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

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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 Ca2+ increased the activity of the recombinant α-amylase whereas the enzyme was inhibited by Cu2+, Zn2+, Hg2+, Pb2+, Fe3+ and Mn2+. 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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Acknowledgements

This work was supported by the National Natural Science Foundation of China (Grant No. 31772016), Jiangsu Province Marine Science and Technology Innovation Project (HY2018-10), the Priority Academic Program Development of Jiangsu Higher Education Institutions, the Scientific Research Foundation for the Returned Overseas Chinese Scholars, Six talent peaks project in Jiangsu Provincev (2016-SWYY-195), and Project “333” of Jiangsu Province.

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Correspondence to Sibtain Ahmed or Yaowei Fang.

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Liu, S., Ahmed, S. & Fang, Y. Cloning, Expression and Characterization of a Novel α-Amylase from Salinispora arenicola CNP193. Protein J 38, 716–722 (2019). https://doi.org/10.1007/s10930-019-09870-3

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