Purification and Characterization of Enterocins A, B, and a Novel High-Mass Bacteriocin from Enterococcus lactis-67 with Antilisterial Activity

从乳酸肠球菌-67中纯化和表征肠球菌素A、B和一种新型高分子量细菌素,该细菌素具有抗李斯特菌活性

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Abstract

Background/Objectives:Listeria monocytogenes is a high-risk pathogen in the food industry involved in several outbreaks. Bacteriocins are natural-origin antimicrobial peptides or proteins that represent a good alternative to synthetic antimicrobials capable of inhibiting the growth of pathogens. This study aimed to purify and identify bacteriocins from the cell-free supernatant of Enterococcus lactis-67, which exhibits antagonistic activity against L. monocytogenes. Methods: Protein purification was performed by precipitation with ammonium sulfate, dialysis, and fast protein liquid chromatography. Active protein fractions were analyzed by SDS-PAGE and identified by mass spectrometry. Results: In addition to enterocins A and B, a novel 47 kDa bacteriocin with LysM and NlpC/P60 domains, on the N- and C-terminal regions, respectively, was identified. This enterocin has not been described for Enterococcus before. Conclusions: This study contributes to the identification of new natural and effective strategies for ensuring food safety.

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