Influence of protein ratios on the structure and gel properties of soybean-wheat co-precipitated proteins

Co-precipitation is a method of combining proteins that can improve the defects of a single protein while also improving its functional properties. The effect of protein ratios on the structure and gelation of co-precipitated prepared with soy protein isolate (SPI) and wheat protein (WP) was investigated in this study. Structural analysis revealed that co-precipitation triggered sheet-helix transitions of SPI and WP, exposing hydrophilic groups and embedding hydrophobic moieties. The water dispersibility of the soybean-wheat co-precipitated protein (SWCP) was significantly improved (p < 0.05). Furthermore, when compared to the protein blend, the effect of co-precipitation was more significant. Small amplitude oscillatory shear tests revealed that the interaction between SPI and WP altered the gel formation temperature and increased gel elasticity. Co-precipitated protein resulted in denser and more homogenous gel networks with very strong inter-floc links, as well as increased water holding capacity and gel strength. According to the findings, co-precipitation may be a simple and practical method for modifying proteins to improve their functional properties.