Results 11 to 20 of about 408 (142)

Construction of hyperthermostable d‐allulose 3‐epimerase from Arthrobacter globiformis M30 using the sequence information from Arthrobacter psychrolactophilus [PDF]

FEBS Open Bio
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, Kouhei Ohtani, Pushpa Kiran Gullapalli, Kazuhiko Ishikawa   +3 more
doaj   +5 more sources

Crystal structure of a novel homodimeric l‐ribulose 3‐epimerase from Methylomonus sp. [PDF]

FEBS Open Bio, 2021
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, Akihide Yoshihara, Shiro Kato, Susumu Mochizuki, Kazuya Akimitsu, Ken Izumori, Shigehiro Kamitori   +6 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]

EFSA 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), Holger Zorn, José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize L. M. Solano, Henk Van Loveren, Laurence Vernis, Silvia Peluso, Cristina Fernández‐Fraguas, Jeroen Pasch, Yi Liu   +16 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]

EFSA 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), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Boet Glandorf, Lieve Herman, Magdalena Andryszkiewicz, Ana Gomes, Yi Liu, Silvia Peluso, Andrew Chesson   +23 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]

EFSA 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), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Magdalena Andryszkiewicz, Laura Sanmartin Cabo, Ana Criado, Cristina Fernàndez‐Fraguas, Yi Liu, Silvia Peluso, Rita Ferreira de Sousa, Andrew Chesson   +24 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]

Frontiers in Bioengineering and Biotechnology
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, Lijun Guan, Ling Zhu, Ling Zhu, Kunlun Wang, Kunlun Wang, Yang Gao, Yang Gao, Jialei Li, Jialei Li, Song Yan, Song Yan, Xindi Zhang, Xindi Zhang, Nina Ji, Jing Fan, Jing Fan, Ye Zhou, Ye Zhou, Xinmiao Yao, Xinmiao Yao, Bo Li, Bo Li   +22 more
doaj   +4 more sources

Ancestral Sequence Reconstruction Enhances Thermal Stability of D-Allulose 3-Epimerase [PDF]

Shipin gongye ke-ji
To solve the problem of poor thermal stability of the current D-allulose 3-epimerase (DAEase), the ancestor sequences of DAEase with different catalytic domains were reconstructed by big data mining, reasonable modification and ancestor sequence ...
Lijun GUAN, Ling ZHU, Kunlun WANG, Jialei LI, Yang GAO, Song YAN, Xindi ZHANG, Qing CHEN, Nina JI, Bo LI   +9 more
doaj   +4 more sources

Growth‐Coupled Evolutionary Pressure Improving Epimerases for D‐Allulose Biosynthesis Using a Biosensor‐Assisted In Vivo Selection Platform [PDF]

Advanced Science
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, Xin Gao, Huimin Li, Tong Wang, Fuping Lu, Hui‐Min Qin   +5 more
doaj   +3 more sources

Efficient Utilization of Fruit Peels for the Bioproduction of D-Allulose and D-Mannitol [PDF]

Foods, 2022
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, Jiajun Chen, Wei Xu, Wenli Zhang, Yeming Chen, Wanmeng Mu   +5 more
doaj   +2 more sources

Recent Advances Regarding the Physiological Functions and Biosynthesis of D-Allulose [PDF]

Frontiers in Microbiology, 2022
D-Allulose, a generally regarded as safe (GRAS) sugar, is rare in nature. It is among the most promising sweeteners for future use due to its low caloric content, sucrose-like taste, and unique functions.
Zhou Chen, Xiao-Dong Gao, Zijie Li
doaj   +2 more sources