The plasmid-encoded lactococcal envelope-associated proteinase is encoded bya chromosomal gene in Lactococcus lactis subsp. cremoris BC101

Article Abstract:

A Lactococcus lactis subspecie cremoris BC101 proteinase was identified and characterized. This proteolytic enzyme was found to be very similar to the proteinase associated with the cell envelope and encoded by the plasmid-linked prtM gene in other lactococci strains. This enzyme from the plasmid-free strainBC101 showed similar characteristics with the plasmid-linked proteinase in its chromatographic characteristics, molecular wieght and in its existence as a dimer. Localization of the chromosomal proteinase prtM gene was confirmed by pulse-field electrophoresis and hybridization. DNA sequencing of the prtM- carrying DNA fragment suggest that the location of this lactococcal envelope- associated proteinase gene makes it possible for the enzyme to exist both on the plasmids and on the chromosome.

Genetic aspects, Proteases, Chromosomal proteins, Microbial genetics

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Antagonistic activity of Lactobacillus plantarum C11: two new two-peptide bacteriocins, plantaricins EF and JK, and the induction actor plantaracin A

Article Abstract:

Amino acid sequencing and mass spectrometry were utilized in the detection of six peptides similar to bacteriocins in Lactobacillus plantarum strain C11. Solid-phase peptide synthesis was undertaken to produce these peptides for bacteriocin-like activity testing. The activity of complementary peptides increased a thousand fold when the complements are present in equimolar concentrations.

Bacterial proteins, Lactobacillus plantarum

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Strong synergy between a eukaryotic antimicrobial peptide and bacteriocins from lactic acid bacteria

Article Abstract:

Results show that a combination of eukaryotic and prokaryotic antimicrobial peptides markedly increases the specific activity and broaden the target-cell range of these peptides. Data reveal that lactic acid bacteria antimicrobial peptides and and the eukaryotic antimicrobial peptide pleurocidin act synergistically against Escherichia coli strain.

Pharmaceutical Preparation Manufacturing, Pharmaceutical preparations, Antiinfective Preparations, Norway, Bacteriostats, Physiological aspects, Anti-infective agents, Antibacterial agents, Bacterial growth, Peptides

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