Abstract
Enterocin AS-48 is a circular bacteriocin produced by Enterococcus. It contains a 70 amino acid-residue chain circularized by a head-to-tail peptide bond. The conformation of enterocin AS-48 is arranged into five alpha-helices with a compact globular structure. Enterocin AS-48 has a wide inhibitory spectrum on Gram-positive bacteria. Sensitivity of Gram-negative bacteria increases in combination with outer-membrane permeabilizing treatments. Eukaryotic cells are bacteriocin-resistant. This cationic peptide inserts into bacterial membranes and causes membrane permeabilization, leading ultimately to cell death. Microarray analysis revealed sets of up-regulated and down-regulated genes in Bacillus cereus cells treated with sublethal bacteriocin concentration. Enterocin AS-48 can be purified in two steps or prepared as lyophilized powder from cultures in whey-based substrates. The potential applications of enterocin AS-48 as a food biopreservative have been corroborated against foodborne pathogens and/or toxigenic bacteria (Listeria monocytogenes, Bacillus cereus, Staphylococcus aureus, Escherichia coli, Salmonella enterica) and spoilage bacteria (Alicyclobacillus acidoterrestris, Bacillus spp., Paenibacillus spp., Geobacillus stearothermophilus, Brochothrix thermosphacta, Staphylococcus carnosus, Lactobacillus sakei and other spoilage lactic acid bacteria). The efficacy of enterocin AS-48 in food systems increases greatly in combination with chemical preservatives, essential oils, phenolic compounds, and physico-chemical treatments such as sublethal heat, high-intensity pulsed-electric fields or high hydrostatic pressure.
Highlights
Bacteriocins can be defined as ribosomally synthesized antimicrobial peptides or proteins, which can be posttranslationally modified or not [1]
Bacteria associated with food systems can be potential sources of antibacterial peptides, such as bacteriocins and peptide antibiotics
Enterocin AS-48 was first described as a peptide antibiotic considering that it could have potential applications for medical purposes because of its broad antibacterial spectrum [31]
Summary
Bacteriocins can be defined as ribosomally synthesized antimicrobial peptides or proteins, which can be posttranslationally modified or not [1]. A plethora of bacteriocins released by bacteria from foods have been characterized in the past decades, such as nisin, pediocins, lacticins, lactococcins, leuconocins, plantaricins, enterocins, carnobacteriocins, and others [23,24,25,26,27,28,29,30]. Many of these have been characterized at the biochemical and genetic level, and tested in food systems as biopreservatives against foodborne spoilage and pathogenic bacteria. The paradigm of bacteriocins is nisin, which is approved as a natural food preservative and widely used over the world
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