Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications

Design principles of food gels

“…Amyloid fibrils, the proteinaceous aggregates with a typical cross-β secondary structure, have a diameter of several nanometres, contour lengths up to a few micrometres and an extremely high Young's modulus ( Fig. 1e) 50,51 . Strands and amyloid fibrils are often used as precursors to prepare cold-set gels, which show many superior properties compared with conventional heat-set gels, such as higher gel strength and fracture properties, improved water-retention capacity and transparency, and lower critical gelation concentration 52 .…”

“…In addition, the cold-set gelation route is of paramount importance when using food gels to encapsulate temperature-sensitive bioactives. Note that both protein fibrillization 51 and cluster formation 46 are generic features of almost all food proteins. In other words, different food proteins can provide network-building blocks with universal features.…”

Accumulation of storage proteins in plant seeds is mediated by amyloid formation

“…However, several plant proteins or their regions were shown to form fibrils with several properties of amyloids in vitro (after the proteolytic digestion or other treatments 14,15 ) suggesting that plants might form bona fide amyloids in vivo 16 .…”

Modulating the Mechanical Performance of Macroscale Fibers through Shear‐Induced Alignment and Assembly of Protein Nanofibrils

“…While the formation of amyloid fibrils has mainly been studied in the context of its connection with neurodegenerative diseases, amyloid fibril assembly often occurs to yield physiologically benign and highly functional materials in nature, for example, as biofilms produced by bacteria, catalytic scaffolds, and hormone storage units in humans . As such structures can be engineered in vitro from a wide range of protein sources, amyloid‐like nanofibrils are receiving increased attention as a potential materials system for the fabrication of functional materials from a variety of peptide and protein building blocks . A well characterized amyloid forming protein systems is the food protein β‐lactoglobulin, which forms semiflexible nanofibrils with the lengths in the micrometer range under acidic conditions .…”

“…[20] As such structures can be engineered in vitro from a wide range of protein sources, amyloid-like nanofibrils are receiving increased attention as a potential materials system for the fabrication of functional materials from a variety of peptide and protein building blocks. [21] A well characterized amyloid forming protein systems is the food protein β-lactoglobulin, which forms semiflexible nanofibrils with the lengths in the Protein-based fibers are used by nature as high-performance materials in a wide range of applications, including providing structural support, creating thermal insulation, and generating underwater adhesives. Such fibers are commonly generated through a hierarchical self-assembly process, where the molecular building blocks are geometrically confined and aligned along the fiber axis to provide a high level of structural robustness.…”