Abstract
The effects of high hydrostatic pressure (HHP) combined with pH-shifting treatment, on the structural and emulsifying properties of soy protein isolate (SPI) were investigated. SPI was subject to different pH solutions (pH 7, pH 3, and pH 11) with pressure levels ranging from 0.1 MPa to 400 MPa before being neutralized to pH 7. The combination of HHP and the pH-shifting process increased the protein solubility and the surface charge of the protein molecule, and induced the formation of smaller re-aggregated protein particles. Structural changes were characterized by free sulfhydryl groups, surface hydrophobicity, ultraviolet–visible spectroscopy, and circular dichroism spectra. Emulsions fabricated with SPI treated by the combined treatment were characterized by mean droplet size, zeta potential, emulsifying activity, emulsifying stability, and fluorescence microstructure. The results suggested that the increasing pressure enhanced the effect of pH shifting, and the protein structure could be significantly unfolded by the synergistic effect of HHP and pH-shifting, further improving the emulsifying performance of SPI. • Structural changes of soy protein isolate were induced by high pressure and pH shifting. • Enhanced unfolding in pH shifted SPI were observed after pressurization. • High pressure aided pH shifting improved the emulsifying properties of SPI.
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