Allergenicity assessment of the edible cricket Acheta domesticus in terms of thermal and gastrointestinal processing and IgE cross-reactivity with shrimp. (15th October 2021)

• Record Type: Journal Article
• Authors: De Marchi, Laura; Mainente, Federica; Leonardi, Massimo; Scheurer, Stephan; Wangorsch, Andrea; Mahler, Vera; Pilolli, Rosa; Sorio, Daniela; Zoccatelli, Gianni
• Is Part Of: Food chemistry. Volume 359(2021)
• Publication Date: 2021-10-15
• Subjects: TM tropomyosin -- SCP sarcoplasmic calcium-binding protein -- MW molecular weight -- %T percentage of acrylamide; Edible insects -- Food allergy -- Tropomyosin -- Simulated gastrointestinal digestion -- Food processing -- Acheta domesticus -- Novel food; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2021.129878
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Shrimp sensitized patients' IgE recognized several cricket proteins. High IgE-cross-reactivity was found among shrimp and cricket tropomyosins. Cricket tropomyosin was more stable to digestion than the shrimp homologue. Baking enhances stability of IgE-binding proteins to gastric digestion. Stability of cricket tropomyosin represents a risk of primary sensitization. Abstract: The allergenic potency of the cricket Acheta domesticus, a promising edible insect, has never been assessed. This work aims to study the immunoreactivity of Acheta domesticus, and its cross-reactivity with the shrimp Litopenaeus vannamei, assessing the effect of cooking and gastrointestinal digestion on their allergenic properties. Different cricket proteins were detected by immunoblotting with shrimp-allergic patients' sera. Tropomyosin was identified as the most relevant IgE-binding protein, and its cross-reactivity with shrimp tropomyosin was demonstrated by ELISA. While shrimp tropomyosin showed scarce stability to gastric digestion, cricket tropomyosin withstood the whole digestion process. The sarcoplasmic calcium-binding protein, specifically detected in shrimp, showed exceptional stability to gastrointestinal digestion. IgE-binding proteins in a model of enriched baked products were partially protected from proteolysis. In conclusion, the ingestion of A. domesticus proteins poses serious concerns to the Crustacean-allergic population. The high stability of tropomyosin may represent a risk of primary sensitization and clinical cross-reactivity.