Recent advances of interfacial and rheological property based techno-functionality of food protein amyloid fibrils

Protein amyloid fibrils (PAF) are formed by assembly and aggregation of protein monomers or peptides. There is an increasing interest for PAF in food research, which owed to their ability to form unique structures with high aspect ratios, tunable flexibility, ordered alignment, and beneficial mechanical properties. Interfacial adsorption and rheological behavior of PAF are vitally important determinants of their techno-functionalities and applications. We reviewed the structural assemblies and characteristics of PAF, emphatically discussed the effect of interfacial adsorption and rheological behavior of PAF on their techno-functionalities, and finally summarized the potential utilization of PAF for encapsulation and delivery of bioactives and nutrients within recent years. The interfacial property composed of thickness, viscoelasticity, alignment and rheological property including viscosity, storage/loss modulus, mechanical strength were highly dependent on PAF type, length, flexibility, surface hydrophobicity and structural arrangement from complexation and entanglement. These properties determined their techno-functionalities of foaming, emulsification, gelation, and filming, accordingly provided applications of PAF in encapsulation and delivery of bioactives and nutrients. Nevertheless, microbes derived PAF, the effect of PAF arrangements at droplets interface on the emulsion stability, and interactions between PAF and in vivo tissues for safety evaluation may serve as the promising directions for upcoming researches.