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

Food-grade material fibril is progressively recognized as an important fundamental area of
current research to improve the functionality of foods. This work investigated the fibrillation of …

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 …

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 …

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) …

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 fibrils (AFs) are generally believed to contribute to the functional properties of food
matrix. In order to improve the application accessibility of protein fibrils, a better …

The fibrillation of food proteins into amyloid fibrils, which possess unique structures, is
widely acknowledged as a reliable method to enhance protein functionality. Hofmeister ions …

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