Fusion expression of pediocin PA-1 gene in Escherichia coli

Objective To construct prokaryotic expression vector of pediocin PA-1 gene fragment induce the expression,and identify the expressed product.Method The expression vector pET32-papA was constructed by recombinant DNA technology.The expressed protein was purified through metal affinity Chromatography and identified by SDS-PAGE and Western blotting after induction by IPTG.Result pET32-papA was constructed successfully and the coding region was inserted into the vector correctly.A new protein band,about 20×103,was observed by SDS-PAGE analysis after induction by IPTG and Western blotting.The expressed product,contained about 25% of fusion protein.Conclusion PapA protein could be expressed in E.coli expression system,which could provide foundation for further studies on pediocin PA-1.