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KMID : 1007520000090040270
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Food Science and Biotechnology
2000 Volume.9 No. 4 p.270 ~ p.276
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Purification and Molecular Characterization of a Bacteriocin from Pediococcus sp. KCA1303-10 Isolated from Fermented Flatfish
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Ahn, Cheol
Ji, Geun Eog/Kim, Chung Hoi
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Abstract
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Pediococcus sp. KCA1303-10 isolated from fermented flatfish produced a bacteriocin which was active against food pathogens, such as Listeria monocytogenes, Enterococcus faecalis, and Enterococcus faecium. Bacteriocin production occurred during the late exponential phase of growth. Optimum temperature for bacteriocin production was 37℃ with an initial pH of 7.0. The bacteriocin of Pediococcus sp. KCA1303-10 was sensitive to proteases, but stable to solvents, pH change and heat treatment. The bacteriocin exhibited a bactericidal mode of action against Enterococcus faecium. The bacteriocin produced by Pediococcus sp. KCA1303-10 was purified by carboxymethyl-cellulose (CM-cellulose) canon exchange column chromatography and CM-sepharose canon exchange column chromatography. Purified bacteriocin exhibited a single band on the sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) with an apparent molecular weight of 4,200 dalton. This bacteriocin was named pediocin K1. Active portions of HPLC were cllected, and amino acid sequence of the amino terminal region was analyzed. The sequence of the first 15 amino acids was NH₃- Lys - Tyr - Tyr - Gly - Asn - Gly - Val - Thr - Cys - Gly - Lys - His - Ser - ? - Ser. Pediococcus sp. KCA1303-10 had four residential plasmids with molecular sizes of 12.8, 9.1, 4.3 and 3.8 kb. A comparison of plasmid profiles between Pediococcus sp. KCA1303-10 and its plasmid-cured mutants revealed that the 9.1 kb plasmid was responsible for bacteriocin production in Pediococcus sp. KCA1303-10.
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