College of Food Science and Engineering, Ocean University of China, No. 5, Yushan Road, Qingdao, Shandong Province 266003, PR China.
College of Food Science and Engineering, Ocean University of China, No. 5, Yushan Road, Qingdao, Shandong Province 266003, PR China.
Food Chem. 2018 May 15;248:287-295. doi: 10.1016/j.foodchem.2017.12.071. Epub 2017 Dec 20.
The present study was performed to determine crosslinking and oxidative reactions catalyzed by tyrosinase (Tyr), caffeic acid (CA) and their combination with respect to IgE binding potential and conformational structure of shrimp tropomyosin (TM). Cross-links and IgE binding potentials were analyzed by SDS-PAGE, western blot and indirect ELISA. While structural changes were characterized using surface hydrophobicity, ultraviolet (UV), fluorescence and circular dichroism (CD) spectroscopies. Maximum reduction in the IgG (37.19%) and IgE binding potentials (49.41%) were observed when treated with 2000 nkat/g Tyr + CA, as indicated by ELISA analyses. These findings correlated well with the denaturation of protein, as evident by slight blue shift and alterations in the ellipticities observed via structural analyses. The results demonstrated that addition of CA mediator with Tyr pronouncedly enhanced crosslinking, and altered the conformational structure, thereby mitigated allergenicity of TM, thus showing promise in developing novel food structures with reduced allergenic potential.
本研究旨在确定酪氨酸酶（Tyr）、咖啡酸（CA）及其与虾肌球蛋白（TM）的 IgE 结合潜力和构象结构催化的交联和氧化反应。通过 SDS-PAGE、western blot 和间接 ELISA 分析交联和 IgE 结合潜力。同时，使用表面疏水性、紫外（UV）、荧光和圆二色性（CD）光谱法表征结构变化。ELISA 分析表明，当用 2000nkat/g Tyr+CA 处理时，观察到 IgG（37.19%）和 IgE 结合潜力（49.41%）最大降低。这些发现与蛋白质的变性很好地相关，结构分析观察到的轻微蓝移和椭圆率的变化表明了这一点。结果表明，CA 介体与 Tyr 的添加显著增强了交联，并改变了构象结构，从而减轻了 TM 的变应原性，因此有望开发具有降低变应原性潜力的新型食品结构。
