In vitro single and combined mycotoxins degradation by Ery4 laccase from Pleurotus eryngii and redox mediators

被引:80
作者
Loi, Martina [1 ,2 ]
Fanelli, Francesca [1 ]
Cimmarusti, Maria Teresa [1 ,2 ]
Mirabelli, Valentina [2 ,3 ]
Haidukowski, Miriam [1 ]
Logrieco, Antonio F. [1 ]
Caliandro, Rocco [3 ]
Mule, Giuseppina [1 ]
机构
[1] CNR, Inst Sci Food Prod, Via Amendola 122-O, I-70126 Bari, Italy
[2] Univ Foggia, Dept Econ, Via Napoli 25, I-71122 Foggia, Italy
[3] CNR, Inst Crystallog, Via Amendola 122-O, I-70126 Bari, Italy
基金
欧盟地平线“2020”;
关键词
Mycotoxins; Bioremediation; Laccase-Mediator System; Multi-mycotoxin degradation; LIQUID-CHROMATOGRAPHY; MAIZE; DECONTAMINATION; BIODEGRADATION; CONTAMINATION; OCHRATOXIN; ENZYME; WHEAT; B-1;
D O I
10.1016/j.foodcont.2018.02.032
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Mycotoxin contamination of staple food commodities is a relevant health and economic issue worldwide. The development of green and effective reduction strategies to counteract the contamination by multiple mycotoxins has become an urgent need. The aim of this work was to evaluate the capability of a laccase (LC) from Pleurotus eryngii and a laccase-mediator systems (LMSs) to degrade aflatoxin B-1 (AFE(1)), fumonisin (FB1), ochratoxin A (OTA), deoxynivalenol (DON), Zearalenone (ZEN) and T-2 toxin in in vitro assays. In addition, the simultaneous mycotoxin degradation capability with selected LMSs was evaluated with combinations of AFB(1) and ZEN, and FB1 and T-2 toxin. Redox mediators were found to drastically increasethe degradation efficiencies of the enzyme. AFB(1), FBI, OTA, ZEN and T-2 toxin degradation by the best performing LMS were 73%, 74%, 27%, 100% and 40%, respectively. No degradation was registered for DON. Notably, AFB(1) and ZEN were simultaneously degraded by 86% and 100%, while FB1 and T-2 by 25% and 100%, respectively. LMS proved to be a promising approach to enhance degradation properties of LC enzymes and for the potential development of a multi-mycotoxin reducing method. (C) 2018 The Authors. Published by Elsevier Ltd.
引用
收藏
页码:401 / 406
页数:6
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