Maillard reaction affecting immunobinding activity and digestibility of tropomyosin in Alectryonella plicatula food matrix
作者机构:College of Ocean Food and Biological EngineeringXiamen Key Laboratory of Marine Functional FoodFujian Provincial Engineering Technology Research Center of Marine Functional FoodJimei UniversityXiamen 361021China The Second Affiliated Hospital of Xiamen Medical CollegeXiamen 361021China
出 版 物:《Food Science and Human Wellness》 (食品科学与人类健康(英文))
年 卷 期:2024年第13卷第5期
页 面:2959-2969页
核心收录:
学科分类:0832[工学-食品科学与工程(可授工学、农学学位)] 08[工学] 083201[工学-食品科学] 083204[工学-水产品加工及贮藏工程]
基 金:supported by the National Natural Scientific Foundation of China(32072336,31871720) the National Key R&D Program of China(2019YFD0901703)
主 题:Alectryonella plicatula Food matrix Immunobinding activity Maillard reaction Tropomyosin
摘 要: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 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 ofα-helix decreased by(24.64±1.46)%.Structural transformation further explains why the Maillard reaction alters the immunobinding activity of *** addition,the Maillard reaction reduces the digestive stability of the AFM and makes TM in the *** food matrix Maillard reaction products(AFM-MRPs)more easily *** on the above research,10 amino acids on the 7 IgE epitopes of TM were *** 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.