Purification and Characterization of Multiple Bacteriocins and an Inducing Peptide Produced by Enterococcus faecium NKR-5-3 from Thai Fermented Fish

• Published in: Bioscience, biotechnology, and biochemistry Vol. 76; no. 5; pp. 947 - 953
• Main Authors: ISHIBASHI, Naoki, HIMENO, Kohei, FUJITA, Koji, MASUDA, Yoshimitsu, PEREZ, Rodney Honrada, ZENDO, Takeshi, WILAIPUN, Pongtep, LEELAWATCHARAMAS, Vichien, NAKAYAMA, Jiro, SONOMOTO, Kenji
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 2012; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: Amino Acid Sequence; Animals; Bacteria; bacteriocin; Bacteriocins - biosynthesis; Bacteriocins - genetics; Bacteriocins - isolation & purification; Base Sequence; Biological and medical sciences; Chromatography, Reverse-Phase; enterocin; Enterococcus faecium; Enterococcus faecium - genetics; Enterococcus faecium - metabolism; Fermentation; Fishes - microbiology; Fundamental and applied biological sciences. Psychology; inducing peptide; lactic acid bacteria; Lactobacillus - drug effects; Lactobacillus - metabolism; Lactobacillus sakei; Listeria; Microbial Sensitivity Tests; Microbial Viability - drug effects; Molecular Sequence Data; Peptides - genetics; Peptides - isolation & purification; Peptides - metabolism; Recombinant Proteins - biosynthesis; Recombinant Proteins - genetics; Recombinant Proteins - isolation & purification; Sequence Analysis, DNA; Lactic acid bacteria; Purification; Peptides; Bacteriocin; Fermented product; Characterization; Streptococcaceae; Enterococcus faecium; Vertebrata; Pisces; enterocin; inducing peptide; Bacteria; Micrococcales
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.110972

Enterocins NKR-5-3A, B, C, and D were purified from the culture supernatant of Enterococcus faecium NKR-5-3 and characterized. Among the four purified peptides, enterocin NKR-5-3A (5242.3 Da) was identical to brochocin A, produced by Brochothrix campestris ATCC 43754, in mature peptides, and its putative synergistic peptide, enterocin NKR-5-3Z, was found to be encoded in ent53Z downstream of ent53A, encoding enterocin NKR-5-3A. Enterocin NKR-5-3B (6316.4 Da) showed a broad antimicrobial spectrum, and enterocin NKR-5-3C (4512.8 Da) showed high activity against Listeria. Enterocin NKR-5-3D (2843.5 Da), showing high homology to an inducing peptide produced by Lactobacillus sakei 5, induced the production of the enterocins. The enterocins showed different antimicrobial spectra and intensities. E. faecium NKR-5-3 concomitantly produced enterocins NKR-5-3A, B, C, and D which probably belong to different classes of bacteriocins. Furthermore, NKR-5-3 production was induced by enterocin NKR-5-3D.