Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications
Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications
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DOI：
10.1016/j.cis.2019.05.002
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发表时间：
2019-07-01
影响因子：
15.6
通讯作者：
Mezzenga, Raffaele
中科院分区：
文献类型：
--
作者：
Cao, Yiping;Mezzenga, Raffaele
淀粉样纤维传统上只被认为是人类神经退行性疾病的病理性聚集体，但越来越清楚的是，形成淀粉样纤维的倾向是所有蛋白质的通用属性，包括食物蛋白质。与病理性淀粉样蛋白纤维不同的是，从食物蛋白质中提取的淀粉样蛋白纤维具有极高的长径比、突出的硬度和表面可获得的官能团等特点，可作为先进材料用于生物医学、组织工程、环境科学、纳米技术、材料科学以及食品科学。在食品科学中，蛋白质纤维化逐渐被认为是拓宽和改善食物蛋白质功能的一种有吸引力的策略。本文综述了已报道的各类食物蛋白淀粉样纤维及其形成条件。此外，它还在广泛的背景下考虑淀粉样纤维，从它们的结构特征到它们的形成机制和随后的物理特性，强调它们在食品相关领域的应用。最后，讨论了食品淀粉样蛋白纤维的生物归宿和潜在的毒性机制，并提出了其健康安全性验证的实验方案。(C)2019爱思唯尔B.V.保留所有权利。
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. (C) 2019 Elsevier B.V. All rights reserved.