Identification of a Bacillus amyloliquefaciens H6 Thioesterase Involved in Zearalenone Detoxification by Transcriptomic Analysis

玉米赤霉烯酮 解淀粉芽孢杆菌 小桶 大肠杆菌 生物 转录组 硫酯酶 食品科学 真菌毒素 生物化学 生物合成 基因 发酵 基因表达
作者
Laipeng Xu,Xiangli Sun,Xianhua Wan,Hui Li,Fengbin Yan,Ruili Han,Hong Li,Zhuanjian Li,Yadong Tian,Xiaojun Liu,Xiangtao Kang,Yanbin Wang
出处
期刊:Journal of Agricultural and Food Chemistry [American Chemical Society]
卷期号:68 (37): 10071-10080 被引量:20
标识
DOI:10.1021/acs.jafc.0c03954
摘要

Zearalenone (ZEA), a nonsteroidal estrogenic mycotoxin produced by Fusarium graminearum, induces hyperestrogenic responses in mammals and can cause reproductive disorders in farm animals. In this study, a transcriptome analysis of Bacillus amyloliquefaciens H6, which was previously identified as a ZEA-degrading bacterium, was conducted with high-throughput sequencing technology, and the differentially expressed genes were subjected to gene ontology (GO) and kyoto encyclopedia of genes and genomes (KEGG) enrichment analyses. Among the 16 upregulated genes, BAMF_RS30125 was predicted to be the key gene responsible for ZEA degradation. The protein encoded by BAMF_RS30125 was then expressed in Escherichia coli, and this recombinant protein (named ZTE138) significantly reduced the ZEA content, as determined by the enzyme-linked immunosorbent assay (ELISA) and high-performance liquid chromatography (HPLC), and decreased the proliferating activity of ZEA in MCF-7 cells. What is more, the liquid chromatography–tandem mass spectrometry (LC–MS/MS) results showed that the relative molecular mass and the structure of ZEA also changed. Sequence alignment of the ZTE138 protein showed that it is a protease that belongs to the YBGC/FADM family of coenzyme A thioesterases, and thus, the protein can presumably cleave the ZEA lactone bond and break down its macrolide ring.
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