Cloning,expression and characterization of a halotolerant esterase from a marine bacterium Pelagibacterium halotolerans B2T |
| |
Authors: | Xiawei Jiang Yingyi Huo Hong Cheng Xinqi Zhang Xufen Zhu Min Wu |
| |
Affiliation: | (1) College of Life Sciences, Zhejiang University, 866 Yuhangtang Road, Hangzhou, 310058, Zhejiang, China; |
| |
Abstract: | An esterase PE10 (279 aa) from Pelagibacterium halotolerans B2T was cloned and overexpressed in Escherichia coli Rosetta in a soluble form. The deduced protein was 29.91 kDa and the phylogenetic analysis of the deduced amino acids sequence showed it represented a new family of lipolytic enzymes. The recombinant protein was purified by Ni–NTA affinity chromatography column and the characterization showed its optimal temperature and pH were 45 °C and pH 7.5, respectively. Substrate specificity study showed PE10 preferred short chain p-nitrophenyl esters and exhibited maximum activity toward p-nitrophenyl acetate. In addition, PE10 was a halotolerant esterase as it was still active under 4 M NaCl. Three-dimensional modeling of PE10 suggested that the high negative electrostatic potential on the surface may relevant to its tolerance to high salt environment. With this halotolerance property, PE10 could be a candidate for industrial use. |
| |
Keywords: | |
本文献已被 PubMed SpringerLink 等数据库收录! |
|