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Rational Design of Amyloid‐Like Fibrillary Structures for Tailoring Food Protein Techno‐Functionality and Their Potential Health Implications

淀粉样纤维 纤维 背景(考古学) 化学 食物蛋白 淀粉样蛋白(真菌学) 人类健康 生物物理学 纳米技术 蛋白质聚集 生物化学 淀粉样β 生物 材料科学 医学 疾病 病理 环境卫生 古生物学 无机化学
作者
Koen J.A. Jansens,Ine Rombouts,Charlotte Grootaert,Kristof Brijs,John Van Camp,Paul Van der Meeren,Frédéric Rousseau,Joost Schymkowitz,Jan A. Delcour
出处
期刊:Comprehensive Reviews in Food Science and Food Safety [Wiley]
卷期号:18 (1): 84-105 被引量:162
标识
DOI:10.1111/1541-4337.12404
摘要

Abstract To control and enhance protein functionality is a major challenge for food scientists. In this context, research on food protein fibril formation, especially amyloid fibril formation, holds much promise. We here first provide a concise overview of conditions, which affect amyloid formation in food proteins. Particular attention is directed towards amyloid core regions because these sequences promote ordered aggregation. Better understanding of this process will be key to tailor the fibril formation process. Especially seeding , that is, adding preformed protein fibrils to protein solutions to accelerate fibril formation holds promise to tailor aggregation and fibril techno‐functionality. Some studies have already indicated that food protein fibrillation indeed improves their techno‐functionality. However, much more research is necessary to establish whether protein fibrils are useful in complex food systems and whether and to what extent they resist food processing unit operations. In this review the effect of amyloid formation on gelation, interfacial properties, foaming, and emulsification is discussed. Despite their prevalent role as functional structures, amyloids also receive a lot of attention due to their association with protein deposition diseases, prompting us to thoroughly investigate the potential health impact of amyloid‐like aggregates in food. A literature review on the effect of the different stages of the human digestive process on amyloid toxicity leads us to conclude that food‐derived amyloid fibrils (even those with potential pathogenic properties) very likely have minimal impact on human health. Nevertheless, prior to wide‐spread application of the technology, it is highly advisable to further verify the lack of toxicity of food‐derived amyloid fibrils.
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