Abstract
The fecal tryptophanase activities were 0.267±0.10 for rats and 0.185±0.01 μmole/min/g wet feces for humans. The activities of indole pyruvate degradation to indole, indole pyruvate lyase, of these feces were 0.051±0.02 and 0.046±0.01 μmole/min/g wet feces, respectively. The optimal pH values of tryptophanase and indole pyruvate lyase were 5.5–7.5 and 5.5–6.5, respectively. When the intestinal flora orE. coli HGU-3 was cultured in GAM broth having six different pH values (5 to 10), the activities of tryptophanase and indole pyruvate lyase in the medium adjusted at pH 6 were dramatically induced by elevating the pH to 9. However, when intestinal microflora were inoculated in the medium containing lactulose, the productions of these enzymes were dramatically inhibited and the pH of the medium was lower than that of the control.
Similar content being viewed by others
References Cited
Botsford, J. L. and DeMoss R. D. Escherichia coli tryptophanase in the enteric environment.J. Bacteriol., 109, 74–80 (1972).
Chung, K.-T., Fulk, G. E. and Slein M. W.. Tryptophanase of fecal flora as a possible factor in the etiology of colon cancer.J. Natl. Cancer Inst., 54, 1073–1078 (1975).
DeMoss, R. D. and Moser, K. Tryptophanase in diverse bacterial species.J. Bacteriol., 98, 167–171 (1969).
Drasaer, B. S. and Hill, M. J. Metabolism of nitrogen compounds inHuman intestinal flora. Academic Press, London, pp. 72–103 (1974).
Dunning, W. F., Curtis, M. R. and Maun, M. E. The effect of added dietary tryptophan on the ocurrance of 2-acetylaminofluorene-induced liver and bladder cancer in rats.Cancer Res., 10, 454–459 (1950).
Finegold, S. M. and Flora, D. J. A. Fecal bacteriology of colonic polyp patients and control patients.Cancer Res., 35, 3407–3417 (1975).
Goldin, B. R. and Gorbach, S. L. Alteration in microflora enzymes related to diet, age, lactobacillus supplements and dimethylhydrazine.Cancer 40, 2421–2426 (1977).
Goldin, B. R., Swenson, L., Dwyer, J., Sexton, M. and Gorbach, S. L. Effect of diet and Lactobacillus acidophilus supplements on human fecal bacterial enzymes.J. Natl. Cancer Inst., 64, 255 (1980).
Hoch, J. A. and DeMoss, R. D. Physiological effects of a constitutive tryptophanase inBacillus alvei J.Bacteriol., 90, 604–610 (1965).
Kim, D.-H., Kang, H.-J., Kim, S.-W. and Kobashi, K. pH-inducible β-glucosidase and β-glucuronidase of intestinal bacteria.Chem. Pharm. Bull., 40, 1667 (1992).
Kim, D.-H., Kang, H.-J., Park, S.-H. and Kobashi, K.- Glucosidase and β-glucuronidase of alkalotolerant intestinal bacteria.Biol. Pharm. Bull. 17, 423 (1994).
Kim, D.-H. and Han, M. J. Inhibition of intestinal bacterial enzymes by lactic acid bacteriaYakhak Hoeji 39, 169–174 1995.
Reddy, B. S. and Wynder, E. L. Metabolic epidemiology of colon cancer.Cancer, 39, 2533–2539 (1977).
Samelson, S. L., Nelson, R. N. and Nynus, L. M. Protective role of fecal pH in experimental colon carcinogenesis.J. Royal Society Med., 78, 230–233 (1985).
Thornton, J. R. High colonic pH promotes colorectal cancer.Lancet 1981–1982 (1982).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kim, DH., Lee, JH., Bae, EA. et al. Induction and inhibition of indole production of intestinal bacteria. Arch. Pharm. Res. 18, 351–355 (1995). https://doi.org/10.1007/BF02976331
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF02976331