Site-specific N-glycosylation characterization and allergenicity analysis of globulin-1 S allele from wheat  

作　　者：Linglin Fu Rongrong Wang Jinru Zhou Chong Wang Yanbo Wang 

机构地区：[1]Food Safety Key Laboratory of Zhejiang Province,School of Food Science and Biotechnology,Zhejiang Gongshang University,Hangzhou 310018,China [2]Zhejiang Engineering Research Institute of Food&Drug Quality and Safety,School of Management and E-Business,Zhejiang Gongshang University,Hangzhou 310018,China

出　　处：《Food Science and Human Wellness》2023年第5期1601-1608,共8页食品科学与人类健康（英文）

基　　金：financially supported by the National Natural Science Foundation of China (31871735)。

摘　　要：N-glycans in many proteins are of great concern because of their strong association with food allergies. Triticum aestivum(bread wheat), a major food crop, is known as one of the “Big Eight” allergenic groups. However, little research has been done about N-glycans in wheat glycoproteins. In this study, a soluble wheat glycoprotein was purified from wheat and further identified as globulin-1 S allele(GSA). The wheat GSA displayed significant IgE-binding activity. Moreover, one N-glycosylation site and 6 kinds of N-glycans were identified by mass spectrometry, including 3 high mannose types and 3 complex types. Furthermore, the IgE-binding activity of wheat GSA is proved to be reduced by the removal of N-glycan, thermal treatment(temperatures > 80 ℃), and strong acidic treatment(pH 3.0). These findings would provide a better understanding of the effects of N-glycosylation, thermal treatment, and acidic treatment on the molecular characteristics of GSA, and further provide new insights into the development of hypoallergenic wheat products.

关 键 词：Triticum aestivum ALLERGEN GLYCOPROTEIN N-GLYCANS N-GLYCOSYLATION C_(18)-RPLC-MS/MS 

分 类 号：S512.1[农业科学—作物学]