Journal
LETTERS IN APPLIED MICROBIOLOGY
Volume 50, Issue 4, Pages 406-411Publisher
WILEY
DOI: 10.1111/j.1472-765X.2010.02810.x
Keywords
bacteriocin; circular peptide; gassericin A; HPLC purification; Lactobacillus gasseri; Lactobacillus reuteri; reutericin 6
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Funding
- Japan Society for the Promotion of Science [19000716]
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Aim: The study aimed for the complete purification and recharacterization of the highly hydrophobic circular bacteriocins, gassericin A and reutericin 6. Methods and Results: Gassericin A and reutericin 6 were purified to homogeneity using previously described method and reverse-phase HPLC with an octyl column and eluents of aqueous acetonitrile and 2-propanol. Mass analysis, N-terminal sequencing and bacteriocin assay of the HPLC-purified bacteriocins showed the two bacteriocins had identical seamless circular structures with the same m/z value (5651) of [M + H]+ and both had the same specific activity. d/l-amino acid composition analysis using two distinct methods with the chiral fluorescent derivatization reagents (+)-1-(9-fluorenyl)ethyl chloroformate and o-phthalaldehyde/N-acetyl-l-cystein revealed neither gassericin A nor reutericin 6 contained d-alanine residues contrary to our previous results. Conclusion: Purified gassericin A and reutericin 6 are chemically identical circular molecules containing no d-alanine residues. Significance and Impact of the Study: The HPLC conditions developed in this study will facilitate advanced purification and correct characterization of other highly hydrophobic bacteriocins.
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