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 1 ; Zhang, Xinyue 2 ; Shi, Lingfang 1 ; Jin, Jing 2 ; Yang, Bolei 2 ; Xing, Fuguo 2 ;
作者机构： 1.Tianjin Univ Sci & Technol, Coll Food Sci & Engn, Tianjin 300457, Peoples R China
2.Chinese Acad Agr Sci, Inst Food Sci & Technol, Minist Agr & Rural Affairs, Key Lab Agroprod Qual & Safety Control Storage & T, Beijing 100193, Peoples R China
关键词：
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.2； 五年影响因子：6.4 ）
ISSN： 0021-8561
年卷期： 2025 年 73 卷 23 期
页码：
收录情况： SCI
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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