Extraction and fractionation of wheat flour proteins

Abstract

Abstract With the aid of a 1.5% sodium dodecyl sulphate solution (SDS) the proteins of two Dutch wheat flours were separated into an SDS‐soluble and an SDS‐insoluble fraction. The SDS‐soluble fraction was fractionated with the aid of ethanol precipitation and gel filtration chromatography into albumins, globulins, gliadins, glutenins II and III, and glutelins I, II, III and IV. The SDS‐insoluble proteinaceous material was separated into glutenins I and glycoproteins. The protein fractions were identified with the aid of SDS‐polyacrylamide gel electrophoresis and amino acid analysis. The glutenins I and II consist of A, B and C subunits. Their molecular weights ranged from about 600 000 to 10 million. The glutenins III consist only of B and C subunits and their molecular weights ranged from 300 000 to 600 000. A hypothesis explains how the glutenins III are the precursors for glutenins I and II and how they contribute to gluten's structure. The glutelins I consist of α β and γ subunits and their molecular weights ranged from about 600 000 to several millions. The glutelins II consist also of α β and γ subunits with a molecular weight of about 300 000 to 600 000, while the molecular weights of the glutelins III and IV ranged from 10 000 to 200 000. All glutelins are insoluble in 70 % aqueous ethanol and 5 M urea, but soluble in SDS and 0.1 M NaOH. Only the glutelins III and IV are soluble in 0.1 M HAc. The globulins consist of a heterogeneous fraction of components, their molecular weights arranged from 98 000 to 10 000. The gliadins form a heterogeneous but homologous group of polypeptides with an average molecular weight of 35 000. The albumins consist of components with molecular weights lower than 15 000.