Author:
Ma Yanling,Zhang Xinfeng,Chen Tianmei,Liu Fulai,Fang Shuting,Zeng Rong
Abstract
We cloned a new gene from the amidase signature (AS) family, designated am , from the marine actinomycete Salinispora arenicola CNS-205. As indicated by bioinformatics analysis and site-directed mutagenesis, the AM (a gene encoding a putative amidase) protein belonged to the
AS family. AM was expressed, purified, and characterised in Escherichia coli BL21 (DE3), and the AM molecular mass was determined to be 51 kDa. The optimal temperature and pH were 40 °C and pH 8.0, respectively. AM exhibited a wide substrate spectrum and showed amidase, aryl acylamidase,
and acyl transferase activities. AM had high activity towards aromatic and aliphatic amides. The AM substrate specificity for anilides was very narrow, and only propanil could be used as an effective substrate. The extensive substrate range of AM indicates it may have broad potential applications
in biosynthetic processes and biodegradation.
Publisher
American Scientific Publishers
Subject
Renewable Energy, Sustainability and the Environment,Biomaterials,Bioengineering
Cited by
2 articles.
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