Results 31 to 40 of about 270 (119)

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

open access: yesShipin 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   +9 more
doaj   +2 more sources

Thermostable D-Allulose 3-Epimerase for Long-Term Food-Compatible Continuous Production Systems

open access: yesApplied Sciences
D-allulose is a rare sugar with promising applications in food and health industries, owing to its low caloric value and multiple health benefits.
Jiawei Cui, Yan Li, Ming Yan
doaj   +2 more sources

Production, purification, characterization, and safety evaluation of constructed recombinant D-psicose 3-epimerase [PDF]

open access: yesMicrobial Cell Factories
Background D-psicose 3-epimerase (DPEase) is a potential catalytic enzyme for D-psicose production. D-psicose, also known as D-allulose, is a low-calorie sweetener that has gained considerable attention as a healthy alternative sweetener due to its ...
Nisit Watthanasakphuban   +5 more
doaj   +2 more sources

Immobilization of d-allulose 3-epimerase into magnetic metal–organic framework nanoparticles for efficient biocatalysis [PDF]

open access: yesWorld Journal of Microbiology and Biotechnology, 2021
Abstract D-allulose is a rare low-calorie sugar that has many fundamental biological functions. D-allulose 3-epimerase from Agrobacterium tumefaciens (AT-DAEase) catalyzes the conversion of D-fructose to D-allulose. The enzyme has attracted considerable attention because of its mild catalytic properties.
Kai Xue   +5 more
openaire   +2 more sources

Review on D-Allulose: In vivo Metabolism, Catalytic Mechanism, Engineering Strain Construction, Bio-Production Technology

open access: yesFrontiers in Bioengineering and Biotechnology, 2020
Rare sugar D-allulose as a substitute sweetener is produced through the isomerization of D-fructose by D-tagatose 3-epimerases (DTEases) or D-allulose 3-epimerases (DAEases).
Suwei Jiang   +9 more
doaj   +1 more source

Reaction Engineering and Comparison of Electroenzymatic and Enzymatic ATP Regeneration Systems

open access: yesChemElectroChem, Volume 10, Issue 22, November 14, 2023., 2023
An electrochemically coupled ATP regeneration by pyruvate oxidase and acetate kinase for the phosphorylation of mevalonate was established and expanded by a polyphosphate kinase. The reaction was characterized and compared with other ATP regenerating systems in terms of the phosphate donor properties and biocatalytic metrics.
Regine Siedentop   +4 more
wiley   +1 more source

Food manufacturing processes and technical data used in the exposure assessment of food enzymes

open access: yesEFSA Journal, Volume 21, Issue 7, July 2023., 2023
Abstract Food enzymes are used for technical purposes in the production of food ingredients or foods‐as‐consumed. In the European Union, the safety of a food enzyme is evaluated by EFSA on the basis of a technical dossier provided by an applicant. Dietary exposure is an integral part of the risk assessment of food enzymes.
EFSA Panel on Food Contact Materials   +25 more
wiley   +1 more source

Improved Performance of D-Psicose 3-Epimerase by Immobilisation on Amino-Epoxide Support with Intense Multipoint Attachment

open access: yesFoods, 2021
D-allulose is an epimer of D-fructose at the C-3 position. With similar sweetness to sucrose and a low-calorie profile, D-allulose has been considered a promising functional sweetener.
Yifan Bu   +3 more
doaj   +1 more source

Research Progress on Efficient Biocatalytic Synthesis of D-Allulose(D-阿洛酮糖的高效生物催化合成研究进展) [PDF]

open access: yesShipin kexue jishu xuebao
D-allulose is a novel low-calorie rare sugar with special physiological functions, including blood sugar regulation and antioxidant effects. In present, the biological synthesis of D-allulose mainly utilized D-allulose 3-epimerase to catalyze the ...
QIN Huimin(秦慧民)   +4 more
doaj   +1 more source

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