Advanced processes for engineering food protein amyloid fibrils: Molecular mechanisms, processing parameters, and structure-function relationships

Abstract

Amyloid fibrils derived from food proteins (PAFs) represent highly ordered supramolecular assemblies with distinctive beta-sheet-rich architectures, exceptional mechanical robustness, and remarkable environmental stability. These nano-structured materials have emerged as promising bio-derived platforms for engineering sustainable, functional, and structurally tunable food systems, as well as advanced biomaterials. Conventional thermal acid-induced fibrillization, while effective, is constrained by long processing times, high energy demands, and limited structural control. Recent breakthroughs in processing technologies, i.e., high-pressure treatment, ultrasonication, cold plasma, moderate electric fields, ohmic and microwave heating, ultraviolet irradiation, radio frequency heating, pH modulation, and enzymatic hydrolysis, offer unprecedented precision in modulating fibrillation kinetics, morphology, and functional performance. This review systematically investigates the molecular mechanisms, processing parameters, and structure-function interrelationships underpinning these emerging methodologies. By integrating advancements in process engineering, protein chemistry, and materials science, we highlight innovative routes to optimize PAF production, enabling the creation of advanced nanostructures with transformative potential for food, biomedical, and cross-industry applications.