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

Area of Science:

• Food Science
• Biochemistry
• Materials Science

Background:

• Dual-protein systems offer synergistic functional and nutritional benefits.
• Fish collagen peptides (FP) and lotus seed protein (LSP) are promising protein sources.
• Understanding protein-protein interactions is crucial for developing novel food ingredients.

Purpose of the Study:

• To investigate the influence of different fish collagen peptide (FP) to lotus seed protein (LSP) ratios on the physicochemical and emulsifying properties of FP-LSP complexes.
• To elucidate the interaction mechanisms governing the formation of FP-LSP complexes.
• To explore the structural characteristics and stability of emulsion gels formed by FP-LSP complexes.

Main Methods:

• Preparation of FP-LSP complexes at varying ratios (k = 6:1 to 1:6).
• Analysis of physicochemical properties including ζ-potential and surface hydrophobicity.
• Characterization of emulsion gel structure and stability at different concentrations (Φ = 0.3 and 0.6).

Main Results:

• FP-LSP complex formation is driven by electrostatic, hydrogen, and hydrophobic interactions.
• Higher LSP content (lower k ratio) increased absolute ζ-potential and surface hydrophobicity.
• Emulsion gels exhibited a triple-network structure at Φ = 0.3, leading to excellent freeze-thaw stability.
• At Φ = 0.6, the FP-LSP continuous phase enhanced gel viscoelasticity.
• LSP content and oil percentage significantly affected structural formation and stability.

Conclusions:

• The ratio of FP to LSP critically influences the formation and properties of their complexes.
• The study provides a theoretical framework for understanding FP-LSP complex formation.
• These findings offer valuable insights for the application of FP-LSP complexes in emulsion-based food products.