Degradation of zearalenone and aflatoxin B1 by Lac2 from Pleurotus pulmonarius in the presence of mediators

被引:44
|
作者
Song, Yanyi [1 ,2 ]
Wang, Yanan [1 ]
Guo, Yongpeng [1 ]
Qiao, Yingying [3 ]
Ma, Qiugang [1 ]
Ji, Cheng [1 ]
Zhao, Lihong [1 ]
机构
[1] China Agr Univ, Coll Anim Sci & Technol, State Key Lab Anim Nutr, Beijing 100193, Peoples R China
[2] China Agr Univ, Coll Biol Sci, Beijing 100193, Peoples R China
[3] Sumy Natl Agr Univ, Fac Biol & Technol, Sumy, Ukraine
基金
中国国家自然科学基金;
关键词
Zearalenone; Aflatoxin B1; Lac2; laccase; Degradation; Laccase-mediator system; Pleurotus pulmonarius; IN-VITRO; BIOCHEMICAL-CHARACTERIZATION; LACCASE; PURIFICATION; MYCOTOXINS; EFFICIENCY; BACTERIAL; ENZYME;
D O I
10.1016/j.toxicon.2021.08.003
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
The contamination of foods and feeds with mycotoxins has been an issue of global significance. For mycotoxin detoxification, enzymatic biodegradation using laccase has received much attention. In this study, a laccase gene lac2 from the fungus Pleurotus pulmonarius was expressed in the Pichia pastoris X33 yeast strain to produce recombinant proteins. Enzymatic properties of recombinant Lac2 and its ability to degrade zearalenone (ZEN) and Aflatoxin B1 (AFB1) in the presence of four mediators (ABTS, TEMPO, AS and SA) were investigated. Result showed that the optimum pH and temperature of recombinant Lac2 were 3.5 and 55 degrees C, respectively. Lac2 was not sensitive to heat and stable under both acidic and alkaline conditions. Lac2-ABTS and Lac2-AS were efficient systems for ZEN degradation over a wide range of pH (4-8) and temperature (40-60 degrees C). Lac2-AS was the most efficient system for AFB1 degradation, reaching 99.82% of degradation at pH 7 and 37 degrees C after 1 h of incubation. Finally, the Lac2-mediator oxidation products were structurally characterized. This study lays a solid foundation for the application of Lac2 laccase combined with AS for degrading mycotoxin in food and feed.
引用
收藏
页码:1 / 8
页数:8
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