biostudies-literatureTenea GNTechnical University of the North6152356https://www.ebi.ac.uk/biostudies/studies/S-EPMC7559518biostudies-literatureUnknown2020Protecting foods from contamination applying peptides produced by lactic acid bacteria is a promising strategy to increase the food quality and safety. Interacting with the pathogen membranes might produce visible changes in shape or cell wall damage. Previously, we showed that the peptides produced by <i>Lactobacillus plantarum</i> UTNGt2, <i>Lactobacillus plantarum</i> UTNCys5-4, and <i>Lactococcus lactis</i> subsp. <i>lactis</i> UTNGt28 exhibit a broad spectrum of antibacterial activity against several foodborne pathogens <i>in vitro</i>. In this study, their possible mode of action against the commensal microorganism <i>Salmonella enterica</i> subsp. <i>enterica</i> ATCC51741 was investigated. The target membrane permeability was determined by detection of beta-galactosidase release frBioMed research internationalPeptide Extracts from Native Lactic Acid Bacteria Generate Ghost Cells and Spheroplasts upon Interaction with <i>Salmonella enterica</i>, as Promising Food Antimicrobials.PMC75595182418/20182929/2019Tenea GNfalsePeptide Extracts from Native Lactic Acid Bacteria Generate Ghost Cells and Spheroplasts upon Interaction with <i>Salmonella enterica</i>, as Promising Food Antimicrobials.Protecting foods from contamination applying peptides produced by lactic acid bacteria is a promising strategy to increase the food quality and safety. Interacting with the pathogen membranes might produce visible changes in shape or cell wall damage. Previously, we showed that the peptides produced by <i>Lactobacillus plantarum</i> UTNGt2, <i>Lactobacillus plantarum</i> UTNCys5-4, and <i>Lactococcus lactis</i> subsp. <i>lactis</i> UTNGt28 exhibit a broad spectrum of antibacterial activity against several foodborne pathogens <i>in vitro</i>. In this study, their possible mode of action against the commensal microorganism <i>Salmonella enterica</i> subsp. <i>enterica</i> ATCC51741 was investigated. The target membrane permeability was determined by detection of beta-galactosidase release fr2020-01-01T00:00:00Z20202026-04-30T05:06:56.886Z2020-10-29T12:37:08ZS-EPMC75595183308347510.1155/2020/6152356