摘要
用抗性库蚊酯酶基因,引入原核表达载体pRL439,转化大肠杆菌HB101细胞,获得表达.通过酶切、Southern杂交鉴定重组质粒.研究了重组菌酯酶的活性,重组质粒pRL-B1表达的酯酶具有高酶活并能高效降解酯酶的特异性底物a-乙酸萘酯(a-NA)和β-乙酸萘酯(β-NA);经对重组菌进行细胞固定化后降解有机磷农药对硫磷(1605),反应时间短,降解效率高.
Through resistant esterase gene cloned into the vector pRL439 the expression had been done for E.coli on bacillius HB101 cell transformation. This recombinant plasmid pRLB1 was identified by digestion and Southern analysis. The activity of recombinant esterase was studied. The esterase expressed by pRLB1 possessed high enzyme activity and could effectively degrade the specific substrate α-naphthyl acetate (α-NA) and β-naphthyl(β-NA) of esterase. The recombinant engineered bacterium was immobilized. Assays showed that the organic phosphorus pesticide parathion (1605) was degraded by the immobilized cell within short time and high efficiency.
出处
《中国环境科学》
EI
CAS
CSSCI
CSCD
北大核心
2001年第5期412-416,共5页
China Environmental Science
基金
山东省自然科学基金资助项目(Y98D16064)
