Amyloid fibrils from plant-based food protein sources bear a large unexploited potential for
applications in food and other biomaterials due to their techno-functional features. However …

Plant proteins self-assembly into amyloid fibrils is a promising modification to be introduced
in emerging food and materials applications. Although the valorization of protein-rich side …

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 …

The assembly behavior of three selected legume proteins was monitored using thioflavin T
(ThT) fluorescence intensity, atomic force microscopy (AFM) and dynamic light scattering …

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) …

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 …

The amyloid fibrils formed by heating 1.0%(w/v) kidney bean phaseolin (7S globulin)
solution at pH 2.0 with an ionic strength of 20 mM at 85° C were characterized using …

Artificial functional materials based on amyloid fibrils are proven to be a promising strategy
toward functional materials. However, scaling‐up applications present sustainability …

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-based nanostructures from food sources have been received intensive interests
recently in material science, biomedicine and especially delivery system. This is due to the …