Molecular structure and functional properties of glycinin conjugated to κ-carrageenan and guar gum: A comparative study.

Molecular structure and functional properties of glycinin conjugated to κ-carrageenan and guar gum using a dry-heating method were comparatively analyzed. Glycosylation was confirmed by analyzing the degree of grafting, protein subunit composition, infrared absorption profile, and changes in contents of protein secondary structures. K-carrageenan was proven to possess a greater susceptibility to be grafted to glycinin than guar gum due to its relatively low molecular weight and negatively charged characteristics. The improvement of solubility by glycosylation with guar gum near the isoelectric point of glycinin was better than that by glycosylation with κ-carrageenan. Glycinin glycosylated with both polysaccharides exhibited enhanced emulsifying activity and stability. The enhanced apparent viscosity, elastic modulus, and viscous modulus also demonstrated that glycosylation promoted the appearance of stable elastic network structure. In summary, glycosylation with these two polysaccharides conferred glycinin superior emulsifying and rheological properties, and κ-carrageenan exhibited a better performance compared to guar gum.

Rheological and textural properties of acid-induced soybean protein isolate gel in the presence of soybean protein isolate hydrolysates or their glycosylated products.

Enzymatic hydrolysis and glycosylation were successively applied to modify soybean protein isolate (SPI) and rheological and textural properties of acid-induced SPI gel added with the obtained SPI hydrolysates and their glycosylated products were then investigated. The incorporation of SPI hydrolysates decreased the elastic modulus (G') and hardness of SPI gel, which might be related to the random aggregation between SPI hydrolysates and native SPI molecules via hydrophobic interactions. In addition, as the molecular weight of SPI hydrolysates decreased, the reduction in G' and hardness became more significant. Although glycosylation of SPI hydrolysates weakened the adverse effects of hydrolysates on the SPI gel formation to some extent, the glycosylated SPI hydrolysates were still unable to improve the gel quality compared with the control. However, results of this research may provide important information for understanding the influencing mechanism of SPI hydrolysates and their glycosylated products on the formation of SPI gel.