{"title":"食品加工对小麦淀粉酶胰蛋白酶抑制剂致敏特性的影响。","authors":"Peter L Weegels, Antoine H P America","doi":"10.3389/falgy.2023.1228353","DOIUrl":null,"url":null,"abstract":"<p><p>Amylase trypsin inhibitors (ATIs) play an important role in wheat allergies and potentially in non-coeliac wheat sensitivity. Food processing could be important to mitigate the pathogenic properties of ATIs, e.g., by denaturation, glycation, enzymatic hydrolysis, cross-linking, and oxidation and reduction. These modifications also impact the solubility and extractability. The complex solubility behaviour of ATI isoforms (water and salt soluble, but also chloroform-methanol soluble, solubility depending on the redox state) becomes even more complex upon processing due to denaturation and (bio)chemical modifications. This significantly hinders the feasibility of quantitative extraction. Moreover, changes in biofunctionality may occur during the process of extraction, and the changes in ATI due to food processing will be more difficult to assess. Heat treatment decreases the extractability of ATIs with water, NaCl, and other buffer extracts, and binding of IgE from wheat-allergic persons to ATIs as observed with Western blotting is decreased or absent. IgE binding is reduced with the total extract in chaotropic and reducing agents. However, it can be increased when the proteins are hydrolyzed by proteases. Fermentation involving certain species of <i>Fructolactobacilli</i> (FLB), followed by baking, decreases the amount of ATIs and IgE binding to ATIs. In yeast-fermented bread, the amount of ATIs decreased in a similar manner, but IgE binding was more prominent, indicating that there was a modification of ATIs that affected the epitope recognition. When isolated ATIs are ingested with high ATI degrading FLB, the immune response in mice is less elevated <i>in vivo</i>, when compared with ATI without high ATI degrading FLB. The pathogenic effects on the skin of dogs and one wheat-allergic child are also decreased when soluble proteins or isolated ATIs are reduced with the thioredoxin/thioredoxin reductase NADPH system. Glycation on the other hand has been shown to potentiate the allergenic properties of ATIs as evidenced by the large increase in IgE binding. The impact of food processing on the pathogenic properties of ATIs is hardly studied <i>in vivo</i> in humans. There seem to be opportunities to mitigate the pathogenic properties <i>in vitro</i>, but potentiation of pathogenic properties is also frequently observed. This requires a deeper understanding on the impact of food processing on the pathogenicity of ATIs.</p>","PeriodicalId":73062,"journal":{"name":"Frontiers in allergy","volume":"4 ","pages":"1228353"},"PeriodicalIF":3.3000,"publicationDate":"2023-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10702574/pdf/","citationCount":"0","resultStr":"{\"title\":\"Impact of food processing on the allergenic properties of amylase trypsin inhibitors from wheat.\",\"authors\":\"Peter L Weegels, Antoine H P America\",\"doi\":\"10.3389/falgy.2023.1228353\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Amylase trypsin inhibitors (ATIs) play an important role in wheat allergies and potentially in non-coeliac wheat sensitivity. Food processing could be important to mitigate the pathogenic properties of ATIs, e.g., by denaturation, glycation, enzymatic hydrolysis, cross-linking, and oxidation and reduction. These modifications also impact the solubility and extractability. The complex solubility behaviour of ATI isoforms (water and salt soluble, but also chloroform-methanol soluble, solubility depending on the redox state) becomes even more complex upon processing due to denaturation and (bio)chemical modifications. This significantly hinders the feasibility of quantitative extraction. Moreover, changes in biofunctionality may occur during the process of extraction, and the changes in ATI due to food processing will be more difficult to assess. Heat treatment decreases the extractability of ATIs with water, NaCl, and other buffer extracts, and binding of IgE from wheat-allergic persons to ATIs as observed with Western blotting is decreased or absent. IgE binding is reduced with the total extract in chaotropic and reducing agents. However, it can be increased when the proteins are hydrolyzed by proteases. Fermentation involving certain species of <i>Fructolactobacilli</i> (FLB), followed by baking, decreases the amount of ATIs and IgE binding to ATIs. In yeast-fermented bread, the amount of ATIs decreased in a similar manner, but IgE binding was more prominent, indicating that there was a modification of ATIs that affected the epitope recognition. When isolated ATIs are ingested with high ATI degrading FLB, the immune response in mice is less elevated <i>in vivo</i>, when compared with ATI without high ATI degrading FLB. The pathogenic effects on the skin of dogs and one wheat-allergic child are also decreased when soluble proteins or isolated ATIs are reduced with the thioredoxin/thioredoxin reductase NADPH system. Glycation on the other hand has been shown to potentiate the allergenic properties of ATIs as evidenced by the large increase in IgE binding. The impact of food processing on the pathogenic properties of ATIs is hardly studied <i>in vivo</i> in humans. There seem to be opportunities to mitigate the pathogenic properties <i>in vitro</i>, but potentiation of pathogenic properties is also frequently observed. This requires a deeper understanding on the impact of food processing on the pathogenicity of ATIs.</p>\",\"PeriodicalId\":73062,\"journal\":{\"name\":\"Frontiers in allergy\",\"volume\":\"4 \",\"pages\":\"1228353\"},\"PeriodicalIF\":3.3000,\"publicationDate\":\"2023-11-22\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10702574/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Frontiers in allergy\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3389/falgy.2023.1228353\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2023/1/1 0:00:00\",\"PubModel\":\"eCollection\",\"JCR\":\"Q2\",\"JCRName\":\"ALLERGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Frontiers in allergy","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3389/falgy.2023.1228353","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2023/1/1 0:00:00","PubModel":"eCollection","JCR":"Q2","JCRName":"ALLERGY","Score":null,"Total":0}
引用次数: 0
摘要
淀粉酶胰蛋白酶抑制剂(ATIs)在小麦过敏症和潜在的非乳糜泻小麦过敏症中发挥着重要作用。食品加工对减轻 ATIs 的致病特性非常重要,例如通过变性、糖化、酶水解、交联、氧化和还原。这些修饰也会影响溶解性和可提取性。由于变性和(生物)化学修饰,ATI 异构体复杂的溶解性能(水溶性和盐溶性,也可溶于氯仿-甲醇,溶解度取决于氧化还原状态)在加工过程中变得更加复杂。这极大地阻碍了定量提取的可行性。此外,在萃取过程中,生物功能可能会发生变化,食品加工导致的 ATI 变化将更难评估。热处理会降低 ATIs 与水、NaCl 和其他缓冲提取物的可提取性,用 Western 印迹法观察到的小麦过敏者的 IgE 与 ATIs 的结合会减少或消失。在混沌剂和还原剂中,总提取物与 IgE 的结合会减少。然而,当蛋白质被蛋白酶水解时,IgE结合率会增加。某些种类的果酸乳杆菌(FLB)发酵后再进行烘烤,会减少 ATIs 的数量和 IgE 与 ATIs 的结合。在酵母发酵的面包中,ATIs 的数量也以类似的方式减少,但 IgE 结合却更加明显,这表明 ATIs 发生了改变,影响了表位识别。与不含高ATI降解FLB的ATI相比,当小鼠摄入含有高ATI降解FLB的分离ATI时,体内免疫反应的升高程度较低。当使用硫氧还原酶/硫氧还原酶 NADPH 系统还原可溶性蛋白质或分离的 ATI 时,对狗和一名小麦过敏儿童皮肤的致病作用也会降低。另一方面,糖化被证明会增强 ATI 的致敏特性,IgE 结合力的大幅增加就是证明。关于食品加工对 ATIs 致病性的影响,几乎没有在人体中进行过研究。在体外似乎有机会减轻致病性,但也经常观察到致病性的增强。这就需要更深入地了解食品加工对 ATIs 致病性的影响。
Impact of food processing on the allergenic properties of amylase trypsin inhibitors from wheat.
Amylase trypsin inhibitors (ATIs) play an important role in wheat allergies and potentially in non-coeliac wheat sensitivity. Food processing could be important to mitigate the pathogenic properties of ATIs, e.g., by denaturation, glycation, enzymatic hydrolysis, cross-linking, and oxidation and reduction. These modifications also impact the solubility and extractability. The complex solubility behaviour of ATI isoforms (water and salt soluble, but also chloroform-methanol soluble, solubility depending on the redox state) becomes even more complex upon processing due to denaturation and (bio)chemical modifications. This significantly hinders the feasibility of quantitative extraction. Moreover, changes in biofunctionality may occur during the process of extraction, and the changes in ATI due to food processing will be more difficult to assess. Heat treatment decreases the extractability of ATIs with water, NaCl, and other buffer extracts, and binding of IgE from wheat-allergic persons to ATIs as observed with Western blotting is decreased or absent. IgE binding is reduced with the total extract in chaotropic and reducing agents. However, it can be increased when the proteins are hydrolyzed by proteases. Fermentation involving certain species of Fructolactobacilli (FLB), followed by baking, decreases the amount of ATIs and IgE binding to ATIs. In yeast-fermented bread, the amount of ATIs decreased in a similar manner, but IgE binding was more prominent, indicating that there was a modification of ATIs that affected the epitope recognition. When isolated ATIs are ingested with high ATI degrading FLB, the immune response in mice is less elevated in vivo, when compared with ATI without high ATI degrading FLB. The pathogenic effects on the skin of dogs and one wheat-allergic child are also decreased when soluble proteins or isolated ATIs are reduced with the thioredoxin/thioredoxin reductase NADPH system. Glycation on the other hand has been shown to potentiate the allergenic properties of ATIs as evidenced by the large increase in IgE binding. The impact of food processing on the pathogenic properties of ATIs is hardly studied in vivo in humans. There seem to be opportunities to mitigate the pathogenic properties in vitro, but potentiation of pathogenic properties is also frequently observed. This requires a deeper understanding on the impact of food processing on the pathogenicity of ATIs.