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Production of butyrate from lysine and the Amadori product fructoselysine by a human gut commensal

Author

Listed:
  • Thi Phuong Nam Bui

    (Laboratory of Microbiology, Wageningen University)

  • Jarmo Ritari

    (University of Helsinki)

  • Sjef Boeren

    (Laboratory of Biochemistry, Wageningen University)

  • Pieter de Waard

    (Wageningen NMR Centre)

  • Caroline M. Plugge

    (Laboratory of Microbiology, Wageningen University)

  • Willem M. de Vos

    (Laboratory of Microbiology, Wageningen University
    University of Helsinki
    Haartmaninkatu 3, University of Helsinki)

Abstract

Human intestinal bacteria produce butyrate, which has signalling properties and can be used as energy source by enterocytes thus influencing colonic health. However, the pathways and the identity of bacteria involved in this process remain unclear. Here we describe the isolation from the human intestine of Intestinimonas strain AF211, a bacterium that can convert lysine stoichiometrically into butyrate and acetate when grown in a synthetic medium. Intestinimonas AF211 also converts the Amadori product fructoselysine, which is abundantly formed in heated foods via the Maillard reaction, into butyrate. The butyrogenic pathway includes a specific CoA transferase that is overproduced during growth on lysine. Bacteria related to Intestinimonas AF211 as well as the genetic coding capacity for fructoselysine conversion are abundantly present in colonic samples from some healthy human subjects. Our results indicate that protein can serve as a source of butyrate in the human colon, and its conversion by Intestinimonas AF211 and related butyrogens may protect the host from the undesired side effects of Amadori reaction products.

Suggested Citation

  • Thi Phuong Nam Bui & Jarmo Ritari & Sjef Boeren & Pieter de Waard & Caroline M. Plugge & Willem M. de Vos, 2015. "Production of butyrate from lysine and the Amadori product fructoselysine by a human gut commensal," Nature Communications, Nature, vol. 6(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms10062
    DOI: 10.1038/ncomms10062
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