TY - JOUR
T1 - Purification and characterization of multiple bacteriocins and an inducing peptide produced by Enterococcus faecium NKR-5-3 from Thai fermented fish
AU - Ishibashi, Naoki
AU - Himeno, Kohei
AU - Fujita, Koji
AU - Masuda, Yoshimitsu
AU - Perez, Rodney Honrada
AU - Zendo, Takeshi
AU - Wilaipun, Pongtep
AU - Leelawatcharamas, Vichien
AU - Nakayama, Jiro
AU - Sonomoto, Kenji
N1 - Funding Information:
This work was partially supported by Grants-in-Aid for Scientific Research from Japan Society for the Promotion of Science (JSPS), the JSPS-NRCT (National Research Council of Thailand) Core University Program on ‘‘Development of Thermotolerant Microbial Resources and Their Applications,’’ the Research Grant for Young Investigators of the Faculty of Agriculture, Kyushu University, and the Kato Memorial Bioscience Foundation.
PY - 2012
Y1 - 2012
N2 - 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 (6316.4Da) 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.
AB - 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 (6316.4Da) 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.
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U2 - 10.1271/bbb.110972
DO - 10.1271/bbb.110972
M3 - Article
C2 - 22738965
AN - SCOPUS:84861430808
SN - 0916-8451
VL - 76
SP - 947
EP - 953
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 5
ER -