Abstract

In the western Sahel and many other regions of sub-Saharan Africa, wild edible plants contribute significantly to human diets, not only during periods when cereal staples are scarce, but also when they are readily available. Although there have been published reports regarding the nutrient contents of these plant foods, little attention has been devoted to their content of antinutrients such as calcium chelators and inhibitors of the pancreas-derived proteases, trypsin and chymotrypsin, which are required for the efficient digestion and absorption of dietary proteins. In this study, aqueous extracts of 61 different leaves, seeds, fruits and flowers of edible plants gathered in the Republic of Niger were analyzed for their content of trypsin inhibitory substances using alpha-N-benzoyl-DL-arginine-p-nitroanilide as the substrate and bovine trypsin as the enzyme source. Twelve of these plant foods contained more antitrypsin activity than soybeans (1.34-8.18 vs. 1.32 microg trypsin inhibited/mg dry weight). Boiling for 3 min did not inactivate the antitrypsin activity in most of the plant extracts. These data confirm that more than half of the wild edible plant foods widely consumed by various populations who inhabit the western Sahel contain significant quantities of heat-stable trypsin inhibitor that could possibly compromise the bioavailability of proteins present in the diets of these populations.

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