Purification of a Bacteriocin from Lactobacillus plantarum ZJ217 Active Against Methicillin-Resistant Staphylococcus aureus

Abstract

Abstract Plantaricin ZJ217 was continually purified by XAD 1180, cation exchange chromatography, gel chromatography, and high performance liquid chromatography (HPLC) system. The peptide functioned as bactericidal, but did not lead to lysis of cells. Considering the potassium efflux experiment, pores may be formed in the surface of cell membrane. Fifteen of twenty amino acids identified by Edman degradation indicated that it may be a novel bacteriocin as no bacteriocin shared similar sequences. This bacteriocin exhibited strong heat stability (121°C, 30 min) and pH stability (pH 2.0–6.0). It was sensitive to proteinase K, trypsin, papain, and pepsin. This bacteriocin inhibited growth of methicillin-resistant Staphylococcus aureus (MRSA) and other bacteria.