Beyond the Acid–Thermal Method: Efficient Preparation Strategies and Functional Research Progress of Amyloid Fibril

ABSTRACT Protein amyloid fibrils (AFs) have garnered significant attention in the food industry. However, the acid–thermal preparation method has obvious limitations, such as harsh reaction conditions and poor product homogeneity. Therefore, this review aimed to summarize recent research advances in the formation of AFs from various source proteins, with a focus on innovative strategies for optimizing preparation conditions. It also provided an in‐depth analysis of the regulatory mechanisms governing the formation of AFs, influenced by environmental factors such as pH, ionic types and strength, heat conditions, and interactions between substances. The kinetic characteristics and morphological evolution of the AFs assembly process were elucidated at the molecular level. The overview of aforementioned formation mechanism lays theoretical foundation for the precise regulation of the functional properties of AFs. Furthermore, thanks to their excellent functional properties, AFs are increasingly applied and play a crucial in fields such as materials science, biomedicine, and food innovation. Therefore, this review presented the latest research trends and application prospects of AFs in these fields. Finally, while comprehensively analyzing the technical advantages, this review also objectively pointed out challenges in recent investigations, including difficulties in large‐scale production and insufficient safety assessment, and put suggestions for development suggestions. This review provides valuable theoretical basis and technical reference for the efficient preparation of AFs from edible proteins through modification or environmental regulation strategies. It also holds its significant research value and broad application potential in the development of novel functional materials, personalized food products, and related fields.