Cloning, Expression and Characterization of a Novel α-Amylase from Salinispora arenicola CNP193.
Clicks: 284
ID: 54310
2019
Article Quality & Performance Metrics
Overall Quality
Improving Quality
0.0
/100
Combines engagement data with AI-assessed academic quality
Reader Engagement
Steady Performance
78.6
/100
279 views
227 readers
Trending
AI Quality Assessment
Not analyzed
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.
| Reference Key |
liu2019cloningthe
Use this key to autocite in the manuscript while using
SciMatic Manuscript Manager or Thesis Manager
|
|---|---|
| Authors | Liu, Shu;Ahmed, Sibtain;Fang, Yaowei; |
| Journal | the protein journal |
| Year | 2019 |
| DOI |
10.1007/s10930-019-09870-3
|
| URL | |
| Keywords |
Citations
No citations found. To add a citation, contact the admin at info@scimatic.org
Comments
No comments yet. Be the first to comment on this article.