Protein amyloid-like fibrils derived from cereals: Formation, structural characteristics, and applications

As a major plant protein source that is widely available and low-cost, the application of cereal protein (CP) is often limited by inherent defects such as poor solubility and weak functional properties. Therefore, their functional modification is crucial to meet the demands of the sustainable food industry. Converting CP into protein amyloid-like fibrils (PALFs), possessing ordered structures and high aspect ratios, through self-assembly represents a promising strategy for functional enhancement. This review systematically elaborates on the mechanism of CP-PALF formation and summarizes the various nucleation hypotheses for CP in the early stages of PALF formation. Moreover, this review summarizes how precise control of environmental factors， including pH, enzymatic treatment, and external physical fields，can influence the morphology and size of CP-PALFs. The review emphasizes that the outstanding functional properties of PALFs，including excellent interface stability and active substance delivery capabilities，are directly influenced by their structure. These properties give PALFs broad application prospects in the food industry, where they can serve as efficient texture modifiers, delivery vehicles for functional ingredients, and even as the matrix for novel food packaging materials. Although CP-PALFs hold great potential in food systems, achieving large-scale, low-cost production and comprehensively evaluating their biosafety in complex food matrices remains a core challenge for the food industry.