摘要
Expression of recombinant protein in Escherichia coli （E.coli） is generally considered as one of the ideal systems to produce proteins for industrial production.However,the majority of proteins usually fail to fold into their native state and accumulate as insoluble inclusion bodies with no biological activity in E.coli（Yang et al.,2003）.
Expression of recombinant protein in Escherichia coli （E.coli） is generally considered as one of the ideal systems to produce proteins for industrial production.However,the majority of proteins usually fail to fold into their native state and accumulate as insoluble inclusion bodies with no biological activity in E.coli（Yang et al.,2003）.
基金
supported by the grants of the National Natural Science Foundation of China(No.31070717)
Tianjin International Science and Technology Cooperation Project (No.09ZCGHHZ00500)
the 111 Project(No.B08011)
