Conditions including heating mode, time, temperature, pH, moisture and protein concentration, shear, and the presence of alcohols, chaotropic/reducing agents, enzymes, and/or salt influence amyloid fibril (AF) formation as they can affect the accessibility of amino acid sequences prone to aggregate. As some conditions applied on model protein resemble conditions in food processing unit operations, we here hypothesize that food processing can lead to formation of protein AFs with a compact cross β‐sheet structure. This paper reviews conditions and food constituents that affect amyloid fibrillation of egg and cereal proteins. While egg and cereal proteins often coexist in food products, their impact on each other's fibrillation remains unknown. Hen egg ovalbumin and lysozyme form AFs when subjected to moderate heating at acidic pH separately. AFs can also be formed at higher pH, especially in the presence of alcohols or chaotropic/reducing agents. Tryptic wheat gluten digests can form fibrillar structures at neutral pH and maize and rice proteins do so in aqueous ethanol or at acidic pH, respectively.

中文翻译：

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食品蛋白质淀粉样蛋白原纤维形成的条件-第一部分：鸡蛋和谷物蛋白质

加热模式，时间，温度，pH，水分和蛋白质浓度，剪切力以及酒精，离液/还原剂，酶和/或盐的存在等条件会影响淀粉样原纤维（AF）的形成，因为它们会影响氨基的可及性酸序列易于聚集。由于应用于模型蛋白质的某些条件类似于食品加工单元操作中的条件，因此我们在此假设食品加工可以导致形成具有紧凑的交叉β折叠结构的蛋白质AF。本文综述了影响鸡蛋和谷物蛋白淀粉样蛋白原纤化的条件和食品成分。尽管鸡蛋和谷类蛋白质通常共存于食品中，但它们对彼此原纤维形成的影响仍然未知。鸡蛋卵清蛋白和溶菌酶分别在酸性pH下适度加热时会形成AF。AF也可以在较高的pH下形成，尤其是在醇或离液/还原剂存在下。胰蛋白酶的小麦面筋消化物可以在中性pH下形成纤维状结构，而玉米和大米蛋白分别在乙醇水溶液或酸性pH下形成纤维状结构。