Efficient Expression and Activity Optimization of Manganese Peroxidase for the Simultaneous Degradation of Aflatoxins AFB1, AFB2, AFG1, and AFG2

• 全文链接

锰过氧化物酶同时降解黄曲霉毒素AFB1、AFB2、AFG1和AFG2的高效表达及活性优化

关键词：

来源：

Journal of Agricultural and Food Chemistry

全文链接：

//agri.nais.net.cn/topic/downloadFile/fb176caa-a50b-48c5-ac02-7f7a5bca1244

来源地址：

https://pubs.acs.org/doi/10.1021/acs.jafc.4c10047

资源所属：

饲料用酶工程

类型：

学术文献

语种：

英语

原文发布日期：

2025-01-03

摘要：

Aflatoxins (AFs), notorious mycotoxins that pose significant risks to human and animal health, make biodegradation extremely crucial as they offer a promising approach to managing and reducing their harmful impacts. In this study, we identified a manganese peroxidase from Punctularia strigosozonata (PsMnp) through protein similarity analysis, which has the capability to degrade four AFs (AFB1, AFB2, AFG1, and AFG2) simultaneously. The gene encoding this enzyme was subject to codon optimization, followed by cold shock induction expression using the pColdII vector, leading to the soluble expression of manganese peroxidase (Mnp) in Escherichia coli. This study tackled the problem of inclusion body formation that often occurs during Mnp expression in E. coli. After optimizing the degradation conditions, the degradation rates for AFB1, AFB2, AFG1, and AFG2 were 87.9, 72.8, 77.3, and 85.6%, respectively. Molecular docking and molecular dynamics simulations indicated that PsMnp facilitated the degradation of AFs through hydrophobic and polar interactions among various amino acid residues. This research offers novel insights into the rapid discovery of enzymes capable of degrading AFs and establishes a theoretical foundation for the efficient expression of mycotoxin detoxification enzymes.