Degradation of Four Major Mycotoxins by Eight Manganese Peroxidases in Presence of a Dicarboxylic Acid
文献类型: 外文期刊
第一作者: Wang, Xiaolu
作者: Wang, Xiaolu;Qin, Xing;Hao, Zhenzhen;Luo, Huiying;Yao, Bin;Su, Xiaoyun;Qin, Xing
作者机构:
关键词: manganese peroxidase; mycotoxin; aflatoxin; zearalenone; deoxynivalenol; fumonisin; detoxification
期刊名称:TOXINS ( 影响因子:4.546; 五年影响因子:4.8 )
ISSN:
年卷期: 2019 年 11 卷 10 期
页码:
收录情况: SCI
摘要: Enzymatic treatment is an attractive method for mycotoxin detoxification, which ideally prefers the use of one or a few enzymes. However, this is challenged by the diverse structures and co-contamination of multiple mycotoxins in food and feed. Lignin-degrading fungi have been discovered to detoxify organics including mycotoxins. Manganese peroxidase (MnP) is a major enzyme responsible for lignin oxidative depolymerization in such fungi. Here, we demonstrate that eight MnPs from different lignocellulose-degrading fungi (five from Irpex lacteus, one from Phanerochaete chrysosporium, one from Ceriporiopsis subvermispora, and another from Nematoloma frowardii) could all degrade four major mycotoxins (aflatoxin B-1, AFB(1); zearalenone, ZEN; deoxynivalenol, DON; fumonisin B-1, FB1) only in the presence of a dicarboxylic acid malonate, in which free radicals play an important role. The I. lacteus and C. subvermispora MnPs behaved similarly in mycotoxins transformation, outperforming the P. chrysosporium and N. frowardii MnPs. The large evolutionary diversity of these MnPs suggests that mycotoxin degradation tends to be a common feature shared by MnPs. MnP can, therefore, serve as a candidate enzyme for the degradation of multiple mycotoxins in food and feed if careful surveillance of the residual toxicity of degradation products is properly carried out.
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