The effect of glycosylation on the aggregation behavior of b-conglycinin (7S) under the macromolecular crowding condition in the liquid system and the influence of covalent attachment of polysaccharide on gelation of b -conglycinin (7S) were investigated. The gel network of the conjugate became orderly and compact at 7S/dextran (mass ratio) of 2:1. First

b-conglycinin-dextran covalent conjugate was prepared via the Maillard reaction under macromolecular crowding condition. Sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS-PAGE) was used to confirm the formation of covalent conjugate of 7S-dextran. Transglutaminase (TGase) was introduced for gelation to form a covalent network. Dynamic rheological analysis indicated that the addition of dextran increased the degree of crowding in the liquid system

promoting the formation of gel network. The presence of dextran with high concentration and the covalent attachment to b-conglycinin led to phase separation and inhibited extensive protein-protein interactions during the process of TGase cross-linking. Moreover

frequency sweep measurements revealed that the strength of the gel prepared by conjugation was reduced with increasing concentration of dextran. Scanning electron microscopy observation indicated that the network of gel began to transform to lamellar structure with increasing dextran concentration.