Cereal Chem 47:626 - 639.  |  VIEW ARTICLE
Characterization of Wheat Flour Proteins by Differential Solubility in Conjunction with Disc Electrophoresis.

P. C. Williams and C. Butler. Copyright 1970 by the American Association of Cereal Chemists, Inc. 

By the Maes extraction procedure (used for removal of proteins from flours and whole meals from different types and species of wheat) up to 97% of proteins present were extractable, and were further characterized by disc electrophoresis. Certain solvents extracted proteins with closely similar electrophoretic mobility. The proteins extracted by 0.10N KOH (about 25% of the toal) could not be resolved into different electrophoretic components. Wheats and flours studied included: A, species of different and B, the same chromosome number; C, different varieties of wheat of the same species; and D, HRS flours denatured by various physical and chemical means. No consistent relation appeared between total protein extracted from flours or amount extracted by any one solvent and the baking and rheological behavior of flours of groups A, B, and C, except as protein content itself varied. Proteins of group A flours showed great differences in electrophoretic mobility between wheats of different chromosome number. Group B flours were more similar electrophoretically; group C flours showed relatively little difference between varieties. Group D flours (with baking and rheological properties drastically altered from the control) showed differences in solubilities of proteins in various solvents, but were electrophoretically identical. It was concluded that this procedure was of more value for identifying genetic types than for differentiating between flours as to baking and rheological properties.