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Escherichia coli tryptophanase in the enteric environment
Journal of Bacteriology
|January 1, 1972
Summary
Escherichia coli (E. coli) produces minimal tryptophanase activity in the gut, even when dietary tryptophan is high. This suggests E. coli
Area of Science:
- Microbiology
- Enzymology
- Gastrointestinal Metabolism
Background:
- Tryptophanase is an enzyme involved in tryptophan metabolism.
- Its role in the enteric environment, particularly concerning Escherichia coli (E. coli), is not fully understood.
- Understanding E. coli's contribution to tryptophanase activity is crucial for comprehending gut microbial metabolism.
Purpose of the Study:
- To investigate the activity of tryptophanase in the enteric environment.
- To determine the significance of tryptophanase in the metabolism of E. coli.
- To quantify the contribution of E. coli to overall enteric tryptophanase activity.
Main Methods:
- Determined tryptophanase activity, tryptophan content, and indole concentration in the intestinal and fecal contents of mice.
- Utilized conventional, germ-free, and monocontaminated axenic mice models.
- Quantified E. coli numbers relative to other facultative enteric coliforms.
Main Results:
- Increasing dietary tryptophan enhanced enteric microflora tryptophanase activity by nearly twofold.
- This dietary change did not increase E. coli numbers, either absolutely or relatively.
- E. coli was found to be responsible for less than 0.02% of the total enteric tryptophanase activity.
- Tryptophanase activity, tryptophan content, indole concentration, and E. coli numbers were consistent between cecal and fecal contents.
Conclusions:
- E. coli contributes negligibly to the total tryptophanase activity within the enteric environment.
- Dietary tryptophan availability significantly influences the overall microflora's tryptophanase activity but not E. coli proliferation.
- The enteric environment's tryptophanase activity is primarily driven by microbes other than E. coli.