THERMODYNAMIC AND STRUCTURAL INCOMPATIBILITY IN GLUTEN CONTAINING PROTEIN SYSTEM

Abstract

Model experiments were made with the ternary systems gluten (glutenin, gliadin)-casein- water and gluten (gliadin, glutenin)-sodium alginate-water. It was found that at low concentrations (1-2%) of gluten proteins the casein-gluten solutions are homogeneous. At higher concentrations, as a result of thermodynamic incompatibility, the solution separates into two phases. The same results were obtained with gluten-alginate-water systems. The solubility of gluten proteins may be extended using ionic polysaccharides. Myosin-gluten gel systems had lower strength than pure myosin gels due to struc- tural incompatibility of the system.