Cereal Chem 55:864 - 876.  |  VIEW ARTICLE
Physicochemical Properties of Wheat Gel Proteins: Effects of Isolation Conditions.

M. F. Jeanjean and P. Feillet. Copyright 1978 by the American Association of Cereal Chemists, Inc. 

Gel proteins (GP) were isolated from wheat flour after sequential extraction under different conditions; a number of extractions with combinations of five solvents (H2O, 0.5M NaCl, 60% ethanol, 0.01M acetic acid, 70% 2-chloroethanol) were compared. From 11 to 29% of the flour proteins were present in the gel fractions. Polyacrylamide gel electrophoresis in aluminum lactate buffer (PAGE) showed large differences between GP; these differences were reduced or absent when GP are dissolved in 6M urea or 0.25% sodium stearate. Molecular weights of GP subunits, determined by sodium dodecylsulfate PAGE, ranged from 12,000 to 136,000; only minor differences occur between samples. In most of the cases, amino acid composition of GP was found to be close to that of glutenin. From the results, GP, a complex of albumin, globulin, gliadin, and specific glutenin fractions, is postulated to differentiate from glutenin only by the strength of hydrogen and hydrophobic bonds between protein units.