Abstract
AbstractCowpea (Vigna unguiculata) is a very important crop for people living in the north‐east of Brazil where it constitutes the principal source of protein and carbohydrate. In this study, it was observed that the in vitro digestibility of the seed albumin and globulin fractions extracted from eight Brazilian cowpea cultivars was high when treated with pepsin but resistant to degradation by trypsin or chymotrypsin even after 3 h of treatment. When the albumin and globulin fractions were given to rats by intragastric intubation it was observed that intact proteins or their fragments were immunodetected in the faeces. Immunohistochemical analyses of the gut sections of these rats showed that a proportion of the albumin fraction (or its fragments), but not the globulin one, was bound to the brush border enterocytes in the duodenum. Thus the incomplete enzymatic degradation of both globulin and albumin fractions as well as the albumin binding to the gut may have a bearing upon the growth depression, malabsorption and diarrhoea observed on rats fed on cowpea seeds. Copyright © 2004 Society of Chemical Industry
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
