Isolation and Characterization of an Anti-listerial Bacteriocin from SD501.

Although bacteriocins with anti-listerial activity have been isolated from a wide variety of lactic acid bacteria, little is known about those from , a heterofermentative bacterium that produces diacetyl and exopolysaccharides in dairy foods. In this study, an anti-listerial bacteriocin was isolated from SD501 and characterized. It was particularly potent against and also inhibited . Anti-listerial activity reached a maximum during the early stationary phase and then decreased gradually. The anti-listerial substance was sensitive to proteinase K and ɑ-chymotrypsin, confirming its proteinaceous nature. Its activity remained stable at pH values ranging from 1 to 10. In addition, it was strongly resistant to high temperatures, retaining its activity even after incubation for 15 min at 121℃. The apparent molecular mass of the partially purified anti-listerial bacteriocin was approximately 7 kDa. The characteristics of the SD501 bacteriocin, including its small molecular size (<10 kDa), strong anti-listerial activity, wide pH stability and good thermostability, indicate its classification as a Class IIa bacteriocin.