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Purification, characterization and antimicrobial spectrum of a bacteriocin produced by Pediococcus acidilactici
Author(s) -
Bhunia A.K.,
Johnson M. C.,
Ray B.
Publication year - 1988
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1988.tb01893.x
Subject(s) - pediococcus acidilactici , bacteriocin , listeria monocytogenes , clostridium perfringens , antimicrobial , food spoilage , chemistry , microbiology and biotechnology , listeria , pediococcus , proteolytic enzymes , staphylococcus aureus , lysis , bacteria , food science , biochemistry , biology , enzyme , lactobacillus , fermentation , lactic acid , genetics , lactobacillus plantarum
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.