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首页> 外文期刊>Journal of Hazardous Materials >Molecular cloning, purification and biochemical characterization of a novel pyrethroid-hydrolyzing carboxylesterase gene from Ochrobactrum anthropi YZ-1
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Molecular cloning, purification and biochemical characterization of a novel pyrethroid-hydrolyzing carboxylesterase gene from Ochrobactrum anthropi YZ-1

机译：拟南芥YZ-1拟除虫菊酯水解羧酸酯酶基因的分子克隆，纯化及生化特性

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摘要

Strain YZ-1 was isolated from activated sludge and identified as Ochrobactrum anthropi. This strain was capable of degrading pyrethroids pesticides, suggesting the presence of degrading enzymes. In the present study, a novel esterase gene pytZ was cloned from the genomic library of YZ-1 successfully. The pytZ contained an open reading frame of 606 bp encoding a pyrethroid-hydrolyzing carboxylesterase. Deduced amino acid sequence showed moderate identities (39-59%) with most homologous carboxylesterase, except a putative carboxylesterase from 0. anthropi ATCC 49188 with the highest identity of 85%. Phylo-genetic analysis revealed that PytZ belonged to esterase VI family. The gene pytZ showed no any sequence similarity with reported pyrethroid-hydrolyzing genes and was a new pyrethroid-degrading gene. PytZ was expressed in Escherichia coli BL21 (DE3) and purified using Ni-NTA Fast Start. PytZ was able to degrade various pyrethroids. The optimal temperature and pH were 35 ℃ and 7.5. This enzyme was very stable over a wide range of temperature and pH. No cofactors were required for enzyme activity. Broad substrate specificity, high enzyme activity, and the favorable stability make the PytZ a potential candidate for the detoxification of pyrethroid residues in biotechnological application.
机译：从活性污泥中分离出菌株YZ-1，并将其鉴定为人形O。该菌株能够降解拟除虫菊酯类农药，表明存在降解酶。本研究成功地从YZ-1基因组文库中克隆了一个新的酯酶基因pytZ。 pytZ包含一个606 bp的开放阅读框，编码拟除虫菊酯水解羧酸酯酶。推导的氨基酸序列显示出与大多数同源羧酸酯酶的中等同一性（39-59％），除了来自人类拟南芥ATCC 49188的推定的羧酸酯酶之外，其最高同源性为85％。系统发育分析表明PytZ属于酯酶VI家族。 pytZ基因与报道的拟除虫菊酯水解基因没有任何序列相似性，是一种新型的拟除虫菊酯降解基因。 PytZ在大肠杆菌BL21（DE3）中表达，并使用Ni-NTA Fast Start纯化。 PytZ能够降解各种拟除虫菊酯。最佳温度和pH分别为35℃和7.5。该酶在很宽的温度和pH范围内都非常稳定。酶活性不需要辅助因子。广泛的底物特异性，高酶活性和良好的稳定性使PytZ成为生物技术应用中拟除虫菊酯残基解毒的潜在候选者。

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  • 来源
    《Journal of Hazardous Materials》 |2012年第30期|p.206-212|共7页
  • 作者

    Yi Zhai; Kang Li; Jinlong Song; Yanhua Shi; Yanchun Yan;

  • 作者单位

    Laboratory of Biology. Graduate School, Chinese Academy of Agriculture Science, Beijing 100087, China;

    Laboratory of Biology. Graduate School, Chinese Academy of Agriculture Science, Beijing 100087, China;

    Laboratory of Biology. Graduate School, Chinese Academy of Agriculture Science, Beijing 100087, China;

    Laboratory of Biology. Graduate School, Chinese Academy of Agriculture Science, Beijing 100087, China;

    Laboratory of Biology. Graduate School, Chinese Academy of Agriculture Science, Beijing 100087, China;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    pyrethroids; biodegradation; carboxylesterase; genomic library;

    机译：拟除虫菊酯;生物降解羧酸酯酶基因组文库;

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