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食用昆虫(粉虫和蟋蟀)中的肌氨酸激酶过敏原之间的交叉反应有限。

Limited cross reactivity among arginine kinase allergens from mealworm and cricket edible insects.

机构信息

Functional and Evolutionary Entomology, Gembloux Agro-Bio Tech, University of Liege, Passage des Deportes-2, B-5030 Gembloux, Belgium; TERRA Research and Teaching Center, Gembloux Agro-Bio Tech, University of Liege, Passage des Deportes-2, B-5030 Gembloux, Belgium.

CHU Brugman, Immunology IRIS Laboratory, Belgium.

出版信息

Food Chem. 2019 Mar 15;276:714-718. doi: 10.1016/j.foodchem.2018.10.082. Epub 2018 Oct 16.

Abstract

Insects are seen as a solution to the increasing demand for protein sources for food. However, entomophagy has unfortunately been linked to allergic reactions in Europe with people with professional contacts. As mealworms (Tenebrio molitor) and crickets (Acheta domesticus) have recently become commercially available (both whole or in food formulation) in several European countries, this research assessed the cross allergenicity of arginine kinase (AK). Based on the collection of sera from a entomology laboratory staff, oven cooked insects but also purified AK fractions were tested. Immunoblotting against the protein extracts revealed different Immunoglobulin E reactivity of sera according to the insect target species: two bands (40 and 14 kDa) for crickets and a pattern including light responses at 17, 25 and 37 kDa for mealworms. Focusing on AK, low specific allergenicity was here illustrated and discussed in relation to the development of a safe edible insect consumption by humans.

摘要

昆虫被视为解决日益增长的食品蛋白质来源需求的一种解决方案。然而,不幸的是,在欧洲,食用昆虫与职业接触者的过敏反应有关。由于黄粉虫(Tenebrio molitor)和蟋蟀(Acheta domesticus)最近在几个欧洲国家商业化供应(整只或用于食品配方),这项研究评估了精氨酸激酶(AK)的交叉变应原性。基于昆虫学实验室工作人员的血清收集,对烘烤昆虫以及纯化的 AK 进行了测试。针对蛋白质提取物的免疫印迹揭示了针对昆虫靶标物种的不同免疫球蛋白 E 反应性:蟋蟀有两条带(40 和 14 kDa),黄粉虫有包括 17、25 和 37 kDa 轻反应的模式。在这里,针对 AK,低特异性变应原性被阐明,并与人类安全食用昆虫的发展进行了讨论。

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