Emulsion gels stabilized by freshwater fish-lotus seed dual-protein complexes: Rheological properties,...

Dual-protein emulsions are gaining attention for their functional and nutritional complementarity. This study investigated how ratios (k = 6:1, 2:1, 1:1, 1:2, 1:6) of fish collagen peptides (FP; from grass carp or silver carp) to lotus seed protein (LSP) influenced physicochemical and emulsifying properties of FP-LSP complexes. Results revealed that formation involved electrostatic interactions, hydrogen bonds, and hydrophobic interactions. As the k decreased to 1:6, the absolute ζ-potential values and surface hydrophobicity increased significantly. At Φ = 0.3, FP-LSP adsorbed at the droplet interface and formed a network structure, with droplet aggregation constructing a triple-network architecture that endowed the emulsion gels with excellent freeze-thaw stability. At Φ = 0.6, the FP-LSP-stabilized continuous phase enhanced gel viscoelasticity. LSP content and oil percentages significantly influenced the structural formation and stability. This study establishes theoretical framework of the formation of FP-LSP complexes, offering technical and theoretical insights for their applications in emulsion-based products.