Purification and mass spectrometry based characterization of a pediocin produced by Pediococcus acidilactici 13

Altuntas E. G., Ayhan K., Peker S., Ayhan B., Demiralp D. O.

MOLECULAR BIOLOGY REPORTS, vol.41, no.10, pp.6879-6885, 2014 (SCI-Expanded, Scopus) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 41 Issue: 10
  • Publication Date: 2014
  • Doi Number: 10.1007/s11033-014-3573-z
  • Journal Name: MOLECULAR BIOLOGY REPORTS
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.6879-6885
  • Keywords: Pediococcus acidilactici, Pediocin, Ultrafiltration purification, Proteomic analysis, 2D-PAGE, MALDI-TOF MS
  • Dokuz Eylül University Affiliated: No

Abstract

Bacteriocins are antimicrobial peptides produced by several bacterial species. Among the bacteriocins pediocin-like bacteriocins have a significant inhibitory activity on the foodborne pathogens especially on Listeria monocytogenes. This study aims to select a simple and usable purification method to purify/concentrate the antimicrobial peptide and characterization of the bacteriocin produced by Pediococcus acidilactici 13 by using proteomic approaches which is a recent omic technology. For purification dialysis, ultrafiltration method was used, and as a result of this study the bacteriocin activity reached 819,200 AU/mL from 102,400 AU/mL initially. Two dimensional gel electrophoresis and then matrix-assisted laser desorption ionization/time of flight mass spectrometry (MALDI-TOF MS) analysis were carried out to identify the current bacteriocin and related proteins. Obtained data revealed similarity to pediocin PA-1 transport/processing ATP-binding protein PedD (accession number: P36497), pediocin operon PedC (accession number: Q68GC4) and bacteriocin pediocin PA-1 (accession number: P29430) from UniProtKB/Swiss-Prot databank, thus the bacteriocin produced by P. acidilactici 13 is considered similar to pediocin PA-1.