Cloning, Expression and Characterization of a Novel α-Amylase from Salinispora arenicola CNP193.

Cloning, Expression and Characterization of a Novel α-Amylase from Salinispora arenicola CNP193.

Liu, Shu;Ahmed, Sibtain;Fang, Yaowei;
the protein journal 2019
267
liu2019cloningthe

Abstract

α-Amylases are used in various biotechnological processes including the textile, paper, food, biofuels, detergents and pharmaceutical industries. In this study, a novel gene encoding α-amylase was cloned from marine bacterium Salinispora arenicola CNP193 and the protein was expressed in Escherichia coli. The α-amylase gene from S. arenicola CNP193 had a length of 1839 bp and encoded a α-amylase with an estimated molecular mass of 74 kDa. The optimum temperature and pH for the recombinant α-amylase was 50 °C and 7 respectively. Na, K and Ca increased the activity of the recombinant α-amylase whereas the enzyme was inhibited by Cu, Zn, Hg, Pb, Fe and Mn. Thin layer chromatography results confirmed that monosaccharide, disaccharide and maltotriose are the hydrolysis products. The results of our study suggest that this enzyme has considerable potential in industrial applications.

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54310
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10.1007/s10930-019-09870-3
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