Electrophoretic analysis of flour proteins. II.—gluten

Abstract

AbstractAn investigation of the electrophoretic composition of the gluten proteins in acidic and basic buffers was undertaken. Three main components predominated, although at different distributions, when gluten was analysed in acidic and basic buffers. In addition, there were small amounts of other components—probably some ‘salt‐soluble’ proteins trapped in the gluten. Acidic and basic extracts of the residues from the extraction of flour with o‐IM‐sodium chloride yielded components similar to those appearing in gluten. Basic and acidic extracts of flour yielded components similar to those appearing in gluten, and in addition, the ‘salt‐soluble’ proteins and polysaccharides. Adjustment to acid pH of alkaline extracts of flour and the above‐mentioned extraction residues did not give electrophoretic patterns identical with those of acidic extracts.Electrophoretic enantiography was best in the acid buffers. Sodium chloride‐hydrochloric acid buffers approached phosphate and aluminium lactate buffers in excellence. Dispersions of gluten in cupric ammonium sulphite were also analysed electrophoretically.Electrophoretic analyses of gluten from flour defatted with butanol and butanol‐ether differed little from those of gluten from intact flour. There was, however, a difference in the electrophoretic analysis of gluten obtained from flour exhaustively extracted with a series of lipid solvents.