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Functional Characterization and Mechanism of Two Zearalenone-Degrading Enzymes from Bacillus velezensis B.26

文献类型： 外文期刊

作者： Wei, Zifan;Zhang, Xinyue;Shi, Lingfang;Jin, Jing;Yang, Bolei;Xing, Fuguo

作者机构：

关键词： zearalenone;Bacillus velezensis;Degradation enzyme;Degradation products;Enzyme characteristics

期刊名称： JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

ISSN： 0021-8561

年卷期： 2025 年

页码：

收录情况： SCIE（2025版） ; ; EI（2025版）

摘要： Mycotoxins threaten human and animal health, necessitating effective detoxification strategies. This study demonstrated that Bacillus velezensis B.26 efficiently degraded zearalenone (ZEN), achieving 91.64% reduction at 70 degrees C within 24 h. After verification, the degradation active components were found to mainly exist in the fermentation supernatant, which was sensitive to metal ions. Under treatment with proteinase K and sodium dodecyl sulfate, the degradation activity was significantly reduced, but it was not affected by heating treatment. Genome mining revealed two candidate genes, a laccase with 66.12% amino acid sequence agreement with CotA from Bacillus licheniformis and another with 42.65% amino acid sequence agreement with peroxiredoxin (Prx) from Acinetobacter nosocomialis. Heterologously expressed CotA (62 kDa) degraded 91.94% of 5 mu g/mL ZEN at 70 degrees C, pH 8.0, within 6 h, while Prx (22 kDa) eliminated 59.74% at pH 11.0 under identical thermal conditions. Na+, Cu2+, and K+ enhanced CotA activity, whereas Mn2+ inhibited both enzymes. LC-MS confirmed nontoxic degradation pathways yielding low-toxicity metabolites C17H24O4 and C12H16O4, without hazardous byproducts (alpha-ZEL/alpha-ZAL). These findings indicated that both enzymes have the potential to serve as detoxification agents in food and feed applications.

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