A novel short‐chain dehydrogenase/reductase catalyzing efficient patulin detoxification: identification and computational characterization

The acidic pH preference of LmSDR indicates its optimal activity under mildly acidic conditions, highlighting its potential as a biocatalyst for applications in acidic food matrices. Moreover, computer-aided approaches offer a theoretical framework for elucidating the proton transfer mechanism of LmSDR and other PAT-degrading SDRs. © 2025 Society of Chemical Industry.

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Publication Details

Journal
Journal of the Science of Food and Agriculture
Published
2025-09-22
DOI
https://doi.org/10.1002/jsfa.70213
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
Field-Weighted Citation Impact
0.00
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article

A novel short‐chain dehydrogenase/reductase catalyzing efficient patulin detoxification: identification and computational characterization

Binbin Ouyang, Junmei Ding, Cuie Guang, Wei Xu et al.
Journal of the Science of Food and Agriculture
Enzyme Catalysis and Immobilization
article

A novel short‐chain dehydrogenase/reductase catalyzing efficient patulin detoxification: identification and computational characterization

Binbin Ouyang, Junmei Ding, Cuie Guang, Wei Xu, Wanmeng Mu, Wenli Zhang
article en

Abstract

The acidic pH preference of LmSDR indicates its optimal activity under mildly acidic conditions, highlighting its potential as a biocatalyst for applications in acidic food matrices. Moreover, computer-aided approaches offer a theoretical framework for elucidating the proton transfer mechanism of LmSDR and other PAT-degrading SDRs. © 2025 Society of Chemical Industry.

Journal of the Science of Food and AgricultureVol. 106(2)
Jiangnan University (CN), Yunnan Normal University (CN), State Key Laboratory of Food Science and Technology (CN)
Openalex Percentile: Top 77%
Enzyme Catalysis and Immobilization
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