingredient in foods. It can be enzymatically produced from d‐fructose by the enzyme d‐allulose 3‐epimerase.
Kensaku Shimada +3 more
doaj +5 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
Safety evaluation of the food enzyme d‐psicose 3‐epimerase from the genetically modified Escherichia coli strain K‐12 W3110‐TKO CDX‐088 [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‐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]
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
Safety evaluation of the food enzyme d‐tagatose 3‐epimerase from the genetically modified Escherichia coli strain PS‐Sav‐001 [PDF]
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
Growth‐Coupled Evolutionary Pressure Improving Epimerases for D‐Allulose Biosynthesis Using a Biosensor‐Assisted In Vivo Selection Platform [PDF]
Fast screening strategies that enable high‐throughput evaluation and identification of desired variants from diversified enzyme libraries are crucial to tailoring biocatalysts for the synthesis of D‐allulose, which is currently limited by the poor ...
Chao Li +5 more
doaj +3 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 +2 more sources
Crystal structure of a novel homodimeric l‐ribulose 3‐epimerase from Methylomonus sp.
d‐Allulose has potential as a low‐calorie sweetener which can suppress fat accumulation. Several enzymes capable of d‐allulose production have been isolated, including d‐tagatose 3‐epimerases.
Hiromi Yoshida +6 more
doaj +2 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 +2 more sources
Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta [PDF]
D-allulose, which is one of the important rare sugars, has gained significant attention in the food and pharmaceutical industries as a potential alternative to sucrose and fructose.
Yang Wang +8 more
doaj +3 more sources

