Cereal Chem 56:90 - 94.  |  VIEW ARTICLE
Studies of Glutenin Solubilized in High Concentrations of Sodium Stearate.

R. J. Waski, H. Daoust, and C. Martin. Copyright 1979 by the American Association of Cereal Chemists, Inc. 

Solubilization of freeze-dried glutenin in water in the presence of sodium stearate at 21 and 45 C was studied by viscometry and electrophoresis at temperatures between 30 and 50 C. Specific viscosity determined at 50 C and at one glutenin concentration indicates that, after incubation at 45 C for 48 hr, the protein molecules are disaggregated into smaller particles that do not appear to change in size or shape between 30 and 50 C. Sodium dodecylsulfate-polyacrylamide gel electrophoresis patterns of glutenin solubilized by sodium stearate differ both quantitatively and qualitatively from the pattern obtained from glutenin solubilized by disulfide bond cleavage with beta-mercaptoethanol, suggesting that disulfide bonds are not cleaved during solubilization in sodium stearate. Solubilization of glutenin in water in the presence of soaps can be explained by peptization of glutenin through the formation of protein-detergent complexes that are soluble in water. It is unnecessary to postulate the presence of many intermolecular disulfide bonds for the insolubility of glutenin in pure water or other mild solvents.