Effect of transglutaminase in conjunction with glucono-δ-lactone treatment on the antigenicity and conformational structure of β-conglycinin
文献类型： 外文期刊
作者： Xing, Guangliang 1 ; Yang, Siran 1 ; Liu, Jia 1 ; Huang, Lu 2 ; Zheng, Maoqiang 1 ;
作者机构： 1.Changshu Inst Technol, Sch Biol & Food Engn, Changshu 215500, Jiangsu, Peoples R China
2.Jiangsu Acad Agr Sci, Inst Ind Crops, Nanjing 210014, Jiangsu, Peoples R China
关键词： Antigenicity; conformational changes; glucono-delta-lactone; transglutaminase; beta-conglycinin
期刊名称：INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY （ 影响因子：3.3； 五年影响因子：3.5 ）
ISSN： 0950-5423
年卷期： 2024 年 59 卷 4 期
页码：
收录情况： SCI
摘要： In this study, beta-conglycinin was treated with transglutaminase (TGase) and glucono-delta-lactone (GDL) to meticulously examine the resulting changes in both antigenicity and structural attributes. The findings elucidated a significant reduction (P < 0.05) in the antigenicity of beta-conglycinin to 72.1% and 77.5% after the modified treatment employing TGase alone or in conjunction with GDL, respectively, in contrast to the untreated samples. Electrophoretic analysis showed a decrease in the density of 7S alpha, 7S alpha ', and 7S beta, indicating the formation of high molecular weight protein aggregates because of the catalytic effect of TGase. Additionally, the simultaneous application of TGase and GDL induced modifications in the structural configuration of beta-conglycinin, as evidenced by a decrease in intrinsic fluorescence intensity, an augmentation in surface hydrophobicity, and a transition from beta-sheet to beta-turn and random coil structures. These observed alterations suggest that the decline in antigenicity is intricately linked to conformational changes, potentially influencing the exposure of antigenic epitopes. Overall, this study holds significant theoretical and practical implications for the development of hypoallergenic soy products and the enhancement of food safety.
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