A Whole-Cell Catalytic System for Equol Production Based on Daidzein Reductase Engineering.

Bing-Juan Li, Jiao-Jiao Zhuo, Meng-Ran Tian, Dan Meng, Hong-Yan Li

Abstract read

In one paragraph

Article in Molecules (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

5 authors.

Bing-Juan LiTianjin Key Laboratory of Food and Biotechnology, Department of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China.ORCID 0000-0003-1484-5728

Jiao-Jiao ZhuoTianjin Key Laboratory of Food and Biotechnology, Department of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China.ORCID 0009-0000-5184-667X

Meng-Ran TianTianjin Key Laboratory of Food and Biotechnology, Department of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China.

Dan MengTianjin Key Laboratory of Food and Biotechnology, Department of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China.

Hong-Yan LiTianjin Key Laboratory of Food and Biotechnology, Department of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China.ORCID 0000-0001-7897-5308

Funding

National Natural Science Foundation of China 31801471

6 · The paper itself

Abstract

As an isoflavone metabolite with diverse physiological activities, the development of efficient and sustainable manufacturing technologies for (S)-equol holds significant importance. This study focuses on the semi-rational design of daidzein reductase (DZNR), the first key enzyme in the (S)-equol biotransformation pathway. Through multiple sequence alignment and three-dimensional structural analysis, two critical residues, Gly30 and Ala105, were identified in DZNR. A library of single and combinatorial mutants was constructed and screened, yielding the double variant DZNR30S+105S with substantially enhanced catalytic performance. In a whole-cell biocatalytic system, the recombinant

Indexed as

EquolIsoflavonesOxidoreductasesProtein EngineeringBiocatalysisEscherichia coliModels, MolecularMutagenesis, Site-DirectedMutationSubstrate SpecificitydaidzeinEquolIsoflavonesOxidoreductasesdaidzein reductaseenzyme engineeringsemi-rational design(S)-equolsite-directed mutagenesissoy isoflavones

Identifiers

PMID41752488

DOI10.3390/molecules31040711

PMCPMC12943075

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LicenceCC BY

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.