Comparative digestibility and the inhibition of mammalian digestive enzymes from mature and immature cowpea (Vigna unguiculata (L.) Walp.) seeds

Globulins and albumins from mature cowpea seeds had inhibitory activity levels of 9.5 and 67.1 units trypsin inhibited per mg protein and globulins and albumins from immature seeds had trypsin inhibitory activity levels of 6.3 and 26.6 units trypsin inhibited per mg protein, respectively. Albumins from immature seeds had inhibitory activity level of 4 units salivary amylase inhibited per mg albumin. The globulins (native and heated) from both seeds were submitted to hydrolysis by trypsin and analyzed by SDS-PAGE. Native globulins from mature and immature seeds showed digestion products of ∼30 and ∼20 kDa, respectively. Trypsin strongly digested heated globulins from both kinds cowpeas.