A highly digestible sorghum mutant cultivar exhibits a unique folded structure of endosperm protein bodies.
The endosperm of a sorghum mutant cultivar, with high in vitro uncooked and cooked protein digestibilities, was examined by transmission electron microscopy and alpha-, beta-, and gamma-kafirins (storage proteins) were localized within its protein bodies. Transmission electron microscopy micrographs revealed that these protein bodies had a unique microstructure related to high protein digestibility. They were irregular in shape and had numerous invaginations, often reaching to the central area of the protein body. Protein bodies from normal cultivars, such as P721N studied here, with much lower uncooked and cooked digestibilities are spherical and contain no invaginations. Immunocytochemistry results showed that the relative location of alpha- and beta-kafirins within the protein bodies of the highly digestible genotype were similar to the normal cultivar, P721N. Gamma-kafirin, however, was concentrated in dark-staining regions at the base of the folds instead of at the protein body periphery, as is typical of normal cultivars. The resulting easy accessibility of digestive enzymes to alpha-kafirin, the major storage protein, in addition to the increased surface area of the protein bodies of the highly digestible cultivar appear to account for its high in vitro protein digestibility.
Oria
M P
MP
Department of Food Science, Purdue University, 1160 Food Science Building, West Lafayette, IN 47907-1160, USA.
Hamaker
B R
BR
Axtell
J D
JD
Huang
C P
CP
D003296:Cooking; D004063:Digestion; D002523:Edible Grain / Q000235:genetics / Q000648:ultrastructure*; D008854:Microscopy, Electron; D010940:Plant Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D012639:Seeds / Q000648:ultrastructure*
D010940:Plant Proteins; C080615:kafirin protein, Sorghum bicolor