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Cereal Chem 53:478 - 487.  |  VIEW ARTICLE
Pearl Millet. I. Characterization by SEM, Amino Acid Analysis, Lipid Composition, and Prolamine Solubility.

S. M. Badi, R. C. Hoseney, and A. J. Casady. Copyright 1976 by the American Association of Cereal Chemists, Inc. 

Pearl millet (random mating population from 'Serere 17' X 'Tift 239') grain endosperm is composed of both hard (translucent) and soft (opaque) parts. The hard part has tightly packed, polygonal-shaped starch granules and a matrix protein containing relatively large, embedded protein bodies. The soft endosperm has loosely packed, spherical starch granules covered with a thin sheet of protein. The soft endosperm contains many voids, or air spaces, and no protein bodies. Dry milling of millet and sorghum grain gave similar flour extractions : 58% for millet, and 53% for sorghum grain. Total grain protein recovered in the flour was approximately constant at 45% for both grains. Millet had higher values for lysine, arginine, aspartic acid, threonine, serine, glycine, valine, and methionine, and lower values for glutamic acid, proline, alanine, and leucine than did sorghum grain. Lysine content of millet was 3.6 g/100 g protein, comparable to that in high-lysine corn. The protein bodies in pearl millet were soluble in 70% ethanol at 60 C (30.7% of total protein), and at least part (27.1% of total protein) of the matrix protein was soluble in 100% t-butyl alcohol at room temperature. Two successive extractions under more vigorous conditions (blender) gave about 55% of the total millet protein soluble in either 60 C, 70% ethanol or 60 C, 60% t-butyl alcohol.

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