Influence of linoleic acid on the immunodetection of shrimp (Litopenaeus vannamei) tropomyosin and the mechanism investigation via multi-spectroscopic and molecular modeling techniques
文献类型： 外文期刊
作者： Zhao, Jinlong 1 ; Liu, Yuhai 4 ; Xu, Lili 5 ; Sun, Lirui 6 ; Chen, Guanzhi 7 ; Wang, Hao 1 ; Zhang, Ziye 1 ; Lin, Hong 1 ; Li, Zhenxing 1 ;
作者机构： 1.Ocean Univ China, Coll Food Sci & Engn, 5 Yushan Rd, Qingdao 266003, Shandong, Peoples R China
2.Southeast Univ, Sch Publ Hlth, Key Lab Environm Med & Engn, Minist Educ, 87 Dingjiaqiao Rd, Nanjing 210009, Jiangsu, Peoples R China
3.Southeast Univ, Sch Publ Hlth, Dept Nutr & Food Hyg, 87 Dingjiaqiao Rd, Nanjing 210009, Jiangsu, Peoples R China
4.Dawning Int Informat Ind Co Ltd, 169 Songling Rd, Qingdao 266101, Shandong, Peoples R China
5.Shandong Acad Agr Sci, Inst Agrofood Sci & Technol, 202 Gongye North Rd, Jinan 250100, Peoples R China
6.Qingdao Univ, Sch Publ Hlth, Ning Xia Rd 308, Qingdao 266071, Peoples R China
7.Qingdao Univ, Dept Dermatol, Affiliated Hosp, 16 Jiangsu Rd, Qingdao 266003, Shandong, Peoples R China
8.Ocean Univ China, Coll Food Sci & Engn, Food Safety Lab, Qingdao, Peoples R China
关键词： Shrimp(Litopenaeusvannamei) tropomyosin; Linoleic acid; Matrix effect; Immunodetection; Spectroscopic analysis; Molecular modeling
期刊名称：FOOD CHEMISTRY （ 影响因子：8.8； 五年影响因子：8.6 ）
ISSN： 0308-8146
年卷期： 2024 年 434 卷
页码：
收录情况： SCI
摘要： The effect of linoleic acid (LA) on the IgG/IgE recognition, in vitro digestibility and immunodetection of shrimp tropomyosin (TM) was investigated. Subsequently, the simultaneous binding of LA-TM was explored using multispectroscopic and molecular modeling techniques. Our findings reveled that the addition of LA significantly reduced TM's IgG/IgE immunoreactivity, digestibility, and immunodetection. Further analysis using multi spectroscopic and molecular modeling techniques indicated that while TM's secondary structure remained largely unchanged, its 3-D structure showed significant alterations such as increased particle size and hydrophobic surface area, and a higher number of buried hydrophobic residues exposed due to the binding of LA to TM. These structural changes rendered it difficult for target antibodies and digestive enzymes to interact with related epitopes and cleavage sites buried inside the molecule. The results obtained in this study provide valuable insights into the molecular mechanism of poor immunodetection caused by food matrix interference.
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