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 epsilon-(gamma-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 TGaseinduced SPI cold-set gels.

Automated summary

Soybean protein isolate (SPI) was treated with ultrasound and high pressure, followed by transglutaminase-catalyzed cross-linking, to improve the properties of SPI cold-set gels. The combined treatment enhanced the gelation properties by promoting various bonds and interactions. The combination of ultrasound and high pressure resulted in gels with higher strength, water holding capacity, immobilized water, lightness, whiteness, and elasticity, as well as a more uniform and compact microstructure. This combined treatment also led to structural modifications of SPI, resulting in a more stable gel structure.