Abstract
A new bacteriocin, lacticin LC14, produced by Lactococcus lactis BMG6.14, was isolated and characterized. It was purified to homogeneity from overnight broth culture by ammonium sulfate precipitation, Sep-Pak chromatography, and two steps of reversed-phase HPLC. Lacticin LC14 showed bactericidal-type antimicrobial activity against several lactic acid bacteria and pathogenic strains including Listeria monocytogenes. It was inactivated by proteinase K and pronase E, but was resistant to papain, lysozyme, lipase and catalase. Lacticin LC14 was heat resistant, stable over a wide range of pH (2-10) and after treatment by solvents and detergents. Its N-terminal end was found unreactive towards Edman sequencing. Based on MALDI-TOF mass spectrometry, its molecular mass was 3333.7 Da. LC14 amino acid composition revealed a high proportion of hydrophobic residues, but no modified ones. LC14 may be able to challenge other well known other bacteriocins in probiotic and therapeutic applications.
Keywords: Antimicrobial activity, Bacteriocin, Lactic acid bacteria, Lacticin LC14, Listeria monocytogenes, Lactococcus lactis subsp. lactis BMG6.14, ammonium sulfate precipitation, chromatography, chromatography, pathogenic strains, lysozyme, lipase and catalase, amino acid, hydrophobic residues
Infectious Disorders - Drug Targets
Title:Lacticin LC14, a New Bacteriocin Produced by Lactococcus lactis BMG6.14: Isolation, Purification and Partial Characterization
Volume: 12 Issue: 4
Author(s): Samar Lasta, Hadda Ouzari, Nicolas Andreotti, Ziad Fajloun, Pascal Mansuelle, Abdellatif Boudabous, François Sampieri and Jean Marc Sabatier
Affiliation:
Keywords: Antimicrobial activity, Bacteriocin, Lactic acid bacteria, Lacticin LC14, Listeria monocytogenes, Lactococcus lactis subsp. lactis BMG6.14, ammonium sulfate precipitation, chromatography, chromatography, pathogenic strains, lysozyme, lipase and catalase, amino acid, hydrophobic residues
Abstract: A new bacteriocin, lacticin LC14, produced by Lactococcus lactis BMG6.14, was isolated and characterized. It was purified to homogeneity from overnight broth culture by ammonium sulfate precipitation, Sep-Pak chromatography, and two steps of reversed-phase HPLC. Lacticin LC14 showed bactericidal-type antimicrobial activity against several lactic acid bacteria and pathogenic strains including Listeria monocytogenes. It was inactivated by proteinase K and pronase E, but was resistant to papain, lysozyme, lipase and catalase. Lacticin LC14 was heat resistant, stable over a wide range of pH (2-10) and after treatment by solvents and detergents. Its N-terminal end was found unreactive towards Edman sequencing. Based on MALDI-TOF mass spectrometry, its molecular mass was 3333.7 Da. LC14 amino acid composition revealed a high proportion of hydrophobic residues, but no modified ones. LC14 may be able to challenge other well known other bacteriocins in probiotic and therapeutic applications.
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Lasta Samar, Ouzari Hadda, Andreotti Nicolas, Fajloun Ziad, Mansuelle Pascal, Boudabous Abdellatif, Sampieri François and Marc Sabatier Jean, Lacticin LC14, a New Bacteriocin Produced by Lactococcus lactis BMG6.14: Isolation, Purification and Partial Characterization, Infectious Disorders - Drug Targets 2012; 12 (4) . https://dx.doi.org/10.2174/187152612801319276
DOI https://dx.doi.org/10.2174/187152612801319276 |
Print ISSN 1871-5265 |
Publisher Name Bentham Science Publisher |
Online ISSN 2212-3989 |
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