Molecular Cloning and Characterization of a Newly Isolated Pyrethroid-Degrading Esterase Gene from a Genomic Library of Ochrobactrum anthropi YZ-1
文献类型： 外文期刊
作者： Ruan, Zhiyong 1 ; Zhai, Yi 3 ; Song, Jinlong 2 ; Shi, Yanhua 2 ; Li, Kang 5 ; Zhao, Bin 1 ; Yan, Yanchun 2 ;
作者机构： 1.Huazhong Agr Univ, Coll Life Sci & Technol, Wuhan, Peoples R China
2.Chinese Acad Agr Sci, Grad Sch, Beijing 100193, Peoples R China
3.Chongqing Acad Agr Sci, Inst Agr Engn, Chongqing, Peoples R China
4.Chinese Acad Agr Sci, Inst Agr Resources & Reg Planning, Beijing 100193, Peoples R China
5.Natl Inst Food & Drug Control, Inst Biol Prod Control, Beijing, Peoples R China
期刊名称：PLOS ONE （ 影响因子：3.24； 五年影响因子：3.788 ）
ISSN： 1932-6203
年卷期： 2013 年 8 卷 10 期
页码：
收录情况： SCI
摘要： A novel pyrethroid-degrading esterase gene pytY was isolated from the genomic library of Ochrobactrum anthropi YZ-1. It possesses an open reading frame (ORF) of 897 bp. Blast search showed that its deduced amino acid sequence shares moderate identities (30% to 46%) with most homologous esterases. Phylogenetic analysis revealed that PytY is a member of the esterase VI family. pytY showed very low sequence similarity compared with reported pyrethroid-degrading genes. PytY was expressed, purified, and characterized. Enzyme assay revealed that PytY is a broad-spectrum degrading enzyme that can degrade various pyrethroids. It is a new pyrethroid-degrading gene and enriches genetic resource. Kinetic constants of Km and Vmax were 2.34 mmol.L-1 21 and 56.33 nmol min(-1), respectively, with lambda-cyhalothrin as substrate. PytY displayed good degrading ability and stability over a broad range of temperature and pH. The optimal temperature and pH were of 35 degrees C and 7.5. No cofactors were required for enzyme activity. The results highlighted the potential use of PytY in the elimination of pyrethroid residuals from contaminated environments.
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