Enzymatic treatment of Tenebrio molitor proteins by papain reduces IgE reactivity and produces sACE-inhibitory hydrolysates.

Edible insects are being investigated as sustainable alternative protein sources; however, their use as food ingredients raises allergenicity concerns due to immunoglobulin (IgE) cross-reactivity with crustacean allergens. This study evaluated a papain-based enzymatic hydrolysis approach to obtain yellow mealworm (Tenebrio molitor) flour hydrolysates with reduced IgE reactivity and somatic angiotensin-converting enzyme (sACE) inhibitory potential. Hydrolysis markedly reduced or eliminated IgE-binding capacity in sera from crustacean-allergic individuals, indicating a substantial decrease in allergenic potential. In parallel, the resulting hydrolysates exhibited ACE inhibitory activity, suggesting potential antihypertensive effects. Epitope disruption and the formation of peptides with predicted sACE-inhibitory activity were further suggested by in silico papain hydrolysis. These findings demonstrate that papain-mediated hydrolysis can simultaneously reduce allergenicity and enhance the bioactive potential of T. molitor proteins, supporting their development as safer and functional food ingredients.