Cereal Chem 50:597 - 604.  |  VIEW ARTICLE
Changes in Flour Proteins During Dough-Mixing. II. Gel Filtration and Electrophoresis Results.

K. Tanaka and W. Bushuk. Copyright 1973 by the American Association of Cereal Chemists, Inc. 

Gel filtration of AUC (0.1M acetic acid, 3M urea, 0.01M cetyltrimethylammonium bromide) extracts of dough on Sephadex G-150 showed that during mixing under conditions of accentuated dough breakdown there was a marked decrease in the amount of the high-molecular-weight (MW) glutenin. Concomitantly, there was an increase in the amount of low-MW glutenin and gliaden. Dough-mixing under normal and accentuated breakdown conditions produced only minor changes in the sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS-PAGE) patterns of the protein fractions obtained by Osborne-type fractionation. The patterns of the alcohol-soluble fraction (gliadin) of doughs that suffered extensive mixing breakdown, e.g., those containing 2.0 microequivalents N-ethylmaleimide, had several new bands in the high-MW region. Components of similar MW were observed in the patterns of the reduced acetic acid- soluble and the reduced proteins. The SDS-PAGE patterns of reduced acetic acid-soluble and residue proteins were essentially identical and were not affected by mixing under the conditions investigated.