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Allergenicity assessment of the edible cricket Acheta domesticus in terms of thermal and gastrointestinal processing and IgE cross-reactivity with shrimp.
- Source :
-
Food Chemistry . Oct2021, Vol. 359, pN.PAG-N.PAG. 1p. - Publication Year :
- 2021
-
Abstract
- • 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. 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 03088146
- Volume :
- 359
- Database :
- Academic Search Index
- Journal :
- Food Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 150695718
- Full Text :
- https://doi.org/10.1016/j.foodchem.2021.129878