Effects of methylglyoxal on shrimp tropomyosin structure and allergenicity during thermal processing

被引：4
|
作者：
Yang, Qingli [1 ]
Qu, Xin [2 ]
Wang, Xiudan [3 ]
Che, Hongxia [3 ]
Huang, Ziqian [1 ]
Ge, Xinyu [1 ]
Lv, Liangtao [1 ]
机构：
[1] Qingdao Agr Univ, Coll Food Sci & Engn, Qingdao 266109, Peoples R China
[2] Qingdao Municipal Ctr Dis Control & Prevent, 175 Shandong Rd,Shibei Dist, Qingdao 266033, Shandong, Peoples R China
[3] Qingdao Univ Sci & Technol, Coll Marine Sci & Biol Engn, Qingdao 266042, Peoples R China
来源：
FOOD CHEMISTRY-X | 2023年 / 17卷
关键词：
Shrimp; Tropomyosin; Methylglyoxal; Allergenicity; IGE-BINDING-CAPACITY; CONFORMATIONAL STRUCTURE; DICARBONYL-COMPOUNDS; TRANSGLUTAMINASE; MALONDIALDEHYDE;
D O I：
10.1016/j.fochx.2022.100532
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
This study aimed to analyze the effect of methylglyoxal (MGO) on the structure and allergenicity of shrimp tropomyosin (TM) during thermal processing. The structural changes were determined by SDS-PAGE, intrinsic fluorescence, circular dichroism, and HPLC-MS/MS. The allergenicity was evaluated by in vitro and in vivo ex-periments. MGO could cause conformational structural changes in TM during thermal processing. Moreover, the Lys, Arg, Asp, and Gln residues of TM were modified by MGO, which could destroy and/or mask TM epitopes. In addition, TM-MGO samples could lead to lower mediators and cytokines released from RBL-2H3 cells. In vivo, TM-MGO caused a significant reduction in antibodies, histamine, and mast cell protease 1 levels in sera. These results indicate that MGO can modify the allergic epitopes and reduce the allergenicity of shrimp TM during thermal processing. The study will help to understand the changes in the allergenic properties of shrimp products during thermal processing.
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页数：11
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