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Identification of a halophilic alpha-amylase gene from Escherichia coli JM109 and characterization of the recombinant enzyme.

机译:鉴定大肠杆菌JM109的嗜盐α-淀粉酶基因并鉴定重组酶。

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摘要

A halophilic alpha-amylase (EAMY) gene from Escherichia coli JM109 was overexpressed in E. coli XL10-Gold and the recombinant protein was purified and characterized. The activity of the EAMY depended on the presence of both Na+ and Cl-, and had maximum activity in 2 M NaCl at 55 degrees C and pH 7.0. When 2 % (w/v) soluble starch was used as substrate, the specific activity was about 1090 U mg-1 protein. This is the first report on identifying a halophilic alpha-amylase with high specific activity from non-halophilic bacteria
机译:来自大肠杆菌JM109的嗜盐α-淀粉酶(EAMY)基因在大肠杆菌XL10-Gold中过表达,纯化并鉴定了重组蛋白。 EAMY的活性取决于Na + 和Cl -的存在,并且在55°C和pH 7.0的2 M NaCl中具有最大活性。以2%(w / v)可溶性淀粉为底物,比活度约为1090 U mg -1 蛋白。这是关于从非嗜盐菌中鉴定具有高比活性的嗜盐α-淀粉酶的第一份报告

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