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Cereal Chem 65:333-340   |  VIEW ARTICLE

Biochemical and Breadmaking Properties of Wheat Protein Components. I. Compositional Differences Revealed Through Quantitation and Polyacrylamide Gel Electrophoresis of Protein Fractions from Various Isolation Procedures.

K. Chakraborty and K. Khan. Copyright 1988 by the American Association of Cereal Chemists, Inc. 

Three hard red spring wheat varieties, grown under similar environmental conditions, were fractionated by three protein solubility procedures and compared for quantitative protein recovery, subunit composition, and molecular weight and size distribution. Variations in the isolation conditions and types of solvent used had a major effect on the amount of protein extracted in each fraction. Polyacrylamide gel electrophoresis of the various protein fractions isolated by the different solubility procedures showed distinct differences in subunit composition for the same class of protein. Contamination of gliadin with glutenin was found in two of the three isolation procedures. The acetic acid soluble, acetic acid insoluble, and lactic acid soluble fractions from the different procedures, although referred to as glutenin, were different in composition. Some residue fractions (those containing starch) contained substantial amounts of protein.

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