Enterocin F4-9, a novel O-linked glycosylated bacteriocin

Mohamed Abdelfattah Maky, Naoki Ishibashi, Takeshi Zendo, Rodney Honrada Perez, Jehan Ragab Doud, Mohamed Karmi, Kenji Sonomoto

Research output: Contribution to journalArticlepeer-review

57 Citations (Scopus)


Enterococcus faecalis F4-9 isolated from Egyptian salted-fermented fish produces a novel bacteriocin, termed enterocin F4-9. Enterocin F4-9 was purified from the culture supernatant by three steps, and its molecular mass was determined to be 5,516.6 Da by mass spectrometry. Amino acid and DNA sequencing showed that the propeptide consists of 67 amino acid residues, with a leader peptide containing a double glycine cleavage site to produce a 47-amino-acid mature peptide. Enterocin F4-9 is modified by two molecules of N-acetylglucosamine β-O-linked to Ser37 and Thr46. The O-linked N-acetylglucosamine moieties are essential for the antimicrobial activity of enterocin F4-9. Further analysis of the enterocin F4-9 gene cluster identified enfC, which has high sequence similarity to a glycosyltransferase. The antimicrobial activity of enterocin F4-9 covered a limited range of bacteria, including, interestingly, a Gram-negative strain, Escherichia coli JM109. Enterocin F4-9 is sensitive to protease, active at a wide pH range, and moderately resistant to heat.

Original languageEnglish
Pages (from-to)4819-4826
Number of pages8
JournalApplied and environmental microbiology
Issue number14
Publication statusPublished - 2015

All Science Journal Classification (ASJC) codes

  • Applied Microbiology and Biotechnology
  • Food Science
  • Biotechnology
  • Ecology


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