Purification and amino acid sequence of lactocin 705, a bacteriocin produced by Lactobacillus casei CRL 705
| Autor: | A. P. de Ruiz Holgado, Graciela Vignolo, Guillermo Oliver, Jorge Palacios, Maria Eugenia Farias, Fernando Sesma |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
chemistry.chemical_classification
Lactobacillus casei biology Molecular Sequence Data food and beverages Peptide Hydrogen-Ion Concentration biology.organism_classification Microbiology Protein Structure Secondary Amino acid Molecular Weight Lacticaseibacillus casei chemistry.chemical_compound Isoelectric point Bacteriocins chemistry Bacteriocin Biochemistry Amino Acid Sequence Peptide sequence Lanthionine Antibacterial agent |
| Zdroj: | Microbiological Research. 154:199-204 |
| ISSN: | 0944-5013 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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