Development of food protein amyloid fibrils co-formulated with polysaccharides, polyphenols, and proteins: A review

Abstract

The highly ordered supramolecular architecture, unique mechanical features, molecular alignment, and adjustable functional attributes of food protein amyloid fibrils (PAFs) enable their application as cutting-edge building blocks in food/biomedical systems. The concomitant application of PAFs with polysaccharides, polyphenols, or proteins has emerged as a versatile platform that exploits a combination of non-covalent forces (hydrogen bonding, hydrophobic interactions, and/or electrostatic attractions) and, in some cases, covalent linkages to create multifunctional constructions. Such associations/interactions are crucial for the development of hydrogels, edible films, emulsions, and bioactive delivery systems with improved mechanical properties, functional features, and encapsulation efficiency. Notwithstanding this promising progress, challenges remain in attaining structural uniformity, interfacial stability, and large-scale reproducibility in complex food systems. An in-depth exploration of the combination of PAFs with polysaccharides, polyphenols, and proteins highlights their potential for tailoring hierarchical structures with predictable properties in functional food systems and related applications.