Immunodetection of legume proteins resistant to small intestinal digestion in weaned piglets
2003
Salgado, P. | Freire, J.P.B. | Ferreira, R.B. | Teixeira, A. | Bento, O. | Abreu, M.C. | Toullec, R. | Lalles, J.P.
Experiments were conducted to investigate the biochemistry of digestion of the major storage proteins from soya bean, pea, faba bean, blue lupin, and chickpea seeds in the ileum of piglets. Hyperimmune plasmas against the crude protein extracts and the purified 11S and 7S globulin fractions of each legume seed and an anti-pea albumin PA2 and lectin antibody were used. They served to probe immunoblots of feed protein extracts and ileal digesta samples. Globally, the recognition by plasmas of intact or partially digested proteins in ileal digesta was rather faint, in agreement with the fairly high in vivo digestibility data obtained with these legume seed proteins. Nevertheless, immunoreactive polypeptides found in digesta of piglets fed pea, faba bean and chickpea belonged mainly to proteins of the 7S family, and to other proteins including low-molecular weight components such as PA2 albumin and lectin in the case of pea. In piglets fed lupin, nearly intact polypeptides from the 11S family were detected. To conclude, the present immunochemical study conducted on ileal digesta of piglets revealed a few dietary legume proteins of the vicilin and albumin families. Legumin proteins were demonstrated unequivocally in the case of lupin and white chickpea.
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