Salt-Induced Disaggregation/Solubilization of Gliadin and Glutenin Proteins in Water

摘要: Abstract The effect of salt concentration used in preparing gluten, on the subsequent dissolution gluten water, was examined. Flour from a Canadian hard red spring wheat cultivar, Katepwa, to prepare glutens using three different solvents, i.e. distilled deionized water (DDW), 0·2% NaCl solution and 2% solution. isolated wet were extracted sequentially with DDW, providing four soluble fractions an insoluble residue. amount protein each fraction determined respective compositions assessed electrophoretically under reducing non-reducing conditions. Surprisingly, DDW extracts prepared contained almost all gliadins, except some ω-gliadin components, most polymeric glutenin. For NaCl, gliadin, but only small portion glutenin, extracted. part gliadins no glutenin extractable water. solubilities proteins 27, 52, 85%, respectively, after sequential DDW. large increases solubility gliadin when is (after removal salt) can be explained basis salt-induced conformational change proteins, which renders more effective solvent.