Cereal Chem 46:495 - 502. | VIEW
Functional (Breadmaking) and Biochemical Properties of Wheat Flour Components. IV. Gluten Protein Fractionation by Solubilizing in 70% Ethyl Alcohol and in Dilute Lactic Acid.
R. C. Hoseney, K. F. Finney, Y. Pomeranz, and M. D. Shogren. Copyright 1969 by the American Association of Cereal Chemists, Inc.
Gluten was fractionated into gliadin and glutenin with 70% ethanol. The ratio of gliadin to glutenin was essentially constant at 53% gliadin and 47% glutenin for four wheat varieties that varied widely in breadmaking quality. The glutenin proteins retained their functional properties, provided that certain rheological properties were restored by remixing. Reconstitution of the glutenin fractions of good-quality and poor-quality varieties with a fixed gliadin-rich fraction has shown that the gliadin proteins controlled the loaf-volume potential of a wheat flour. Similar reconstitution studies have shown that the glutenin fraction governed the mixing requirement of a wheat flour. Additional evidence supporting the above conclusions was obtained by reconstituting and baking protein fractions that were obtained by partially solubilizing gluten in dilute (0.002N) lactic acid. The fractions were characterized as gliadin-rich (soluble) and glutenin-rich (insoluble) by starch-gel electrophoresis.