A quinone-dependent dehydrogenase and two NADPH-dependent aldo/keto reductases detoxify deoxynivalenol in wheat via epimerization in a Devosia strain

文献类型： 外文期刊

第一作者： He, Wei-Jie

作者： He, Wei-Jie;Shi, Meng-Meng;Yang, Peng;Huang, Tao;Zhao, Yue;Li, He-Ping;Zhang, Jing-Bo;Liao, Yu-Cai;He, Wei-Jie;Shi, Meng-Meng;Yang, Peng;Dong, Wu-Bei;Zhang, Jing-Bo;Liao, Yu-Cai;Huang, Tao;Zhao, Yue;Li, He-Ping;Wu, Ai-Bo

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关键词： Deoxynivalenol epimerization; Enzymatic detoxification; Alcohol dehydrogenase; Aldo/keto reductases; Molecular docking

期刊名称：FOOD CHEMISTRY （ 影响因子：7.514； 五年影响因子：7.516 ）

ISSN： 0308-8146

年卷期： 2020 年 321 卷

页码：

收录情况： SCI

摘要： The Fusarium mycotoxin deoxynivalenol (DON) is typically controlled by fungicides. Here, we report DON detoxification using enzymes from the highly active Devosia strain D6-9 which degraded DON M 2.5 mu g/min/10(8) cells. Strain D6-9 catabolized DON to 3-keto-DON and 3-epi-DON, completely removing DON in wheat. Genome analysis of three Devosia strains (D6-9, D17, and D13584), with strain D6-9 transcriptomes, identified three genes responsible for DON epimerization. One gene encodes a quinone-dependent DON dehydrogenase QDDH which oxidized DON into 3-keto-DON. Two genes encode the NADPH-dependent aldo/keto reductases AKR13B2 and AKR6D1 that convert 3-keto-DON into 3-epi-DON. Recombinant proteins expressed in Escherichia coll. efficiently degraded DON in wheat grains. Molecular docking and site-directed mutagenesis revealed that residues S497, E499, and E535 function in QDDH's DON-oxidizing activity. These results advance potential microbial and enzymatic elimination of DON in agricultural samples and lend insight into the underlying mechanisms and molecular evolution of DON detoxification.

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