FUNCTIONAL-PROPERTIES OF GLYCOSYLATED DERIVATIVES OF THE 11S STORAGE PROTEIN FROM PEA (PISUM-SATIVUM L)

The viscosity, solubility, foaming, and emulsifying properties of glycosylated derivatives of pea legumin were compared with those of the unmodified protein. These properties reflected conformational changes induced by covalent attachment of glycosyl residues (galactose, lactose, galacturonic acid). The neoglycoproteins were more viscous than the native protein, reflecting a greater hydrodynamic volume and increased protein-water interactions. The solubility of the legumin was also improved by glycosylation, especially with galactose. Galacturonic acid derivatives had pH(i) shifted toward more acidic values. Likewise, foaming capacity as well as the stability of foams and emulsions was improved by glycosylation, and the degree of improvement in their properties depended on the type of carbohydrate bound to the protein. Neutral sugars favored the foaming properties, while the charged carbohydrates improved the emulsifying properties.