Purification, characterization and antimicrobial spectrum of a bacteriocin produced by <i>Pediococcus acidilactici</i>

TLDR

Pediocin AcH was isolated from Pediococcus acidilactici strain H and purified by ion exchange chromatography. Pediocin AcH, a ~2700‑Da peptide, is protease‑sensitive but heat‑ and solvent‑stable, active across a wide pH range, rapidly bactericidal against food spoilage bacteria and pathogens such as *Staphylococcus aureus*, *Clostridium perfringens*, and *Listeria monocytogenes*, without causing cell lysis or membrane permeability loss.

Abstract

An antimicrobial peptide designated pediocin AcH was isolated from Pediococcus acidilactici strain H. The pediocin AcH was purified by ion exchange chromatography. The molecular weight of pediocin AcH was determined by SDS‐PAGE to be about 2700 daltons. Pediocin AcH was sensitive to proteolytic enzymes, resistant to heat and organic solvents, and active over a wide range of pH. Pediocin AcH exhibited inhibition against several food spoilage bacteria and foodborne pathogens including Staphylococcus aureus, Clostridium perfringens and Listeria monocytogenes. It was bactericidal to sensitive cells and acted very rapidly. The bactericidal effect was not produced by either cell lysis or apparent loss of membrane permeability.