食用昆虫蛋白质组学在昆虫蛋白食品应用安全性方面的研究

Q2 Medicine
Voprosy pitaniia Pub Date : 2024-01-01 Epub Date: 2024-11-11 DOI:10.33029/0042-8833-2024-93-6-57-66
N V Tyshko, K A Timoshenko, E O Sadykova
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引用次数: 0

摘要

目前,俄罗斯联邦正在考虑使用昆虫作为食品原料的可能性,首先,昆虫被定位为完整蛋白质的来源,因此,此类产品的安全性评估方法应包括研究昆虫蛋白质的蛋白质组学特征。昆虫衍生的新型食品的蛋白质组分析不仅为评估其安全性提供了新的机会,而且还为开发从最终产品中消除潜在致敏蛋白的方法提供了新的机会。旨在破坏或修饰这类蛋白质结构的现代技术方法,即化学修饰(糖基化、磷酸化、酰化)和与多酚、花青素和其他化合物的络合,以及干湿热暴露、水解、发酵、辐照、超声波或高静水压力处理,将提供获得具有降低致敏潜力的产品的可能性。本研究旨在对昆虫蛋白的蛋白质组学分析现状及其在食品安全性方面的应用进行评估。材料和方法。工作的分析部分包括文献检索,收集国内外科学出版物中发表的信息和统计资料,检索主要使用谷歌科学院搜索引擎和PubMed、MEDLINE、EMBASE、Scopus、Web of Science、eLIBRARY等电子数据库,检索时间主要为近25年。结果。对一些食用昆虫的蛋白质组学数据进行了分析和整理。鉴定出三种节肢动物特异性蛋白质(血青素、化学感觉蛋白和气味结合蛋白),以及58种非特异性蛋白质(包括在植物中发现的蛋白质——至少52种(90%),真菌中发现的蛋白质——49种(84%),软体动物中发现的蛋白质——47种(81%),甲壳类动物中发现的蛋白质——53种(91%),其他动物中发现的蛋白质——54种(93%))。研究了昆虫蛋白通过热处理和水解降低其致敏性的可能性。结论。基于分析,得出结论,大多数昆虫蛋白不是独特的,在传统食物来源中也存在。在食用昆虫中发现的潜在ige结合过敏原主要是与其他节肢动物(螨类、甲壳类)、软体动物和线虫中存在的一些同源蛋白具有交叉反应性的泛过敏原。在节肢动物(尤其是昆虫和甲壳类动物)中,只有血青素、化学感觉蛋白和气味结合蛋白可以被归类为特定的蛋白质。在研究的所有蛋白质中,只有一种蛋白质是专门在昆虫中发现的,即所谓的蟑螂过敏原样蛋白质,由于其结构和功能尚不清楚,需要进一步研究,它占据了特殊的位置。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
[Edible insects' proteome in the safety aspect of entomoprotein's food application].

Currently, the Russian Federation is considering the possibility of using insects as food raw materials, which, first of all, is positioned as a source of complete protein, therefore, the methodology of safety assessment of such products should include studying the proteomic profile of entomoprotein. Proteome profiling of the insect-derived novel food opens fresh opportunities not only for assessing their safety, but also for developing methods of elimination of potentially allergenic proteins from the final product. Modern technological approaches aimed at destruction or modification of the structure of such proteins, namely chemical modification (glycosylation, phosphorylation, acylation) and complexation with polyphenols, anthocyanins and other compounds, along with wet and dry thermal exposure, hydrolysis, fermentation, irradiation, ultrasound or high hydrostatic pressure treatment, will provide the possibility of obtaining products with reduced allergenic potential. The purpose of the work was to assess the current state of proteomic profiling of insect proteins in the aspect of the safety of their food application. Material and methods. The analytical part of the work included literature search, collection of information and statistical materials published in domestic and foreign scientific publications, the search was conducted using the Google Academy search engine and electronic databases PubMed, MEDLINE, EMBASE, Scopus, Web of Science, eLIBRARY, mainly for the last 25 years. Results. Proteomic profile data on a number of edible insects were analyzed and systematized. Three arthropod-specific proteins (hemocyanin, chemosensory protein, and odorant-binding protein) were identified, as well as 58 nonspecific proteins (including those found in plants - at least 52 (90%), in fungi - 49 (84%), in mollusks - 47 (81%), in crustaceans - 53 (91%), and in other animals - 54 (93%). The possibility of entomoproteins' allergenicity reducing by their thermal treatment and hydrolysis was studied. Conclusion. Based on the analysis, it was concluded that most of the entomoproteins are not unique and are also present in traditional food sources. The potential IgE-binding allergens identified in edible insects correspond mainly to pan-allergens with crossreactivity with some homologous proteins present in other arthropods (mites, crustaceans), molluscs and nematodes. Only hemocyanin, chemosensory protein, and odorant-binding protein can be classified as specific proteins found in arthropods (particularly insects and crustaceans). Of all the proteins studied, only one is found exclusively in insects, the so-called cockroach allergen-like protein, which occupies a special place because its structure and function are still unclear and require further study.

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Voprosy pitaniia
Voprosy pitaniia Medicine-Medicine (all)
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