Effect of grain structure and cooking on sorghum and maize in vitro protein digestibility

Uncooked and cooked sorghum showed improvement in in vitro protein digestibility as the structural complexity of the sample reduced from whole grain flour through endosperm flour to protein body-enriched samples. This was not the case for maize. Cooking reduced protein digestibility of sorghum but not maize. Treating cooked sorghum and maize whole grain and endosperm flours with alpha-amylase to reduce ample complexity before in vitro pepsin digestion slightly improved protein digestibility. The reduction in sorghum protein digestibility on cooking was not related to the total polyphenol content of samples. Pericarp components. germ. endosperm cell walls, and gelatinised starch were identified as possible factors limiting sorghum protein digestibility. Electrophoreis of uncooked and cooked protein-body-enriched samples of sorghum and maize, and prolamin fractions of sorghum under non-reducing conditions showed oligomeric proteins with molecular weights (M-t) 45, 66 and >66 kDa and monomeric kafirins and zeins. Protein-body-enriched samples of sorghum had inure 45-50 kDa oligomers than those of maize. In cooked sorghum, some of these were resistant to reduced. Pepsin-indigestible residues from protein-body-enriched samples consisted mainly of alpha-zein (uncooked and cooked maize) or alpha-kafirin (uncooked sorghum) whilst cooked sorghum had ill addition. beta- and gamma-kafirin and reduction-resistant 45-50 kDa oligomers. cooking appears to lead to formation of disulphide-bonded oligomeric proteins that occurs to a greater extent in sorghum than in maize. This may explain the poorer protein digestibility of cooked sorghum. (C) 2002 Elsevier Science Ltd.