Fibrillar Protein Structures in Food Systems

Fibrillar protein structures arise when globular or partly unfolded proteins self-assemble into elongated, thread-like aggregates often enriched in cross-β-sheet motifs. In food systems such assemblies can emerge from animal-derived sources such as whey or egg proteins, as well as from plant proteins including legumes, seeds and cereals. Controlled fibrillation is induced by adjusting pH, temperature, ionic strength or by enzymatic hydrolysis, and yields materials with distinct rheological, textural and functional properties. These fibrils can enhance gel strength, stabilise foams and emulsions, confer barrier properties in edible films, and serve as scaffolds for nutrient delivery or biobased materials. Safety and digestibility profiles show that many food fibrils are broken down in the gastrointestinal tract without adverse effects, supporting their utilisation as novel nutritional ingredients. The diversity of protein sources and assembly conditions offers a rich toolkit for tailoring fibril morphology, flexibility and network formation, underpinning applications in sustainable packaging, smart materials and next-generation food formulations.

Research from Nature Portfolio

Recent studies have shown that amyloid-type food fibrils prepared from β-lactoglobulin and lysozyme retain comparable or enhanced digestibility relative to their native monomers, with no detectable cytotoxicity in cell cultures or adverse effects in nematode and rodent models. This work highlights the safety profile of digested fibrils and supports their incorporation as functional ingredients in human nutrition. Foundational investigations into plant protein fibrillation in the presence of magnetic nanoparticles have revealed that nanoparticle–protein interactions at low pH accelerate β-sheet assembly, yielding hybrid nanocomposites with tunable magnetic properties and structural stability under varied pH conditions. Such composites illustrate the potential to direct fibril organisation for responsive food-material applications.

Fibrillar Protein Structures in Food Systems publication trend

The graph below shows the total number of articles in fibrillar protein structures in food systems across all publications each year (not limited to Nature Index journals).

Technical terms

Amyloid fibril: Highly ordered protein aggregate characterised by stacked β-sheet structures running perpendicular to the fibril axis.

Nanofibril: Fibrillar assembly with nanoscale diameter (typically 5–20 nm) and variable length, formed by protein self-association.

β-sheet: A common protein secondary structure in which strands lie side by side, stabilised by hydrogen bonds, and forming the core of many fibrils.

Electrostatic self-assembly: Directed organisation of charged fibril segments at interfaces or in solution, driven by attractive and repulsive forces between charged groups.

References

1. Food amyloid fibrils are safe nutrition ingredients based on in-vitro and in-vivo assessment. Nature Communications (2023).
2. Interfacial Electrostatic Self‐Assembly of Amyloid Fibrils into Multifunctional Protein Films. Advanced Science (2023).
3. Self-assembly of plant protein fibrils interacting with superparamagnetic iron oxide nanoparticles. Scientific Reports (2019).
4. Plant Protein Amyloid Fibrils for Multifunctional Sustainable Materials. Advanced Sustainable Systems (2023).
5. Formation and characterization of plant-based amyloid fibrils from hemp seed protein. Food Hydrocolloids (2023).