Plant protein interactions with polysaccharides and their influence on legume protein functionality - A review

Associative interactions between proteins and polysaccharides, both coulomb ic and non-coulombic, lead to the formation of interpolymer complexes. Comp lex formation with charged polysaccharides, either anionic or cationic, imp arts solubility to seed globulins in the vicinity of their isoelectric poin ts. This has been shown for the complexes "sun-flower 11 S globulin (helian thinin) - sodium alginate" and "faba bean legumin (or the product of its li mited 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 legumi n-T with chitosan substantially increases the emulsion stability of the bot h proteins.