Purification, characterization and antimicrobial spectrum of a bacteriocin produced by Pediococcus acidilactici.
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.
Bhunia
A K
AK
Department of Animal Science, University of Wyoming, Laramie 82071.
Johnson
M C
MC
Ray
B
B
D001419:Bacteria / Q000187:drug effects*; D001430:Bacteriocins / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003016:Clostridium perfringens / Q000187:drug effects; D015169:Colony Count, Microbial; D004591:Electrophoresis, Polyacrylamide Gel; D004798:Enzymes / Q000378:metabolism; D005516:Food Microbiology; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007778:Lactobacillus / Q000187:drug effects; D008089:Listeria monocytogenes / Q000187:drug effects; D010376:Pediococcus; D011549:Pseudomonas / Q000187:drug effects; D013211:Staphylococcus aureus / Q000187:drug effects
D001430:Bacteriocins; D004798:Enzymes