The effect of glycosylation with dextran chains of differing lengths on the thermal aggregation of β-conglycinin and glycinin

This study was designed to determine the effect of β-conglycinin glycosylation on the thermal aggregation of β-conglycinin and glycinin under extreme conditions of pH and ionic strength and to investigate the effect of glycan chain length (i.e., dextrans with different molecular masses) on the thermal aggregation of soy protein by the Maillard conjugation. It was confirmed that the glycosylation of β-conglycinin can inhibit its thermal aggregation at various pH or ionic strength values. The results highlighted the fact that neutral polysaccharides can suppress the thermal aggregation of protein through changes in hydrophobicity and steric hindrance, regardless of the molecular mass of the polysaccharide, at least within the range of 67 to 150 kDa. The results showed that the glycosylation of β-conglycinin increased its ability to suppress the thermal aggregation of glycinin relative to non-glycosylated β-conglycinin. Thus, the glycosylation of soy protein can be expected to be a practical method used to regulate the thermal aggregation of protein.