ArticleThe protein journal2019
Cloning, Expression and Characterization of a Novel α-Amylase from Salinispora arenicola CNP193.
Article in The protein journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 10 citations in OpenAlex.
- Overcoming cellular secretion bottlenecks: advanced secretion engineering and molecular tailoring for next-generation microbial α-amylases with enhanced industrial performance.World journal of microbiology & biotechnology · 2026Review
- Characterization of an Amylolytic Enzyme from Massilia timonae of the GH13_19 Subfamily with Mixed Maltogenic and CGTase Activity.Applied biochemistry and biotechnology · 2023Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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
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