| Autor: |
Xu, Laipeng, Sun, Xiangli, Wan, Xianhua, Li, Hui, Yan, Fengbin, Han, Ruili, Li, Hong, Li, Zhuanjian, Tian, Yadong, Liu, Xiaojun, Kang, Xiangtao, Wang, Yanbin |
| Zdroj: |
Journal of Agricultural and Food Chemistry; September 2020, Vol. 68 Issue: 37 p10071-10080, 10p |
| Abstrakt: |
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 amyloliquefaciensH6, 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. |
| Databáze: |
Supplemental Index |
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