Progress and innovations in food protein amyloid fibrils for fabricating cutting-edge soft materials

Abstract

Food protein-based amyloid fibrils (PAFs) represent a novel and sustainable class of functional nanomaterials with growing importance in the design of soft matter systems. Derived from abundant, renewable, and often byproduct protein sources, PAFs offer a sustainable/biodegradable alternative to synthetic nanomaterials, combining eco-friendly production with versatile functional applications. Through precise control of environmental factors such as pH, temperature, and ionic strength, diverse food proteins can be transformed into highly ordered fibrillar structures, exhibiting robust mechanical properties, remarkable surface activity, and structural anisotropy. These unique features have positioned PAFs as promising agents for stabilizing emulsions and foams, enhancing the textural properties of hydrogels, and serving as active components in food packaging and biomedical carriers. Their biocompatibility and the presence of modifiable surface groups enable effective encapsulation of bioactive compounds and responsive release under targeted conditions. As research advances, deeper understanding of their formation pathways, physicochemical behaviour, and interaction with other biopolymers will expand their utility across food science, material engineering, and therapeutic delivery systems. This review offers a comprehensive overview of recent insights and emerging strategies in the development and application of PAFs, emphasizing their role in shaping the future of environmentally conscious material innovation.