Tauroconjugation of cholic acid stimulates 7 alpha-dehydroxylation by fecal bacteria.

Appl Environ Microbiol

Rega Institute for Medical Research and Biostatistical Centre, Department of Epidemiology, Catholic University of Leuven, Belgium.

Published: February 1996

We examined the effect of the type of cholic acid conjugation (taurine-conjugated, glycine-conjugated, or unconjugated cholic acid) on cholic acid 7 alpha-dehydroxylation by intestinal flora. Cholic acid 7 alpha-dehydroxylation in fecal cultures, in cultures of a defined limited flora consisting of a mixture of seven bacterial species isolated from the intestinal tract, and in a binary culture of a 7 alpha-dehydroxylating Clostridium species plus a cholic acid-deconjugating Bacteroides species was studied. We found that tauroconjugation of cholic acid significantly (P < 0.05) increased bacterial 7 alpha-dehydroxylation of cholic acid into deoxycholic acid from 34 to 55% in fecal cultures, from 45 to 60% in defined limited fecal cultures, and from 75 to 100% in binary cultures. Equimolar concentrations of free taurine did not stimulate 7 alpha-dehydroxylation in fecal cultures or in the defined limited flora, but free taurine did stimulate 7 alpha-dehydroxylation in the binary culture. In the binary culture of Clostridium species strain 9/1 plus Bacteroides species strain R1, the minimal flora capable of increased 7 alpha-dehydroxylation of taurocholic acid, strain R1 deconjugated taurine and rapidly reduced it to H2S. Bacteroides species strain R1 did not grow unless taurine or another appropriate reducible sulfur source was present. Clostridium species strain 9/1 did not grow or 7 alpha-dehydroxylate unless H2S or another source of reduced sulfur was present. We conclude that the increased 7 alpha-dehydroxylation of tauroconjugated cholic acid depends on the reduction of taurine to H2S, which is a necessary growth factor for the 7 alpha-dehydroxylating bacteria.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC167832PMC
http://dx.doi.org/10.1128/aem.62.2.656-661.1996DOI Listing

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