Cloning, sequencing, and expression of a novel epoxide hydrolase gene from Rhodococcus opacus in Escherichia coli and characterization of enzyme

文献类型： 外文期刊

第一作者： Liu, Zhiqiang

作者： Liu, Zhiqiang;Li, Yin;Xu, Yingying;Ping, Lifeng;Zheng, Yuguo

作者机构：

关键词： cloning;prokaryotic expression;epoxide hydrolase;rhodococcus opacus ML-0004;characterization;DIRECTED EVOLUTION;ASPERGILLUS-NIGER;BACTERIAL-CELLS;ENCODING GENE;PURIFICATION;RADIOBACTER;HYDROLYSIS;ACID

期刊名称：APPLIED MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：4.813； 五年影响因子：4.697 ）

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收录情况： SCI

摘要： An epoxide hydrolase gene of about 0.8 kb was cloned from Rhodococcus opacus ML-0004, and the open reading frame (ORF) sequence predicted a protein of 253 amino acids with a molecular mass of about 28 kDa. An expression plasmid carrying the gene under the control of the tac promotor was introduced into Escherichia coli, and the epoxide hydrolase gene was successfully expressed in the recombinant strains. Some characteristics of purified recombinant epoxide hydrolase were also studied. Epoxide hydrolase showed a high stereospecificity for L(+)-tartaric acid, but not for D(+)-tartaric acid. The epoxide hydrolase activity could be assayed at the pH ranging from 3.5 to 10.0, and its maximum activity was obtained between pH 7.0 and 7.5. The enzyme was sensitive to heat, decreasing slowly between 30 degrees C and 40 degrees C, and significantly at 45 degrees C. The enzyme activity was activated by Ca2+ and Fe2+, while strongly inhibited by Ag+ and Hg+, and slightly inhibited by Cu2+, Zn2+, Ba2+, Ni+, EDTA-Na-2 and fumarate.

分类号： Q93

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