Purification and amino acid sequence of lactocin 705, a bacteriocin produced by Lactobacillus casei CRL 705. |
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Authors: | J Palacios G Vignolo M E Farías A P de Ruiz Holgado G Oliver F Sesma |
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Affiliation: | Centro de Referencia para Lactobacilos (CERELA)-CONICET, Tucumán, Argentina. |
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Abstract: | Lactobacillus casei CRL 705, isolated from a dry fermented sausage, produces an antibacterial peptide which is active against Listeria monocytogenes. Previous studies have shown that this compound is potentially useful to control food-borne pathogens in ground meat. In view of the potential application of this antimicrobial substance in food fermentation, a detailed biochemical analysis of this peptide is required. In this work, the purification and amino acid sequence of this bacteriocin is presented. The adsorption-desorption pH-dependent property of lactocin 705 was exploited for purification. The active extract was further subjected to RP-HPLC and SDS-PAGE. The active antimicrobial band was electroeluted from an SDS-PAGE gel and its amino acid sequence determined. Lactocin 705 had an estimated molecular weight of 3357.80 and an isoelectric point of 10.03. The peptide contains a high ratio of glycine residues and does not show any modified amino acids, like lanthionine or beta-methyllanthionine. The sequence was unique when compared to several databases. |
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