摘要
从长期受农药污染的土壤中分离得到一株能高效降解氨基甲酸酯类农药的假单胞菌AE-BL3,它在呋喃丹的诱导下能产生较高活性的呋喃丹水解酶.通过硫酸鱼精蛋白处理、(NH4)2SO4分级沉淀、DEAE纤维素离子交换层析和苯基交联琼脂糖层析,从菌体中纯化得到凝胶电泳均一的呋喃丹水解酶,纯化倍数为30.33倍.用SDS-PAGE测得该酶的分子质量约为85ku,酶作用的最适温度为40°C,最适pH值为4.5和6.5,30°C下保温30min,酶活力基本不变,高于50°C酶活力则迅速下降;K+和Na+等对酶有激活作用,Hg2+、Zn2+、Cu2+和Mn2+等对酶有抑制作用.
A bacterium capable of hydrolyzing carbofuran was isolated from a soil exposed to repeated spills of carbamate pesticides. This bacterium is characterized taxonomically as a Pseudomonas sp. and designated strain AEBL3. A carbofuran hydrolase present in this strain was purified to homogeneity by protamine sulfate treatment, ammonium sulfate precipitation, and hydrophobic, anion-exchange chromatographies. The purification fold is 30.33. Its molecular weight was estimated to be about 85 ku by SDS-PAGE. The optimum temperature is 40(°C). The optimum pH for the enzyme activity are (4.5) and (6.5.) The enzyme is stable at 30(°C), but not stable at temperature above 50(°C). Its activity can be stimulated by K^+ and Na^+, but strongly inhibited by Hg^(2+),Cu^(2+),Zn^(2+) and Mn^(2+).
出处
《上海交通大学学报》
EI
CAS
CSCD
北大核心
2004年第5期834-837,共4页
Journal of Shanghai Jiaotong University
基金
天津市重点自然科学基金资助项目(99380291)
关键词
呋喃丹
水解酶
纯化
酶学性质
carbofuran
hydrolase
purification
enzyme character
