[Purification and characterization of "Clostridium perfringens" BP6K-N5 strain bacteriocin N5 (author's transl)]

Abstract

The bacteriocin N5 produced by Clostridium perfringens, strain BP6K-N5, after UV irradiation induction, was purified by ammonium sulfate precipitation, followed by ion-exchange chromatography on DEAE cellulose and gel filtration on Sephadex G100. By polyacrylamid-gel electrophoresis and immunodiffusion analysis the purified material was shown to be homogenous. The purified bacteriocin N5 is inactivated by proteolytic enzymes and by heat treatment at 50 degrees C for 15 minutes. It is a simple protein with a molecular weight of approximately 82.000. The protein appears to be a single polypeptide chain, as no dissociation is obtained by sodium dodecyl sulfate and beta-mercaptoethanol disc-gel-electrophoresis.