Rising health concerns and increasing obesity levels in human society have led some consumers to cut back on animal protein consumption and switch to plant-based proteins as an alternative. Soy protein is a versatile protein supplement and contains well-balanced amino acids, making it comparable to animal protein. With sufficient processing and modification, the quality of soy protein can be improved above that of animal-derived proteins, if desired. The modern food industry is undergoing a dynamic change, with advanced processing technologies that can produce a multitude of foods and ingredients with functional properties from soy proteins, providing consumers with a wide variety of foods. This review highlights recent progress in soy protein processing technologies. Using the current literature, the processing-induced structural changes in soy protein are also explored. Furthermore, the molecular structure of soy protein, particularly the crystal structures of β-conglycinin and glycinin, is comprehensively revisited.

The effect of ultrasound on the conformational and physicochemical properties of soy protein isolate hydrolysates (SPHs) was investigated. SPHs were prepared at hydrolysis times of 20 min, 60 min, and 180 min, then treated with ultrasound for 10 min, 20 min, and 30 min at a frequency of 20 kHz and output powers of 150 W and 450 W. The structural properties and antioxidant capacities of the aqueous layer of SPHs (ASPHs) after sonication were evaluated by Fourier-transform infrared spectroscopy (FTIR), intrinsic fluorescence, DPPH radical scavenging activity assays, and microscopy observations. Results obtained showed that ultrasound treatment significantly disrupted the peptide aggregates formed during protein hydrolysis. The protein solubility was significantly increased after sonication (by up to 18.33%), as did the percentage of proteins with MW < 1 kDa in ASPHs. The antioxidant capacity of ASPHs also increased, as measured by DPPH assay. FTIR analysis of ASPHs indicated that the protein secondary structures were different, with an increase in β-sheet and a decrease in α-helix and β-turn. Furthermore, the changes in fluorescence spectra of ASPHs showed the transition of protein tertiary structure with a greater exposure of Trp residues in the side chains. Scanning electron microscope (SEM) and atomic force microscope (AFM) observations of the morphological structure of ASPHs further confirmed the significant effect of sonication on disrupting peptide aggregates. In conclusion, ultrasound can be used as an efficient treatment to promote the solubility of protein hydrolysates.