Food protein amyloid fibrils have superior technological, nutritional, sensorial, and physical
properties compared to native monomers, but there is as yet insufficient understanding of …

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 structural properties of amyloid fibrils combined with their highly functional surface
chemistry make them an attractive new food ingredient, for example as highly effective …

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 …

The deposition of proteins in the form of amyloid fibrils is closely associated with several
serious diseases. The events that trigger the conversion from soluble functional proteins into …

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 …

Both intrinsic and extrinsic factors impact amyloid formation of food proteins. We here review
the impact of various conditions and food constituents on amyloid fibrillation of milk and …

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

Protein aggregation is important in food processing, and this work investigated the
aggregation of food proteins as a source of amyloid fibrils for use in bionanotechnology …

Amyloids were first identified in association with amyloidoses, human diseases in which
proteins and peptides misfold into amyloid fibrils. Subsequent studies have identified an …