| Literature DB >> 22100232 |
Peng Jin1, Xiaolin Pei, Pengfei Du, Xiaopu Yin, Xiaolong Xiong, Huili Wu, Xiuling Zhou, Qiuyan Wang.
Abstract
In this study, an esterase, designated EstC23, was isolated from a soil metagenomic library. The protein was amenable to overexpression in Escherichia coli under control of the T7 promoter, resulting in expression of the active, soluble protein that constituted 30% of the total cell protein content. This enzyme showed optimal activity at 40 °C and retained about 50% maximal activity at 5-10 °C. EstC23 showed remarkable stability in up to 50% (v/v) benzene and alkanes (high logP solvents). When incubated for 7 days in the presence of 50% benzene or alkanes, the enzyme maintained its 2-3 fold elevated activity. The purified enzyme also cleaved sterically hindered esters of tertiary alcohols. These results indicate that EstC23 has potential for use in industrial processes.Entities:
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Year: 2011 PMID: 22100232 DOI: 10.1016/j.biortech.2011.10.087
Source DB: PubMed Journal: Bioresour Technol ISSN: 0960-8524 Impact factor: 9.642