Abstract: Glycosylated soybean protein isolate (SPI) was prepared by reaction between SPI and glucose at a ratio of 1:1 (m/m) at 70 ℃ for 4 h, and its blends with myofibrillar protein (MP) at different ratios of 9:1, 8:2, 7:3, 6:4 and 5:5 (m/m) were determined for emulsifying properties, turbidity, surface hydrophobicity and gel properties (texture properties, whiteness and microstructure) in order to elucidate the effect and mechanism of glycosylated SPI on the functional properties of MP. The results showed that the emulsifying properties and surface hydrophobicity of glycosylated SPI and MP blends were significantly improved compared with MP (P < 0.05). The turbidity of the blended proteins rose with increasing temperature (30?80 ℃), but it decreased with higher proportion of glycosylated SPI. The gel hardness and springiness of MP and glycosylated SPI blends were significantly better than those of MP and native SPI blends (P < 0.05), and the gel microstructure was more compact and uniform than that of MP and native SPI blends. Compared with MP, the gel whiteness of the mixed proteins significantly decreased, except for no significant difference at a mixing ratio of 9:1 (P > 0.05).

Key words: soybean protein isolate, glycosylation, myofibrillar protein, emulsifying properties, gel properties