Purification and mass spectrometry based characterization of a pediocin produced by Pediococcus acidilactici 13 |
| |
Authors: | Evrim Güne? Altunta? Kamuran Ayhan Selen Peker Beycan Ayhan Duygu Özel Demiralp |
| |
Institution: | 1. Central Laboratory, Biotechnology Institute, Ankara University, 06110, Tando?an, Ankara, Turkey 2. Food Engineering Department, Engineering Faculty, Ankara University, Ankara, Turkey
|
| |
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. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|