Improved qualities of cod-rice dual-protein gel as affected by rice protein: Insight into molecular flexibility, protein interaction and gel properties

[Display omitted] •The addition of rice protein improved the gel properties of dual-protein gel.•The decreased particle size facilitating the formation of a dense network structure.•Glutelin is more likely to bind with MHC, compared to actin and MLC.•Hydrogen bonding and hydrophobic interactions play the main role in the gel. Blending plant-based proteins with animal-based proteins to achieve adequate dietary protein intake is a strategy to address dietary deficiencies in the elderly. This research systematically investigated the effect of the ratio of cod protein/rice protein (21:0, 21:1.5, 21:3, 21:4.5, 21:6, 21:7.5, and 21:9) on the gelation properties of dual-protein gels and the underlying dual-protein interaction mechanisms. The results indicated that the myosin heavy chain (MHC) of cod and the glutelin in rice protein are primarily linked by hydrogen bonds, particularly involving Tyr residues, as evidenced by molecular docking and fluorescence quenching results. The addition of rice protein in cod protein promoted α-helix transforming into β-sheet, β-turn and random coil of the original protein solution, which was significantly correlated with molecule flexibility increasing. The decrease in the dual-protein particle size, and rice protein uniformly distributed in a cod protein-based gel network, which promoted the compactness and density of the gel structure. It was found that the hardness and springiness of 21:6 cod-rice protein gel increased by 73.96% and 17.28% compared to single cod gel, respectively. This study provides theoretical basis to the mechanism of dual-protein interaction affecting gel properties from the molecular level.