Bacteriocin E50-52, a class IIa bacteriocin with a wide antibacterial spectrum, has huge potential to be a substitute for conventional antibiotics. In this research, the bacteriocin E50-52 gene was cloned into the expression vector pET SUMO (small ubiquitin-related modifier) and transformed into Escherichia coli BL21 (DE3). The recombinant fusion protein SUMO-bacteriocin E50-52 expressed in a soluble form was purified to a purity of more than 90% by Ni-NTA sepharose column and 117 mg fusion protein was obtained per liter of fermentation culture. The fusion protein was cleaved with SUMO protease and re-applied to a Ni-NTA Sepharose column. Finally, about 16 mg recombinant bacteriocin E50-52 (rbE50-52) was obtained from a 1-liter fermentation culture with no less than 95% purity. The rbE50-52 had similar antimicrobial properties and molecular weight as the native bacteriocin E50-52 and showed very low hemolytic activity.