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Cloning and expression of a novel α‐amylase from Salinispora arenicola CNP193 in E. coli
Author(s) -
Ahmed Sibtain,
Fang Yaowei
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.00737
Subject(s) - maltotriose , amylase , recombinant dna , chemistry , escherichia coli , enzyme , hydrolysis , biochemistry , molecular mass , monosaccharide , gene , microbiology and biotechnology , biology
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 2+ increased the activity of the recombinant α‐amylase whereas the enzyme was inhibited by Cu 2+ , Zn 2+ , Hg 2+ , Pb 2+ , Fe 3+ and Mn 2+ . 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.