Using high-pressure homogenization as a potential method to pretreat soybean protein isolate: Effect on conformation changes and rheological properties of its acid-induced gel

This study evaluated the conformational changes and rheological properties of acid-induced gels of insoluble soybean protein isolate (SPI) pretreated with high-pressure homogenization (HPH) under different pressure and cycles. Results showed that HPH pretreatment destroyed the spatial structure of the insoluble SPI, significantly decreased the particle size of the SPI dispersion, and increased the SH content. Through the characterization of its acid-induced gelation product, the best ability to withstand small strains (< 3%) of gel was found in a single HPH cycle under 100 MPa. The SPI gels with a relatively compact structure transformed from strain stiffening to strain softening with the strain increased, and it provided satisfactory stability to withstand large-amplitude oscillatory shear in three-time HPH cycles under 100 MPa. Meanwhile, SPI gels exhibited a more chaos spatial topology network after HPH pretreatment through fractal analysis, and the gels eventually exhibited “soft gel” and shear-thinning behavior with HPH pretreatment. This provides an evidence for the beneficial effect of HPH on the structural homogenization and subsequent gel formation stability of protein gels, and explores its potential applications in the food industry. •High-Pressure Homogenization can replace heating pretreatment on insoluble protein.•High-Pressure Homogenization (HPH) increased the complexity of irregular gel network.•Proper HPH promotes the viscoelastic property of gels in linear viscoelastic region.•Stable and hard structure gels were formed under large amplitude oscillation.•HPH treated protein exhibited “soft gel” and shear-thinning behavior.