Cereal Chem 53:1 -  12.  |  VIEW ARTICLE
Biochemical Properties and Ultrastructure of Protein Bodies Isolated from Selected Cereals.

C. A. Adams, L. Novellie, and N. v. d. W. Liebenberg. Copyright 1976 by the American Association of Cereal Chemists, Inc. 

The protein bodies of millet (Eleusine coracana Gaertn.), barley (Hordeum vulgare L.), babala (Pennisetum typhoideum Burm.), white maize (Zea mays L.), and sorghum (Sorghum bicolor (L.) Moench), isolated by a new method, are distinct organelles differing markedly in their ultrastructure. Wheat (Triticum aestivum L.) lacks identifiable protein bodies although a protein-rich fraction was obtained. The protein bodies and the wheat protein preparation are composed of predominantly insoluble protein and have insoluble protease activity. Phytase activity is more variable being undetectable in wheat and millet but present in the other cereal preparations. The products obtained varied from 51% protein in wheat to 79% protein in maize and thus the method used yields protein-rich fractions from different cereals in a relatively simple and rapid process.