ABSTRACT
The digestive enzymes alkaline phosphatase and 5'-nucleotide phosphodiesterase, solubilized from bovine intestinal mucosa and purified to homogeneity, were found to be strongly inhibited in vitro by condensed tannins (proanthocyanidins) purified from sorghum seeds and from quebracho. Tannin inhibition was prevented and reversed by the detergent Triton X-100 (protein-binding agent), by soluble polyvinylpyrrolidone (tannin-binding agent), or by phosphatidylcholine (membrane component). When tested as a crude particulate membrane fraction more characteristic of their in vivo condition, both enzymes were inhibited much less than either purified enzyme at the same tannin concentration. Because the enzymes appear to be relatively insensitive to inhibition by tannin in conditions which mimic in vivo conditions, and because the proportion of the dietary tannin which is available to interact with these enzymes in the digestive tract is likely to be rather small, we suggest that the antinutritional effects and ecological significance of dietary tannins are not due to tannin inhibition of these or other digestive enzymes by direct binding to them.
