Function Analysis of Organophosphate Pesticides Hydrolase from Pseudomonas stutzeri HS-D36
In this paper, a novel organophosphatedegrading bacterium HS-D36 belonging to Pseudomonas stutzeri was reported. This bacterium has a strong ability to hydrolyze methyl parathion and the organophosphate pesticides hydrolase gene (oph) was cloned for the organophosphate hydrolase (OPH) function analysis. The oph gene was expressed in Escherichia coli BL21 (DE3) by using pET-28 expression system. The activity of the recombinant OPH in crude extracts reached 52.5 U ·ml-1.Thermal stability experiment showed that the enzyme inactivated little for 60 minutes at temperature below 50 ℃. Further, the sequence alignment and phylogenetic analysis suggested that the OPH protein from the strain HS-D36 was 99.0％ similar to MPD protein from Pseudomonas sp.WBC-3 and may be originated from metallo-β-lactamases family. The protein structure prediction results suggested that the mature OPH comprise two independent subunits, each is composed of an active metal center (Zn2+ and Cd2+).
Organophosphate pesticides hydrolase Sequence alignment OPH protein structure Degradation characteristics Thermal stability
Zhenzhong Guo Yongze Yuan Shangying Xu Binbin Wang Deli Liu Jiangke Yang Yunjun Yan
Laboratory of Genetic Regulation and Integrative Biology,College of Life Science,Central China Norma College of Life Science and Technology,Huazhong University of Science and Technology,Wuhan,China,430
国际会议
北京
英文
1-4
2009-06-11（万方平台首次上网日期，不代表论文的发表时间）