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

被引：10

作者：

Liu, Shu ^{[1
,3
]}

Ahmed, Sibtain ^{[2
]}

Fang, Yaowei ^{[1
,3
,4
]}

机构：

[1] Jiangsu Key Lab Marine Bioresource & Environm, Lianyungang 222005, Peoples R China

[2] Univ Calif San Diego, 9500 Gilman Dr, San Diego, CA 92093 USA

[3] Jiangsu Marine Resources Dev Res Inst, Lianyungang 222000, Peoples R China

[4] Huaihai Inst Technol, Coll Marine Life & Fisheries, Lianyungang 222005, Peoples R China

来源：

PROTEIN JOURNAL | 2019年 / 38卷 / 06期

基金：

中国国家自然科学基金;

关键词：

Salinispora arenicola; alpha-Amylase; Expression; Biochemical characterization; PURIFICATION; STARCH; FAMILY; GLUCOAMYLASE; SUBTILIS; SEQUENCE; STRAIN;

D O I：

10.1007/s10930-019-09870-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

alpha-Amylases are used in various biotechnological processes including the textile, paper, food, biofuels, detergents and pharmaceutical industries. In this study, a novel gene encoding alpha-amylase was cloned from marine bacterium Salinispora arenicola CNP193 and the protein was expressed in Escherichia coli. The alpha-amylase gene from S. arenicola CNP193 had a length of 1839 bp and encoded a alpha-amylase with an estimated molecular mass of 74 kDa. The optimum temperature and pH for the recombinant alpha-amylase was 50 degrees C and 7 respectively. Na+, K+ and Ca2+ increased the activity of the recombinant alpha-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.

引用

页码：716 / 722

页数：7

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