Purification and characterization of a cis-epoxysuccinic acid hydrolase from Bordetella sp strain 1-3
文献类型： 外文期刊
第一作者： Li, Xia
作者： Li, Xia;Lu, Hongbo;Ma, Xiaohang;Kai, Lei;Guo, Kangping;Zhao, Yuhua;Li, Xia;Xu, Tongcheng
作者机构：
关键词： cis-Epoxysuccinic acid hydrolase; Bordetella sp.; Purification; Enzyme characterization
期刊名称：PROTEIN EXPRESSION AND PURIFICATION （ 影响因子：1.65； 五年影响因子：1.548 ）
ISSN： 1046-5928
年卷期： 2010 年 69 卷 1 期
页码：
收录情况： SCI
摘要： Purification of a cis-epoxysuccinic acid hydrolase was achieved by ammonium sulfate precipitation, ionic exchange chromatography, hydrophobic interaction chromatography followed by size-exclusion chromatography. The enzyme was purified 177-fold with a yield of 14.4%. The apparent molecular mass of the enzyme was determined to be 33 kDa under denaturing conditions. The optimum pH for enzyme activity was 7.0, and the enzyme exhibited maximum activity at about 45 degrees C in 50 mM sodium phosphate buffer (pH 7.5). EDTA and o-phenanthrolin inhibited the enzyme activity remarkably, suggesting that the enzyme needs some metal cation to maintain its activity. Results of inductively coupled plasma mass spectrometry analysis indicated that the cis-epoxysuccinic acid hydrolase needs Zn2+ as a cofactor. Eight amino acids sequenced from the N-terminal region of the cis-epoxysuccinic acid hydrolase showed the same sequence as the N-terminal region of the beta subunit of the cis-epoxysuccinic acid hydrolase obtained from Alcaligenes sp. (C) 2009 Elsevier Inc. All rights reserved.
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