Transglutaminase-induced soybean protein isolate cold-set gels treated with combination of ultrasound and high pressure: Physicochemical properties and structural characterization

Soybean protein isolate (SPI) was treated by the combined exposure to ultrasound and high pressure and then subjected to transglutaminase (TGase)-catalyzed cross-linking to prepare SPI cold-set gels. The effects of combined treatments on physicochemical and structural properties of TGase-induced SPI cold-set gels were investigated. The combination of ultrasound and high pressure promoted the covalent disulfide bonds and ε-(γ-glutaminyl) lysine isopeptide bonds as well as non-covalent hydrophobic interactions, which further improved the gelation properties of SPI compared to ultrasound or high pressure alone. In particular, the 480 W ultrasound followed by high pressure treatment of gels led to higher strength (120.53 g), water holding capacity (95.39 %), immobilized water (93.92 %), lightness (42.18), whiteness (51.03), and elasticity (G′ = 407 Pa), as well as more uniform and compact microstructure, thus resulting in the improved gel network structure. The combination of two treatments produced more flexible secondary structure, tighter tertiary conformation and higher denaturation degree of protein in the gels, leading to more stable gel structure. The structural modifications of SPI contributed to the improvement of its gelation properties. Therefore, the combined application of ultrasound and high pressure can be an effective method for improving the structure and properties of TGase-induced SPI cold-set gels.