University of Verona, Department of Biotechnology, Verona, Italy.
Paul-Ehrlich-Institut, Molecular Allergology, Langen, Germany.
Food Chem. 2021 Oct 15;359:129878. doi: 10.1016/j.foodchem.2021.129878. Epub 2021 Apr 20.
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.
蟋蟀 Acheta domesticus 的变应原性效力从未被评估过，它是一种很有前途的可食用昆虫。本研究旨在研究蟋蟀 Acheta domesticus 的免疫反应性及其与虾 Litopenaeus vannamei 的交叉反应性，评估烹饪和胃肠道消化对其变应原性的影响。利用虾过敏患者的血清通过免疫印迹检测到不同的蟋蟀蛋白。肌球蛋白轻链被鉴定为最相关的 IgE 结合蛋白，并通过 ELISA 证明其与虾肌球蛋白的交叉反应性。虽然虾肌球蛋白对胃消化的稳定性较差，但蟋蟀肌球蛋白耐受整个消化过程。在特定于虾的肌钙蛋白中，肌钙蛋白具有异常的稳定性，可耐受胃肠道消化。在富含烘烤产品的模型中，IgE 结合蛋白部分免受蛋白水解的影响。总之，食用 Acheta domesticus 蛋白可能会对甲壳类过敏人群造成严重威胁。肌球蛋白的高稳定性可能代表初级致敏和临床交叉反应的风险。
