CHAPTER 3: Food Protein Allergenicity: Characterization, Epitope Mapping and Deactivation
Published:03 Jun 2021
F. C. Ekezie, I. Ahmed, C. C. Udenigwe, and Z. Li, in Food Proteins and Peptides: Emerging Biofunctions, Food and Biomaterial Applications, ed. C. C. Udenigwe, The Royal Society of Chemistry, 2021, pp. 58-96.
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Allergic reactions are developed in response to the consumption of certain foods. However, the entire allergen does not elicit the immune response – only a specific part of the protein called the epitope contributes to the onset of allergic reactions. Hence the accurate identification of epitopes on food allergens can provide a better understanding of the pathophysiology of food allergies. Conventionally, epitopes are categorized into linear/continuous and conformational/discontinuous epitopes but are often called T-cell and B-cell epitopes, respectively. With advances in biological and analytical methods, epitopes on food allergens can be identified and characterized. Examples of approaches used for B-cell epitope mapping include fabrication of peptides in various formats, X-ray crystal diffraction and nuclear magnetic resonance spectroscopy, among others. For identification of T-cell epitopes, methods such as flow cytometry, proliferation assay and enzyme-linked immunospot assays are utilized. In addition, different food processing methods have the potential to alter the allergenic properties of food proteins to such an extent that allergic reactions will no longer be elicited, simply by destroying/deactivating the epitope site. To advance further the development of hypoallergenic foods, more experimental and validation studies focused on the characterization of epitopes and the determination of optimum conditions vital to food allergy mitigation using food processing techniques are required.