Structure and allergenicity of a-lactalbumin:effects of ultrasonic prior to glycation and subsequent phosphorylation  

作　　者：Wenmei Chen Qiongzhen Chen Houze Zhou Yanhong Shao Yang Wang Jun Liu Zongcai Tu 

机构地区：[1]National R&D Center for Freshwater Fish Processing,College of Life Science,Jiangxi Normal University,Nanchang 330022,China [2]State Key Laboratory of Food Science and Technology,Nanchang University,Nanchang 330047,China

出　　处：《Food Science and Human Wellness》2023年第3期825-831,共7页食品科学与人类健康（英文）

基　　金：supported by Science Foundation for Young Scientists of Jiangxi Province(20202BABL215027);National Natural Science Foundation of China(31960457)。

摘　　要：Bovineα-lactalbumin(BLA)induced severe cow's milk allergy.In this study,a novel strategy combining ultrasonication,performed before glycation,and phosphorylation was proposed to reduce BLA allergenicity.Result showed that IgE-and IgG-binding capacities and the release rates of histamine and interleukin-6 from RBL-2 H3 were reduced.Moreover,intrinsic fluorescence intensity and surface hydrophobicity were decreased,whereas glycated sites(R10,N44,K79,K108,N102 and K114)and phosphorylated sites(Y36 and S112)of BLA were increased.Minimum allergenicity was detected during BLA treatment after ultrasonic prior to glycation and subsequent phosphorylation because of considerable increase in glycated and phosphorylated sites.Therefore,the decrease in allergenicity of BLA,the effect correlated well with the shielding effect of glycated sites combined with phosphorylated sites and the conformational changes.This study provides important theoretical foundations for improving and using the ultrasonic technology combined with protein modification in allergenic protein processing.

关 键 词：Bovineα-lactalbumin ALLERGENICITY ULTRASONIC Protein modification 

分 类 号：TS254[轻工技术与工程—水产品加工及贮藏工程]