Abstract:

The tachi1 gene of Trichoderma chitinase by Trichoderma asperelluma with pEHisTEV prokaryotic expression vector fusion was highly expressed in E. coli BL21 strains. After induced by isopropyl-β-D-thiogalactoside (IPTG), the recombinant protein Tachi1 was highly expressed in the for mofinclusion bodies. The protein Tachi1 in the inclusion bodies could be solubilized, renatured and purified by a serial of treatments, including washing, denaturing and renaturing as well as purification. The renaturation protein possessed chitinase activity.