Molecular Size Distribution of Glutenin from Wheat Flour and the Polymerization of Proteins during Purification(Food & Nutrition)

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The molecular size distribution of unreduced glutenin was studied by gel filtration on a Toyopearl HW-75F column, with 0.05 m Tris-HCl buffer (pH 8.3) containing 0.2% sodium dodecyl sulfate (SDS) as the elution solvent. The unreduced glutenin was extracted with 0.5 % SDS (pH 7.0) from the flour residue after exhaustive extraction of the gliadin and water-soluble proteins. The yield of glutenin with a little gliadin as a contaminant was about 20 % of the total flour proteins, and the flour protein was almost completely extracted by this procedure. The gel filtration patterns gave two peaks, a small one at the void volume of the column and a broad peak eluting from near the void volume to the elution volume for gliadin. The proteins eluted from the column were analyzed by SDS-polyacrylamide gel electrophoresis with or without prior reduction of their disulfide bonds. Only a slight difference among the glutenin samples in the fractions eluted from the column was observed in their subunit patterns. The peak eluted at the void volume contained no giutenin. However, a markedly increased proportion in the first peak was observed when the glutenin sample was prepared by an ethanol-fractionation method. The results suggest polymerization of the glutenin proteins during the purification procedure.
1990-04-23