{"title":"马氏反应影响栉水母食物基质中肌球蛋白的免疫结合活性和消化率","authors":"","doi":"10.26599/FSHW.2022.9250239","DOIUrl":null,"url":null,"abstract":"<div><div>In recent years, the allergy rate of oysters has surged, and daily food processing methods make it hard to reduce heat resistance and digestive allergy such as tropomyosin (TM). In this study, the Maillard reaction with xylose (Xyl) significantly reduced the IgE binding capacity of <em>Alectryonella plicatula</em> food matrix (AFM), that reduced by (77.81 ± 2.68)%. The study found the Maillard reaction changes the structure of the AFM, in which the content of <em>α</em>-helix decreased by (24.64 ± 1.46)%. Structural transformation further explains why the Maillard reaction alters the immunobinding activity of AFM. In addition, the Maillard reaction reduces the digestive stability of the AFM and makes TM in the <em>A. plicatula</em> food matrix Maillard reaction products (AFM-MRPs) more easily digested. Based on the above research, 10 amino acids on the 7 IgE epitopes of TM were modified. This result indicates that the Maillard reaction reduces the immunobinding activity of the AFM by changing the structure and modifying the amino acids on the epitope.</div></div>","PeriodicalId":12406,"journal":{"name":"Food Science and Human Wellness","volume":"13 5","pages":"Pages 2959-2969"},"PeriodicalIF":5.6000,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Maillard reaction affecting immunobinding activity and digestibility of tropomyosin in Alectryonella plicatula food matrix\",\"authors\":\"\",\"doi\":\"10.26599/FSHW.2022.9250239\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>In recent years, the allergy rate of oysters has surged, and daily food processing methods make it hard to reduce heat resistance and digestive allergy such as tropomyosin (TM). In this study, the Maillard reaction with xylose (Xyl) significantly reduced the IgE binding capacity of <em>Alectryonella plicatula</em> food matrix (AFM), that reduced by (77.81 ± 2.68)%. The study found the Maillard reaction changes the structure of the AFM, in which the content of <em>α</em>-helix decreased by (24.64 ± 1.46)%. Structural transformation further explains why the Maillard reaction alters the immunobinding activity of AFM. In addition, the Maillard reaction reduces the digestive stability of the AFM and makes TM in the <em>A. plicatula</em> food matrix Maillard reaction products (AFM-MRPs) more easily digested. Based on the above research, 10 amino acids on the 7 IgE epitopes of TM were modified. This result indicates that the Maillard reaction reduces the immunobinding activity of the AFM by changing the structure and modifying the amino acids on the epitope.</div></div>\",\"PeriodicalId\":12406,\"journal\":{\"name\":\"Food Science and Human Wellness\",\"volume\":\"13 5\",\"pages\":\"Pages 2959-2969\"},\"PeriodicalIF\":5.6000,\"publicationDate\":\"2024-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Science and Human Wellness\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2213453024002167\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Science and Human Wellness","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2213453024002167","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Maillard reaction affecting immunobinding activity and digestibility of tropomyosin in Alectryonella plicatula food matrix
In recent years, the allergy rate of oysters has surged, and daily food processing methods make it hard to reduce heat resistance and digestive allergy such as tropomyosin (TM). In this study, the Maillard reaction with xylose (Xyl) significantly reduced the IgE binding capacity of Alectryonella plicatula food matrix (AFM), that reduced by (77.81 ± 2.68)%. The study found the Maillard reaction changes the structure of the AFM, in which the content of α-helix decreased by (24.64 ± 1.46)%. Structural transformation further explains why the Maillard reaction alters the immunobinding activity of AFM. In addition, the Maillard reaction reduces the digestive stability of the AFM and makes TM in the A. plicatula food matrix Maillard reaction products (AFM-MRPs) more easily digested. Based on the above research, 10 amino acids on the 7 IgE epitopes of TM were modified. This result indicates that the Maillard reaction reduces the immunobinding activity of the AFM by changing the structure and modifying the amino acids on the epitope.
期刊介绍:
Food Science and Human Wellness is an international peer-reviewed journal that provides a forum for the dissemination of the latest scientific results in food science, nutriology, immunology and cross-field research. Articles must present information that is novel, has high impact and interest, and is of high scientific quality. By their effort, it has been developed to promote the public awareness on diet, advocate healthy diet, reduce the harm caused by unreasonable dietary habit, and directs healthy food development for food industrial producers.