Abstract: The inclusion body of the recombinant pediocin fusion protein was produced by the excess expression of gene engineering E.coli BL21( DE3).The inclusion body was separated,denatured,and then refolded using direct dilution,reversed dilution,dialysis,CTAB assisted,and CTAB and β- CD assisted refolding.The results showed that CTAB and β- CD assisted refolding have advantage over other refolding methods. Through this method,a higher concentration of denatured inclusion protein and a smaller volume renatured solution were used. And a higher concentration of refolding product and a relatively stable refolding rate were achieved.