Mechanistic action of pediocin and nisin: recent progress and unresolved questions |
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| Authors: | T J Montville Y Chen |
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| Institution: | (1) Department of Food Science, Cook College, Rutgers, The State University of New Jersey, 65 Dudley Road, New Brunswick, NJ 08901, USA Tel.: +732-932-9611 ext. 201 Fax: +732-932-6776 e-mail: montville@aesop.rutgers.edu, CK |
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| Abstract: | Nisin and pediocin PA-1 are examples of bacteriocins from lactic acid bacteria (LAB) that have found practical applications
as food preservatives. Like other natural antimicrobial peptides, LAB bacteriocins act primarily at the cytoplasmic membranes
of susceptible microorganisms. Studies with in vivo as well as in␣vitro membrane systems are directed toward understanding
how bacteriocins interact with membranes so as to provide a mechanistic basis for their rational applications. The dissipation
of proton motive force was identified early on as the common mechanism for the lethal activity of LAB bacteriocin. Models
for nisin/membrane interactions propose that the peptide forms poration complexes in the membrane through a multi-step process
of binding, insertion, and pore formation. This review focuses on the current knowledge of: (1) the mechanistic action of
nisin and pediocin-like bacteriocins, (2) the requirement for a cell factor such as a membrane protein, (3) the influence
of membrane potential, pH, and lipid composition on the of specificity and efficacy of bacteriocins, and (4) the roles of
specific amino acids and structural domains of the bacteriocins in their action.
Received: 3 April 1998 / Received last revision: 27 July 1998 / Accepted: 29 July 1998 |
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