[Objective] This study aimed to obtain recombinant alpha-bungarotoxin (α-BGT)gene fusion protein with biological activity and investiagte its fusion expression.[Method] The plasmid pGEX-α-BGT was transformed into E coil BL21 (DE3) and BL21 (DE3) plysS host bacteria to identify the optimal engineering strain.Fusion expression of the optimal engineering strain was induced,in order to optimize the induced expression conditions of the soluble fusion protein.[Result] JP-α-BGT was identified as the optimal engineering strain,which could express fusion protein after induced by IPTG.The optimal induced expression conditions of the soluble fusion protein were investigatect JP-α-BGT was incubated at 37 ℃ for 25 h and induced with 0.50 mmol/L IPTG for 4 h at 22 ℃,and the expression level of the soluble fusion protein reached 18.42％.[Conclusion] This study laid a solid foundation for the subsequent purification of fusion proteins and the separation and purification of α-BGT.
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