RAPID PURIFICATION, PARTIAL CHARACTERIZATION, AND ANTIMICROBIAL SPECTRUM OF THE BACTERIOCIN, PEDIOCIN ACM, FROM PEDIOCOCCUS-ACIDILACTICI-M

The bacteriocin from Pediococcus acidilactici M, designated as Pedioci n AcM, was rapidly purified to homogeneity by the pH mediated cell ads orption-desorption method and semi-preparative reversed-phase HPLC. Th e purification yield was 40.4% and the specific activity was increased by 2450-fold. It gave a single band and a single peak on SDS-PAGE and HPLC analysis, respectively. When subjected to electrospray LC-MS ana lysis, the protein was found to be highly pure and the molecular weigh t was determined as 4,618 Da. High concentration of the bacteriocin (> 50 mu g/ml) showed good resistance to extremes of pH (1-12) and temper ature (121 degrees C). Pediocin AcM was deduced to be a monomer with a n intra-peptide disulfide bond from the results of reversed-phase anal ytical HPLC analyses after reduction, oxidation and trypsin digestion. P. acidilactici M inhibited a large number of bacteria, including Sta phylococcus aureus, Listeria monocytogenes, Clostridium perfringens, B acillus coagulans, B. cereus, and Aeromonas hydrophila. (C) 1997 Elsev ier Science B.V.