Isolation of a fluoroglycofen-degrading KS-1 strain and cloning of a novel esterase gene fluE

文献类型： 外文期刊

第一作者： Huang, Xing

作者： Huang, Xing;Chen, Feng;Sun, Bin;Zhang, Hao;Tian, Yunlong;Zhu, Changxiong

作者机构：

关键词： diphenyl ether herbicide;Lysinibacillus sp KS-1;degradation;fluE

期刊名称：FEMS MICROBIOLOGY LETTERS （ 影响因子：2.742； 五年影响因子：2.856 ）

ISSN： 0378-1097

年卷期： 2017 年 364 卷 16 期

页码：

收录情况： SCI

摘要： The bacterium KS-1, capable of degrading fluoroglycofen, was isolated from sludge collected at a herbicide factory. The isolate was identified as Lysinibacillus sp. according to its phenotypic features and 16S rDNA phylogeny. KS-1 degraded 85.25% of the fluoroglycofen (50 mg L-1) within 3 days of incubation. The optimum temperature and pH for fluoroglycofen degradation were 30 degrees C and 7.0, respectively. Furthermore, Zn2+ and Cu2+ could significantly decrease the degradation rate. Three degradation products, which appeared during KS-1-mediated fluoroglycofen metabolism, were identified as deethyl-fluoroglycofen, acifluorfen and decarboxylate-acifluorfen. The fluE gene, which encodes a novel esterase that catalyzes the cleavage of carboxyl ester bonds of fluoroglycofen, was cloned from the KS-1 strain. Sequence alignment reveals that FluE shares 30%-40% amino acid sequence identity with members of the hormone sensitive lipase family. FluE was expressed in Escherichia coli BL21 and purified by Ni-NTA affinity chromatography. Purified FluE could efficiently hydrolyze fluoroglycofen and short-chain p-nitrophenol esters. However, no lipolytic activity was observed with esters containing acyl chains longer than 10 carbon atoms, thereby indicating that this enzyme is an esterase.

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