ABSTRACT Protein fibrillation has emerged as a promising strategy to enhance structural and functional properties of various protein‐based matrices, owing to the unique thin, elongated, β‐sheet‐rich structures of fibrils that impart superior texture, stability, and encapsulation functionalities. This review critically examines the formation of protein fibrils, highlighting the kinetic mechanisms, effects of protein sources, and their influence on fibril morphology and functionality. Special emphasis is placed on fibril synthesis from by‐product protein streams, which aligns with circular economy principles by reducing waste and production costs while extending fibril applications to both food and non‐food domains, including packaging and bioplastics. Challenges associated with fibril instability at food‐relevant pH conditions are discussed in detail, alongside emerging stabilization strategies such as complexation with polysaccharides, polyphenols, and physical treatments such as dialysis. This review presents protein fibrils as highly tunable and scalable sustainable biomaterials with considerable potential to advance both food and polymer industries.
Sawant et al. (Mon,) studied this question.
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