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Amyloids of Food Proteins: Balancing Benefits and Risks
Vikash Poonia1, Jay Kant Yadav1
1Department of Biotechnology, Central University of Rajasthan, NH-8 Bandarsindri, Kishanagarh, Ajmer-305817, Rajasthan, India.
Current Protein & Peptide Science
|June 2, 2026
Summary
Food Protein-derived Amyloid Fibrils (FPAFs) offer functional food benefits but raise safety questions. Some FPAFs degrade during digestion, while others show cytotoxicity, requiring further safety evaluation.
Area of Science:
- Food Science and Technology
- Biochemistry
- Toxicology
Background:
- Food Protein-derived Amyloid Fibrils (FPAFs) are novel nanomaterials with desirable functional properties for food applications.
- Their potential use in plant-based and clean-label foods is increasing due to superior gelling, emulsifying, and water-binding capabilities.
- However, the safety of FPAFs is under scrutiny, necessitating a thorough risk assessment.
Purpose of the Study:
- To critically evaluate the dual nature of FPAFs, balancing their functional advantages against emerging safety concerns.
- To review the current understanding of FPAF digestion, stability, and potential health implications.
- To identify knowledge gaps and guide future research for safe FPAF utilization.
Main Methods:
- Review of in vitro gastrointestinal digestion models assessing FPAF degradation.
- Analysis of cytotoxicity data for FPAFs in human epithelial cells.
- Examination of theoretical concerns regarding transmissible amyloidosis from food sources.
Main Results:
- Fibrils from β-lactoglobulin and lysozyme are largely degraded during digestion into non-amyloidogenic peptides.
- Certain legume-derived amyloid fibrils resist digestion and exhibit cytotoxicity at high concentrations.
- Heat-stable amyloid A fibrils in animal products raise theoretical concerns, though most food-grade fibrils lack pathogenic structures.
Conclusions:
- FPAFs present a dichotomy of functional benefits and potential safety risks.
- Further research is essential to understand real food matrix effects, long-term exposure impacts, and relevant biomarkers.
- Strict regulation and comprehensive risk evaluation are crucial for the sustainable application of FPAFs in the food industry.
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Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
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Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
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