ABSTRACT
Grain sorghum has been documented to have low protein digestibility relative to other cereal grains. Low protein digestibility of sorghum is most pronounced in cooked foods and is ranked slightly lower than corn as a feed grain. In this article, sorghum germ plasm is identified that has substantially higher uncooked and cooked flour in vitro protein digestibility than normal cultivars. Sorghum lines were found within a high-lysine opulation derived from the mutant P721Q that have ≈10–15% higher uncooked and ≈25% higher cooked protein digestibilities using a pepsin assay. Highly digestible sorghum grain showed little reduction in digestibility after cooking, compared to the large reduction that is typical of normal sorghum cultivars. Using the three-enzyme pH-stat method, we showed that the highly digestible lines had the same degree of peptide bond hydrolysis in ≈5 min, as was found in 60 min in the normal cultivar, P721N. Differences in protein digestibility were related to enyzme susceptibility of the major storage prolamin, α-kafirin, that comprises ≈50–60% of the total sorghum grain protein. Using the enzyme-linked immunosorbent assay (ELISA) technique to track the pepsin digestion of α-kafirin, the highly digestible lines had ≈90–95% α-kafirin digested in 60 min compared to 45–60% for two normal cultivars. γ-Kafirin, a minor structural prolamin found mainly at the periphery of protein bodies, was also somewhat more digestible in the highly digestible sorghums. Highly digestible grain was of a floury kernel type, though recently this trait has been found in a modified background. More digestible protein from sorghum grain, that additionally is high in lysine content and has a fairly hard endosperm, could be of important benefit to populations who lack adequate protein in their diets, and may, pending further studies, prove to increase the value of sorghum as a feed grain.
