Purification and Characterization of Recombinant Methyl Parathion Hydrolase from Pseudomonas aeruginosa HS-D38

被引：0

作者：

Zheng, Yongliang ^{[1
,2
]}

Long, Lifang ^{[2
]}

Fang, Jianping ^{[2
]}

Wang, Shuzhen ^{[1
]}

机构：

[1] Hubei Key Lab Econ Forest Germplasm Improvement &, Huangzhou 438000, Hubei Province, Peoples R China

[2] Huanggang Normal Univ, Huangzhou 438000, Hubei Province, Peoples R China

来源：

RESEARCH JOURNAL OF BIOTECHNOLOGY | 2014年 / 9卷 / 04期

关键词：

Methyl parathion hydrolase; enzyme activity; crude enzyme extract; Pseudomonas aeruginosa; SURFACE-DISPLAY; P-NITROPHENOL; PHOSPHOTRIESTERASES; THERMOSTABILITY;

D O I：

暂无

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Organophosphate hydrolase plays an important role in the bioremediation of organophosphate chemicals contaminating the environment. In this study, some characteristics of recombinant methyl parathion hydrolase (MPH) cloned from Pseudomonas aeruginosa HS-D38 were investigated. The optimum conditions of the MPH reaction were determined i.e. 30 degrees C, pH 10.0. Some metal ions such as Zn2+, Fe3+, Cr2+ and Co2+ activated the activity whereas others, including Cu2+, K+ and Mg2+, inhibited it. SDS-PAGE analysis indicated a molecular weight of 35 kDa for the recombinant MPH protein and the enzyme activity was two-fold higher compared to that in the wild-type strain.

引用

页码：32 / 36

页数：5

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