漆酶
多铜氧化酶
玉米赤霉烯酮
化学
链霉菌
黄曲霉毒素
生物转化
真菌毒素
生物化学
阿布茨
生物降解
酶
微生物学
生物
食品科学
有机化学
细菌
抗氧化剂
遗传学
DPPH
作者
Xing Qin,Yanzhe Xin,Jiahuan Zou,Xiaoyun Su,Li Wang,Yaru Wang,Jie Zhang,Tao Tu,Bin Yao,Huiying Luo,Huoqing Huang
出处
期刊:Toxins
[MDPI AG]
日期:2021-10-24
卷期号:13 (11): 754-754
被引量:30
标识
DOI:10.3390/toxins13110754
摘要
Multicopper oxidases (MCOs) are a diverse group of enzymes that could catalyze the oxidation of different xenobiotic compounds, with simultaneous reduction in oxygen to water. Aside from laccase, one member of the MCO superfamily has shown great potential in the biodegradation of mycotoxins; however, the mycotoxin degradation ability of other MCOs is uncertain. In this study, a novel MCO-encoding gene, StMCO, from Streptomyces thermocarboxydus, was identified, cloned, and heterologously expressed in Escherichia coli. The purified recombinant StMCO exhibited the characteristic blue color and bivalent copper ion-dependent enzyme activity. It was capable of oxidizing the model substrate ABTS, phenolic compound DMP, and azo dye RB5. Notably, StMCO could directly degrade aflatoxin B1 (AFB1) and zearalenone (ZEN) in the absence of mediators. Meanwhile, the presence of various lignin unit-derived natural mediators or ABTS could significantly accelerate the degradation of AFB1 and ZEN by StMCO. Furthermore, the biological toxicities of their corresponding degradation products, AFQ1 and 13-OH-ZEN-quinone, were remarkably decreased. Our findings suggested that efficient degradation of mycotoxins with mediators might be a common feature of the MCOs superfamily. In summary, the unique properties of MCOs make them good candidates for degrading multiple major mycotoxins in contaminated feed and food.
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