Amyloid fibrillation of food-derived dietary proteins has been increasingly accepted as an
effective approach to enhance protein functionality. Soy protein, an abundant and …

Food protein-derived amyloid fibrils possess great untapped potential applications in food
and other biomaterials. The objective of this report was to investigate the formation …

Amyloid-like fibrils from food proteins possess unique functional properties for food and
many other uses. This study reports the effect of hydrolytic heating (pH 2.0, 85° C, 0–24 h) …

The impact of protein types, heating temperatures, and times on protein fibrillation has been
widely studied. However, there is little understanding of the influence of protein …

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 (AFs) are highly ordered nanofibers composed of proteins rich in β-sheet
structures. In this study, the impact of heating conditions relevant in food processing on AF …

Legume seed storage proteins can be induced to form amyloid fibrils upon heating at low
pH, which could improve their functionality for use in food and materials. However, the …

Conditions including heating mode, time, temperature, pH, moisture and protein
concentration, shear, and the presence of alcohols, chaotropic/reducing agents, enzymes …

Formation of amyloid fibrils (ie., protein structures containing a compact core of ordered β-
sheet structures) from food proteins can improve their techno-functional properties. Wheat …

Amyloid fibrils (AFs) are highly ordered protein nanofibers composed of cross β-structure
that occur in nature, but that also accumulate in age-related diseases. Amyloid propensity is …