Browsing by Author "Van der Merwe, Iansha (Iansha Rosalia), 1975-"

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    Characterization of thoeniicin 447 produced by Propionibacterium thoenii
    (Stellenbosch : Stellenbosch University, 2002-12) Van der Merwe, Iansha (Iansha Rosalia), 1975-; Dicks, Leon Milner Theodore; Britz, T. J.; Stellenbosch University. Faculty of Science. Dept. of Microbiology.
    ENGLISH ABSTRACT: Antimicrobial peptides continue to be one of the most important classes of food additives. The food industry is especially interested in the application of naturally occuring and biologically derived preservatives. Among the metabolites of industrial importance produced by propionibacteria are peptides called bacteriocins. Bacteriocins are ribosomally synthesized peptides with antagonistic activity against closely related microorganisms. Many microorganisms associated with food produce bacteriocins, which have stimulated interest in the use of these peptides as natural food preservatives. Numerous bacteriocins are produced by lactic acid bacteria, but only a few have been reported for propionibacteria. Since propionic acid bacteria have GRAS (generally regarded as safe) status, their metabolic compounds should be safe for human consumption. Propionibacterium thoenii 447, isolated from Emmentaler cheese, produces a bacteriocin-like peptide, named thoeniicin 447, with a narrow spectrum of activity. The peptide displays a bactericidal mode of action against Lactobacillus delbrueckii subsp. bulgaricus and a bacteriostatic action against Propionibacterium acnes. Optimal bacteriocin production was detected during the early stationary growth phase. The peptide is resistant to heat treatments of 60°C and 80°C for 15 and 30 min and to 100°C for 15 min, but loses 80% of its activity after autoclaving (10 min at 121°C). Thoeniicin 447 remains active after incubation in buffers with pH values ranging from 1-10. The peptide is inactivated by pepsin, pronase, a-chymotrypsin, trypsin and Proteinase K. Thoeniicin 447 was partially purified by ammonium sulfate precipitation, followed by SP-Sepharose cation exchange chromatography. The estimated size of thoeniicin 447, according to tricine-SDSPAGE, is approximately 6 kDa. Based on DNA sequencing, the mature peptide is 7130 Da in size and homologous to propionicin Tl produced by P. thoenii strain 419. Thoeniicin 447 is a relatively small, cationic and heat-stable peptide and can therefor be classified as a member of class II bacteriocins. These features are very similar to those of bacteriocins produced by lactic acid bacteria. However, no unique classification system has been proposed for bacteriocins of propionibacteria. As a member of the genus Propionibacterium, P. thoenii 447 is generally regarded as safe. This, together with the narrow spectrum of activity, particularly the action against P. acnes, heat tolerance of thoeniicin 447 and its activity over a wide pH range renders the peptide suitable for possible pharmaceutical applications.