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Updated: Sep 17, 2026
Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens
Published on: February 24, 2021
Extraction-dependent changes in immunoglobulin E binding profiles of processed lesser mealworm (Alphitobius
Michelle M Epstein1, Isabel Mafra2, Carla Ss Teixeira2
1Laboratory of Experimental Allergy, Department of Dermatology, Medical University of Vienna, Vienna, Austria.
Background:
Alphitobius diaperinus, the lesser mealworm, is an edible insect considered safe for human consumption; however, its proteins show documented cross-reactivity with crustacean and house dust mite (HDM) allergens, raising potential concerns for allergic populations. In this study, different lesser mealworm materials were extracted using three protein extraction protocols to evaluate how methodological choices and food processing treatments influence immunoglobulin E (IgE)-binding profiles.
Results:
All protocols yielded satisfactory protein recovery, with protocols 1 and 2 enabling the extraction of distinct protein fractions (TRIS-, UREA-, and SDS/DTT-soluble) and protocol 3 providing a faster and simpler workflow. A range of food-processing treatments, spanning industrial and household methods, was applied to lesser mealworm materials, and the resulting extracts were assessed for immunoglobulin G (IgG)- and IgE-binding using sera from crustacean- and HDM-allergic individuals. Processing induced marked changes in IgE-binding patterns, with several treatments, including boiling, baking, microwaving, autoclaving, canning, frying, and grilling, showing an increased number and/or intensity of detectable IgE-reactive bands under the applied in vitro conditions. Putative IgE-reactive protein candidates, inferred from apparent molecular weight and the literature, included proteins consistent with tropomyosin, arginine kinase/serpin, hexamerin/glycogen phosphorylase-like protein/filamin C, and apolipophorin.
Conclusions:
In vitro IgE-binding does not equate directly to clinical reactivity, but these findings indicate that food processing can modulate IgE-binding profiles of lesser mealworm proteins substantially and underscore the relevance of cross-reactive IgE-responses in crustacean- and HDM-allergic populations. © 2026 The Author(s). Journal of the Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.
