Abstract
This study cloned a new amidase signature (AS) family gene from Escherichia coli (E. coii), and mainly investigated the activity of this enzyme. The protein, according to the bioinformatics analysis, belonged to the AS family. It was expressed, purified and characterized in E. coli BL21 (DE3). As a result, 40 °C and pH 8.0 were the optimum temperature and pH. It showed a wide substrate spectrum and high activity for aromatic and aliphatic amides, while with a narrow range of anilide substrate, and only propanol could be adopted as an effective substrate. Because of its wide range of substrate specificities, this will boost the applicability of amidase and make it have the potential for a wide range of applications in biosynthesis and biodegradation.
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