Purification, partial characterization and plasmid‐linkage of pediocin SJ‐1, a bacteriocin produced by Pediococcus acidilactici

摘要: Pediococcus acidilactici SJ-1, isolated from a naturally-fermented meat product, produced an antibacterial agent active against selected strains of Lactobacillus spp., Clostridium perfringens and Listeria monocytogenes. The was bactericidal sensitive indicators, to proteolytic enzymes; it identified as bacteriocin, designated pediocin SJ-1. It stable over wide pH range (3-9), apparently most in the lower part that range. At 3.6, SJ-1 at heat-processing temperatures within 65-121 degrees C; its activity decreased significantly, however, when heated 7.0. on indicator cells lost presence alpha-amylase, suggesting contains glyco moiety, necessary for action. Native exists form monomers aggregates (with molecular weights 80-150 kDa). Pediocin purified 262-fold by direct application cell-free supernatant fluids cation-exchange chromatography column, resolved SDS-PAGE single peptide band with MW ca 4 kDa. original SJ-1-producing strain (bac+) harbours three plasmids 4.6, 23.5, 45.7 MDa. Production but not immunity is associated 4.6 MDa plasmid.