Extraction‐dependent changes in immunoglobulin E binding profiles of processed lesser mealworm ( Alphitobius diaperinus ) proteins

Abstract 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.

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Journal
Journal of the Science of Food and Agriculture
Published
2026-09-15
DOI
https://doi.org/10.1002/jsfa.71060
Primary Topic
Insect Utilization and Effects
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article
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article

Extraction‐dependent changes in immunoglobulin E binding profiles of processed lesser mealworm ( Alphitobius diaperinus ) proteins

Joana Costa, Caterina Villa, Oskar Hoffmann, Isabel Mafra et al.
Journal of the Science of Food and Agriculture
Insect Utilization and Effects
article

Extraction‐dependent changes in immunoglobulin E binding profiles of processed lesser mealworm ( Alphitobius diaperinus ) proteins

Joana Costa, Caterina Villa, Oskar Hoffmann, Isabel Mafra, Carla S. Silva Teixeira, M. Epstein, Sahar Kazemi, Bruno Carriço-Sá, Anna‐Laura Mettinger
article en

Abstract

Abstract 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.

Journal of the Science of Food and Agriculture
University of Vienna (AT), Universidade do Porto (PT), Rede de Química e Tecnologia (PT), Medical University of Vienna (AT)
Zero hunger
Openalex Percentile: Top 11%
Insect Utilization and Effects
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