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Biochemical characterization of an enantioselective esterase from Brevundimonas sp LY-2

文献类型： 外文期刊

作者： Zhang, Jing 1 ; Zhao, Mengjun 1 ; Yu, Die 1 ; Yin, Jingang 3 ; Zhang, Hao 1 ; Huang, Xing 1 ;

作者机构： 1.Nanjing Agr Univ, Coll Life Sci, Minist Agr, Key Lab Agr Environm Microbiol, Nanjing 210095, Jiangsu, Peoples R China

2.Jiangsu Acad Agr Sci, Inst Agr Resources & Environm, Nanjing 210014, Jiangsu, Peoples R China

3.East China Univ Sci & Technol, Lab Biocatalysis & Synthet Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

关键词： Esterase;Lactofen;Brevundimonas sp.;Enantioselective degradation

期刊名称：MICROBIAL CELL FACTORIES （ 影响因子：5.328； 五年影响因子：5.588 ）

ISSN： 1475-2859

年卷期： 2017 年 16 卷

页码：

收录情况： SCI

摘要： Background: Lactofen, a member of the diphenylether herbicides, has high activity and is commonly used to control broadleaf weeds. As a post-emergent herbicide, it is directly released to the environment, and easily caused the pollution. This herbicide is degraded in soil mainly by microbial activity, but the functional enzyme involved in the biodegradation of lactofen is still not clear now. Results: A novel esterase gene lacH, involved in the degradation of lactofen, was cloned from the strain Brevundimonas sp. LY-2. The gene contained an open reading frame of 921 bp, and a putative signal peptide at the N-terminal was identified with the most likely cleavage site between Ala 28 and Ala 29. The encoded protein, LacH, could catalyze the hydrolysis of lactofen to form acifluorfen. Phylogenetic analysis showed that LacH belong to family V of bacterial lipolytic enzymes. Biochemical characterization analysis showed that LacH was a neutral esterase with an optimal pH of 7.0 and an optimal temperature of 40 degrees C toward lactofen. Besides, the activity of LacH was strongly inhibited by Hg2+ and Zn2+. LacH preferred short chain p-nitrophenyl esters (C-2-C-6), exhibited maximum activity toward p-nitrophenyl acetate. Furthermore, the enantioselectivity of LacH during lactofen hydrolysis was also studied, and the results show that R-(-)-lactofen was degraded faster than S-(+)-lactofen, indicating the occurrence of enantioselectivity in the enzymatic reaction. Conclusions: Our studies characterized a novel esterase involved in the biodegradation of diphenylether herbicide lactofen. The esterase showed enantioselectivity during lactofen degradation, which revealed the occurrence of enzyme-mediated enantioselective degradation of chiral herbicides.

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[1]Detoxification of diphenyl ether herbicide lactofen by Bacillus sp Za and enantioselective characteristics of an esterase gene lacE. Zhang, Jing,Lu, Luyao,Chen, Feng,Chen, Lingling,Huang, Xing,Zhang, Jing,Yin, Jingang. 2018

[2]Interaction of plant epicuticular waxes and extracellular esterases of Curvularia eragrostidis during infection of Digitaria sanguinalis and Festuca arundinacea by the fungus. Wang, Fei,Zhang, Peng,Qiang, Sheng,Xu, Lang-Lai. 2006

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