Co-precipitates proteins prepared by soy and wheat: Structural characterisation and functional properties.

Co-precipitation was a novel method for improving the functional properties of pure proteins. To investigate the mechanism of this effect, different protein proportions of soy-wheat co-precipitated protein were extracted by isoelectric point co-precipitation. Soy protein isolate (SPI) was mainly linked to wheat protein (WP) through non-covalent forces and disulfide bonds as determined by circular dichroism spectroscopy, disulfide bond, protein fraction extraction, interaction, and molecular modeling. Amino acid analysis indicated that co-precipitation could increase wheat lysine content. Furthermore, co-precipitation improved multiple functional properties of pure protein, and the emulsifying and foaming properties of the composite system with a mass ratio of 7:3 outperformed those of other systems. At the same time, correlation analysis revealed that protein structure and intermolecular forces significantly affected its functional properties. This study provided some useful and interesting information for the development and application of protein-protein systems with diverse functional properties.