Amyloid fibrils have traditionally been considered only as pathological aggregates in human neurodegenerative diseases, but it is increasingly becoming clear that the propensity to form amyloid fibrils is a generic property for all proteins, including food proteins. Differently from the pathological amyloid fibrils, those derived from food proteins can be used as advanced materials in biomedicine, tissue engineering, environmental science, nanotechnology, material science as well as in food science, owing to a combination of highly desirable feature such as extreme aspect ratios, outstanding stiffness and a broad availability of functional groups on their surfaces. In food science, protein fibrillization is progressively recognized as an appealing strategy to broaden and improve food protein functionality. This review article discusses the various classes of reported food protein amyloid fibrils and their formation conditions. It furthermore considers amyloid fibrils in a broad context, from their structural characterization to their forming mechanisms and ensued physical properties, emphasizing their applications in food-related fields. Finally, the biological fate and the potential toxicity mechanisms of food amyloid fibrils are discussed, and an experimental protocol for their health safety validation is proposed in the concluding part of the review.

淀粉样蛋白原纤维传统上仅被认为是人类神经退行性疾病中的病理性聚集体，但是越来越清楚的是，形成淀粉样蛋白原纤维的倾向是所有蛋白质（包括食物蛋白）的通用特性。与病理性淀粉样蛋白原纤维不同，由于极高的特性（例如极端方面）的结合，衍生自食物蛋白的那些原纤维可以用作生物医学，组织工程，环境科学，纳米技术，材料科学以及食品科学中的高级材料。比率，出色的刚度和表面上官能团的广泛可用性。在食品科学中，蛋白质原纤维化逐渐被认为是扩大和改善食品蛋白质功能的诱人策略。这篇综述文章讨论了各种报道的食物蛋白淀粉样蛋白原纤维及其形成条件。此外，从结构特征到它们的形成机理以及随后的物理性质，广泛地考虑淀粉样蛋白原纤维，强调了它们在食品相关领域中的应用。最后，讨论了食物淀粉样蛋白原纤维的生物学命运和潜在的毒性机理，并在本综述的最后部分提出了用于验证其健康安全性的实验方案。