Cloning, expression of a peroxiredoxin gene from Acinetobacter sp SM04 and characterization of its recombinant protein for zearalenone detoxification

文献类型： 外文期刊

第一作者： Yu, Yuanshan

作者： Yu, Yuanshan;Wu, Hui;Yu, Yuanshan;Wu, Hui;Tang, Yuqian;Qiu, Liping

作者机构：

关键词： Cloning;Expression;Peroxiredoxin;Decontamination;Zearalenone;Acinetobacter sp.

期刊名称：MICROBIOLOGICAL RESEARCH （ 影响因子：5.415； 五年影响因子：6.038 ）

ISSN： 0944-5013

年卷期： 2012 年 167 卷 3 期

页码：

收录情况： SCI

摘要： Zearalenone (ZEN) is a Fusarium mycotoxin, which has been associated with hyperestrogenism and other reproductive disorders in farm animals. ZEN-contaminated grains as well as its by-products had engendered numerous economic losses to farm animals' production, so the detoxification of ZEN-contaminated grains and its by-products would be necessary and beneficial. In this study, a peroxiredoxin (Prx) gene from Acinetobacter sp. SM04 was cloned, and over-expressed in Escherichia coli BL21 (DE3). The Prx gene of Acinetobacter sp. SM04 encodes a protein of 187 amino acids residues and NCBI BLAST program analysis of deduced amino acids shows high identity with 2-Cys Prx family. Interestingly, recombinant Prx show efficient ability to degrade ZEN using H2O2. Results of MCF-7 cell proliferation assay also found ZEN were oxidized into little estrogenic metabolites by purified recombinant Prx plus H2O2. Further, model experiments on decontamination of ZEN-contaminated corn using recombinant Prx were performed, and results found nearly 90% of ZEN was degraded when crushed ZEN-contaminated corn samples (nearly 1000 mu g ZEN per kg grain) were treated with purified recombinant Prx plus 0.09% (m/m) H2O2 for 6 h at 30 degrees C. In addition, the optimum pH and temperature of purified recombinant Prx for ZEN degradation were 9.0 and 70 degrees C respectively. (C) 2011 Elsevier GmbH. All rights reserved.

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