Research Progress on the Regulation of Amyloid Fibril Formation in Cereal Proteins by Nonthermal Approaches

Amyloid fibrils (AFs) are highly ordered protein aggregates with excellent interfacial activity, foam stability, and gel-enhancing properties, making them promising candidates for food applications. Cereal proteins, due to their abundance, low cost, environmental benefits, and structural adaptability, represent ideal substrates for constructing plant-based AFs. This review highlights recent progress in using nonthermal approaches such as ultrasound and enzymatic hydrolysis to regulate the fibrillation of cereal proteins, focusing on nucleation, aggregation kinetics, structural evolution, and conformational transitions. Under optimized conditions, nonthermal treatments can accelerate fibril formation and stabilize morphology while improving interfacial and self-assembly properties, thereby broadening applications in emulsion stabilization, bioactive delivery, and sustainable food innovation, while future studies should emphasize multifactor mechanisms and industrial feasibility.