Associative interactions between proteins and polysaccharides, both coulombic and non-coulombic, lead to the formation of interpolymer complexes. Complex formation with charged polysaccharides, either anionic or cationic, imparts solubility to seed globulins in the vicinity of their isoelectric points. This has been shown for the complexes "sunflower 11 S globulin (helianthinin)--sodium alginate" and "faba bean legumin (or the product of its limited proteolysis with trypsin--legumin-T)--chitosan". Hysteresis effects allow to control the solubility of seed globulins in weakly acid or weakly basic media. Formation of soluble complexes of faba bean legumin or legumin-T with chitosan substantially increases the emulsion stability of the both proteins.