Comparison of tropomyosin released peptide and epitope mapping after in vitro digestion from fish (Larimichthys crocea), shrimp (Litopenaeus vannamei) and clam (Ruditapes philippinarum) through SWATH-MS based proteomics
文献类型: 外文期刊
作者: Xu, LiLi 1 ; Zhang, Xiao Mei 2 ; Wen, Yun Qi 1 ; Zhao, Jin Long 1 ; Xu, Tong Cheng 3 ; Yong, Ling 4 ; Lin, Hong 1 ; Zhang, Hong Wei 2 ; Li, Zhen Xing 1 ;
作者机构: 1.Ocean Univ China, Coll Food Sci & Engn, 5 Yushan Rd, Qingdao 266003, Shandong, Peoples R China
2.Technol Ctr Qingdao Customs Dist, 70 Qutangxia Rd, Qingdao 266002, Shandong, Peoples R China
3.Shandong Acad Agr Sci, Inst Agrofood Sci & Technol, 202 Gongye North Rd, Jinan 250100, Peoples R China
4.China Natl Ctr Food Safety Risk Assessment, Beijing 100022, Peoples R China
关键词: Tropomyosin; In vitro digestion; Cross-reactivity; SWATH-MS based proteomics; Peptide marker; Epitope
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: 2023 年 403 卷
页码:
收录情况: SCI
摘要: Tropomyosin (TM) is a major shellfish allergen and a minor fish allergen. Different digestion profiles affect potential allergen anaphylaxis of protein. In this study, released peptides of fish-TM, shrimp-TM, and clam-TM by in vitro digestion of simulated gastric fluid (SGF), simulated intestinal fluid (SIF), and gastrointestinal (GI) were analyzed using sequential windowed acquisition of all theoretical fragment ion mass spectra (SWATH-MS) based proteomics. Results showed that digestion products of shrimp-TM yielded a lot of peptides matched T/B cell epitopes while core regions matched epitopes were distributed along the entire chain. Pepsin or trypsin-based digestion products of shrimp-TM presented many more peptides matched T/B cell epitopes compared with those of fish-TM and clam-TM. Besides, a differentiating peptide of VEKDKALSNAEGEVAAL (72-88) overlapped T/B cell epitopes could be used as a candidate peptide marker to identify tropomyosin allergen. These findings would supply new insight into the different allergenicity of tropomyosin.
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