Plant protein-polysaccharide interactions in solutions: application of soft particle analysis and light scattering measurements

Globulin was found to be highly charged and spherically shaped. The best coacervation condition was obtained at the pH value, which corresponds to the protein conformation with a dense and compact accessible layer. On the contrary, for the alpha gliadin, bearing a lower charge, a more extended conformation seems to be more favourable. For the plant proteins studied, the coacervation seems to be controlled by the structure of the counter polyanion used: from our model, it turns out that the rod-like structure of arabic gum observed at acidic pH allows the interaction with plant proteins to form coacervates, contrary to the highly charged and spherical structure of alginate.