Molecular Determinants of IgE-Mediated Food Allergenicity: Structural Dynamics, Processing-Induced Remodeling, and Analytical Interpretation

Immunoglobulin E (IgE)-mediated food allergenicity is not determined by protein identity alone. Processing, food matrix interactions, and gastrointestinal transit reshape allergen molecular states, while clinical consequences also depend on exposure. These transformations can alter the persistence, epitope accessibility, and digestive susceptibility of allergen-derived species. This narrative review examines how molecular architecture shapes these changes and their consequences for IgE binding, effector-cell activity, and analytical detectability. Examples from major allergen families show why structural stability and digestive persistence must be interpreted in context. Processing may reduce, preserve, or enhance immunoreactivity depending on the allergen, matrix, conditions, and endpoint measured. Persistence of intact proteins or IgE-binding fragments does not, by itself, establish functional activity or clinical elicitation. Analytical interpretation depends on the measurand: methods targeting different molecular features do not provide interchangeable estimates of intact allergen abundance or biological activity. Changes in analytical signals may reflect extraction efficiency, epitope accessibility, or target recovery rather than proportional changes in biologically relevant allergenic material. By connecting molecular transformation with analytical measurement, this review examines how validated analytical results can inform exposure assessment and comparison with reference doses in processed foods, alternative proteins, and complex formulations. Interpretive claims should therefore be aligned with the structural, immunological, analytical, or clinical evidence available.