Heterologous production of antimicrobial peptides in Propionibacterium freudenreichii

Article Abstract:

Heterologous bacteriocin production in Propionibacterium freudenreichii is described and an efficient system for DNA shuttling between Escherichia coli and Propionibacterium freudenreichii is developed using vector pAMT1. The constitutive promoter and the protease-activated antimicrobial peptide (PAMP) promoters directed constitutive gene expression and activity of both promoters is enhanced by elements upstream of the promoter core region.

Escherichia coli, Acne, Chemical properties, Bacteriocins

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Prevalence of the genes encoding propionicin T1 and Protease-activated antimicrobial peptide and their expression in classical propionibacteria

Article Abstract:

Screening of 64 isolated classical propionibacteria was conducted for identifying the frequency of production of the bacteriocin propionicin T1 and the protease-activated antimicrobial peptide (PAMP) and their corresponding genes coding. Studies show that in Propionibacterium jensenii and Propionibacterium thoenii, genes are present in large numbers but were absent in the other species of classical propionibacteria.

Pharmaceutical Preparation Manufacturing, All Other Basic Organic Chemical Manufacturing, Pharmaceutical preparations, Antiinfective Preparations, Industrial Organic Chemicals, Propionates, Anti-infective agents, Peptides

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Biochemical and genetic characterization of propionicin T1, a new bacteriocin from Propionibacterium thoenii

Article Abstract:

Research reveals that the bacteriocin propionicin T1 in propionibacteria is produced as a prebacteriocin of 96 amino acid residues, which on further processing yields a mature bacteriocin of 65 residues. Data indicate that propionicin does not show sequence similarity with other known bacteriocins.

United States, Norway, Statistical Data Included, Genetic aspects, Antibacterial agents, Nucleotide sequence, Base sequence, Bacteria

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