Open Access
Bacteriocins of grampositive bacteria
Rw Jack
- Vol. 59, pp 171-200
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The article was published on 1995-01-01 and is currently open access. It has received 1250 citations till now. The article focuses on the topics: Bacteriocin.read more
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Journal ArticleDOI
Influence of Lactobacillus plantarum WCFS1 on post-acidification, metabolite formation and survival of starter bacteria in set-yoghurt
Sarn Settachaimongkon,Hein J.F. van Valenberg,Inge Gazi,M.J. Robert Nout,Toon van Hooijdonk,Marcel H. Zwietering,Eddy J. Smid +6 more
TL;DR: Insight is provided in the technological implications of non-dairy model probiotic strain L. plantarum WCFS1, such as its good stability in fermented milk and the inhibitory effect on post-acidification and the metabolite profiles of set-yoghurt.
Journal ArticleDOI
Antimicrobial potential of bacteriocin producing Lysinibacillus jx416856 against foodborne bacterial and fungal pathogens, isolated from fruits and vegetable waste.
TL;DR: Collectively, the broad spectrum inhibitory potential and physical stability offered the antimicrobial potential to Lysinibacillus, and its relevant bacteriocin might be used as an alternative food preservative or therapeutic agent to control spoilage of different food products.
Journal ArticleDOI
Lactococcal membrane-permeabilizing antimicrobial peptides
TL;DR: The most studied and prominent bacteriocin, nisin A is characterized in the high activity and has been utilized as food preservatives for more than half a century.
Book ChapterDOI
Food Preservation with Chemicals
TL;DR: A large number of chemicals have been described that show potential as food preservatives, but only a relatively small number are allowed in food products, due in large part to the strict rules of safety adhered to by the Food and Drug Administration and to a lesser extent to the fact that not all compounds that show antimicrobial activity in vitro do so when added to certain foods.
Journal ArticleDOI
Distinguishing between different pathways of bilayer disruption by the related antimicrobial peptides cecropin B, B1 and B3
TL;DR: Different pathways of bilayer disruption by the structurally related antimicrobial peptides cecropin B, B1 and B3, revealed by surface plasma resonance analysis of immobilized liposomes, differential scanning calorimetry of peptide-large unilamellar vesicle interactions, and light microscopic analysis of peptIDE-treated giant unilamese vesicles, have been identified.