Directed Evolution of Insoluble Arabidopsis thaliana Zeta Class Glutathione S-Transferase Mutants for Higher Solubility in Escherichia coli

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).Although numerous strategies and approaches are proposed to solve the problem (Nygaard and Harlow,2001;Mogk et al.,2002;Austin,2003),they still fail to improve the solubility of protein and are not ideal for high-throughput applications (Waldo,2003).Furthermore,with the expression condition becoming stricter,the procedures become more complex and the costs grow higher,thus making them inappropriate for application in industrial production.