Purification, partial amino acid sequence and mode of action of pediocin PD-1, a bacteriocin produced by Pediococcus damnosus NCFB 1832.
Date
2005
Authors
Bauer R.
Chikindas M.L.
Dicks L.M.
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
Pediocin PD-1 is a ribosomally synthesized antimicrobial peptide produced by Pediococcus damnosus NCFB1832. It inhibits the growth of several food spoilage bacteria, including malolactic bacteria isolated from wine. Pediocin PD-1 is 2866.87+/-0.4 Da in size, has an isoelectric point (pI) of ca. 9.0 and, on amino acid composition, has partial homology to the lantibiotic plantaricin C. The highest activity of pediocin PD-1 against cells of Oenococcus oeni was observed at an external pH of 5.0 and at 25 degrees C. The primary mode of action of pediocin PD-1 is most probably due to pore formation, as indicated by the efflux of K+ from metabolically active cells of O. oeni. In the presence of 10 mM gadolinium (Gd3+), pediocin PD-1 did not affect cells of O. oeni. This suggests that the mode of action of pediocin PD-1 relies on a net negatively charged cell surface. In comparison to nisin, pediocin PD-1 is less active against non-growing cells of O. oeni.
Description
Keywords
bacteriocin, pediocin PD 1, pediocin PD-1, amino acid sequence, article, chemistry, food contamination, food control, isoelectric point, isolation and purification, mass spectrometry, metabolism, microbiological examination, microbiology, molecular weight, Pediococcus, pH, sequence alignment, sequence homology, temperature, wine, Amino Acid Sequence, Bacteriocins, Food Contamination, Food Microbiology, Hydrogen-Ion Concentration, Isoelectric Point, Mass Spectrometry, Microbial Sensitivity Tests, Molecular Weight, Pediococcus, Sequence Alignment, Sequence Homology, Amino Acid, Temperature, Wine
Citation
International journal of food microbiology
101
1
101
1