Lab of Food Safety, College of Food Science and Engineering, Ocean University of China, Qingdao 266003, Shandong, China.
Lab of Food Safety, College of Food Science and Engineering, Ocean University of China, Qingdao 266003, Shandong, China.
Food Chem. 2015 May 15;175:374-80. doi: 10.1016/j.foodchem.2014.12.001. Epub 2014 Dec 9.
The aim of this work was to determine the effect of malondialdehyde (MDA) treatment of shrimp tropomyosin (TM) with respect to IgE binding capacity and conformational structure. Following treatment with MDA, changes in TM molecular weight were characterized by SDS-PAGE and TM cross-linking was observed, then the aggregates were recognized by IgG/IgE in immunoblot analysis. Meanwhile, TM allergenicity slowly decreased following MDA treatment. These data show a correlation between the loss of TM structure and allergenic potential. TM secondary structure became more disordered following treatment with increasing concentrations of MDA. Moreover, the enhancement of surface hydrophobicity was also in accordance with the effect caused by MDA. Additionally, MDA treatment resulted in an increase in carbonyl content and a decrease in free amine groups and available lysine. The results suggest that MDA-induced conformational changes in TM can significantly influence the antigenicity and allergenicity of TM.
本工作旨在研究丙二醛(MDA)处理对虾肌球蛋白轻链(TM)的 IgE 结合能力和构象结构的影响。MDA 处理后,通过 SDS-PAGE 对 TM 分子量的变化进行了特征分析,并观察到 TM 的交联,然后通过免疫印迹分析识别聚集物中的 IgG/IgE。同时,TM 的变应原性随着 MDA 处理逐渐降低。这些数据表明 TM 结构和变应原性之间存在相关性。随着 MDA 浓度的增加,TM 的二级结构变得更加无序。此外,表面疏水性的增强也与 MDA 引起的效应一致。此外,MDA 处理导致羰基含量增加,游离胺基和可用赖氨酸减少。结果表明,MDA 诱导的 TM 构象变化可显著影响 TM 的抗原性和变应原性。