Effect of Ionic Strength on Freeze-Thaw Stability of Glycosylated Soy Protein Emulsion

This study used Soy Protein Isolate (SPI), Soy Protein Isolate Hydrolysates (SPH) and Dextran (D) as raw materials. Covalent compounds were prepared by grafting soy protein isolate and soy protein isolate hydrolysate with dextran by water-heating method, which were SPI-D and SPH-D, respectively. The effect of ionic strength (0-500 mM) on the freeze-thaw stability of SPI, SPI-D, and SPH-D emulsions was investigated. Fourier transform infrared analysis and Fluorescence emission spectroscopy analysis indicated that the structure of the protein changed. In this study, it was found that with the increase of ionic strength, the zeta potential of the three samples presented a downward trend and the surface hydrophobicity first decreased and then increased. The addition of ions effectively improved the freeze-thaw stability of the emulsions. The particle size of the emulsions changed little after freeze-thaw cycles, and coalescence degree, creaming index, and oiling off significantly decreased. Especially when the ionic strength reached 300 mM, the degree of coalescence was 248.46%, 170.92%, and 167.77%, respectively, and the oiling off was also reduced by 68.52%, 68.25%, and 59.92%, respectively. The creaming index of the SPI emulsion was 48.49% lower than the creaming index without ions. However, when the ionic strength exceeded 300 mM, the coalescence degree, creaming index, and oiling off of the emulsions increased. Optical microstructures also found that at ionic strength of 300 mM, the oil droplets produced by the three kinds of emulsion after freeze-thaw were smaller than those without ions.