The impact of processing on food allergens: a molecular dynamics perspective and research outlook

Food allergies are a significant global public health concern, affecting an estimated 3–8% of the population in Western nations. Although the structural and immunological basis of food allergens is increasingly well understood, the mechanisms by which processing modifies their allergenicity remain largely unresolved. This narrative review synthesizes current evidence on the effects of thermal and nonthermal processing treatments, such as high hydrostatic pressure, enzymatic hydrolysis, digestion, and chemical modification, on the structure and immunoglobulin E (IgE)-binding ability of food allergens. Fish allergens, primarily parvalbumin, were used as the primary case study throughout, given their high thermal stability, cross-reactivity, and the availability of molecular dynamics (MD) data. The review also examines how MD simulations have contributed to understanding these processing effects at the atomic scale, including conformational changes, epitope exposure, and digestibility under thermal stress. The synthesized evidence shows that, while processing can reduce allergenicity by disturbing epitopes or improving digestibility, it can also have the opposite effect by unmasking hidden epitopes or generating new ones, depending on the protein identity, processing conditions, and food matrix. A major gap identified is the limited application of long-term MD simulations under relevant stress conditions, which affects the interpretative value of existing studies. Combining MD simulation results with experimental validation offers a promising path for developing processing strategies for safer food products.