Secretory expression and characterization of a novel peroxiredoxin for zearalenone detoxification in Saccharomyces cerevisiae

文献类型： 外文期刊

第一作者： Wu, Hui

作者： Wu, Hui;Yu, Yuanshan

作者机构：

关键词： Secretory expression;Zearalenone;Detoxification;Peroxiredoxin

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： 2013 年 168 卷 1 期

页码：

收录情况： SCI

摘要： Zearalenone (ZEN) is a Fusarium mycotoxin, which is considered to be an oestrogenic endocrine disruptor found to cause severe morphological and functional disorders of reproductive organs in livestock. Increasing attention has been paid to the development of an effective strategy for ZEN decontamination. ZEN is oxidized into smaller estrogenic metabolites by a novel peroxiredoxin (Prx) isolated from Acinetobacter sp. SM04. The Prx coding gene was cloned in a secretory vector pYES2-alpha (pY alpha) with an alpha (alpha) signal peptide gene inserted into the multiple cloning site of pYES2. The recombinant Prx was secreted from Saccharomyces cerevisiae INVSc1 after inducing with 2% (w/v) galactose for 72 h, and was found to be nearly 20 kDa through 12% SDS-PAGE. The expressed amount of recombinant Prx was 0.24 mg/mL in the extracellular supernatant. Recombinant Prx showed a gradient increase at the beginning of ZEN degradation. The final ZEN degradation amount was 0.43 mu g by one unit recombinant Prx after 12 h. Furthermore, the temperature, H2O2 concentration, and pH for highest peroxidase activity of recombinant Prx were 80 degrees C, 20 mM and 9.0, respectively. When compared with other peroxidases, the thermal stability and alkali resistance of recombinant Prx were much better. The results suggest that recombinant Prx is successfully expressed in S. cerevisiae. (C) 2012 Elsevier GmbH. All rights reserved.

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