Soy Protein Isolate/Sodium Alginate Microparticles under Different pH Conditions: Formation Mechanism and Physicochemical Properties

The effects of sodium alginate (SA) and pH value on the formation, structural properties, microscopic morphology, and physicochemical properties of soybean protein isolate (SPI)/SA microparticles were investigated. The results of ζ-potential and free sulfhydryl (SH) content showed electrostatic interactions between SPI and SA, which promoted the conversion of free SH into disulfide bonds within the protein. The surface hydrophobicity, fluorescence spectra, and Fourier transform infrared spectroscopy data suggested that the secondary structure and microenvironment of the internal hydrophobic groups of the protein in the SPI/SA microparticles were changed. Compared with SPI microparticles, the surface of SPI/SA microparticles was smoother, the degree of collapse was reduced, and the thermal stability was improved. In addition, under the condition of pH 9.0, the average particle size of SPI/SA microparticles was only 15.92 ± 0.66 μm, and the distribution was uniform. Rheological tests indicated that SA significantly increased the apparent viscosity of SPI/SA microparticles at pH 9.0. The maximum protein solubility (67.32%), foaming ability (91.53 ± 1.12%), and emulsion activity (200.29 ± 3.38 m(2)/g) of SPI/SA microparticles occurred at pH 9.0. The application of SPI/SA microparticles as ingredients in high-protein foods is expected to be of great significance in the food industry.