Allergenicity of edible insect proteins: Cross-reactivity, processing effects, and food safety considerations

초록

Edible insect proteins are emerging as sustainable alternative protein sources; however, their use in food systems is limited by allergenicity concerns. This review synthesizes current knowledge on edible insect protein allergenicity, focusing on molecular cross-reactivity, species-specific candidate insect allergens, processing effects, analytical detection, and insect-specific risk management. Conserved arthropod pan-allergens, particularly tropomyosin and arginine kinase, share structural features and IgE-binding epitopes with crustacean and mite allergens, supporting clinically relevant cross-reactivity. Species-specific allergens may also contribute to sensitization and variable allergic responses. Processing methods, including thermal treatment, enzymatic hydrolysis, fermentation, drying, defatting, protein extraction, and food matrix interactions, may alter IgE reactivity by altering epitope accessibility, solubility, digestibility, and allergen release. Immunoassays, LC-MS/MSbased proteomics, and clinical evaluations support allergen identification and risk assessment, although standardized product-specific approaches remain limited. This review highlights the need for species-specific allergen characterization, final-product assessment, and insect-specific labeling to support safe food use.

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