Food-derived protein amyloid-like fibrils: Fibrillation mechanism, structure, and recent advances for the stabilization of emulsions

Food-derived protein amyloid-like fibrils (PAFs) are fibrous structure formed from proteins under strong acidic and high thermal conditions for long durations to form fibrous structure. PAFs have the properties of a high aspect ratio, ordered arrangement and high surface activity; PAFs have exhibited excellent performance, especially in the formulation of emulsions. This communication described the self-assembly behavior and structural characteristics of PAFs. Food-derived PAF-stabilized emulsions were then emphasized, covering the influencing factors and the poteJntial applications of the PAF-based emulsion. Ultimately, their future outlook was presented. The superior emulsification properties of PAFs were mainly attributed to the high interfacial modulus and the high surface activity of the interface formed. The emulsification properties were influenced by the structure (mainly rod-like structure, high aspect ratio, anisotropy), concentration, purity of the PAFs, pH of the system, ionic strength, stress conditions (stirring, rotor-stator dispersion, ultrasonication and high-pressure homogenization) and complexation with polysaccharides or polyphenols. Furthermore, a more systematic and theoretical analysis was needed for the safety assessment involving amyloid-like fibrils, and the techno-functionality involving pure amyloid-like fibrils warrants more attention for food-related applications.