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作 者:Shiqiang Yang Yexin Chen Fei Huan Xinrong He Xiao Yun Hong Liu Guixia Chen Guangming Liu
机构地区:[1]College of Ocean Food and Biological Engineering,Xiamen Key Laboratory of Marine Functional Food,Fujian Provincial Engineering Technology Research Center of Marine Functional Food,Jimei University,Xiamen 361021,China [2]Women and Children’s Hospital Affi liated to Xiamen University,Xiamen 361003,China [3]College of Marine Biology,Xiamen Ocean Vocational College,Xiamen,Fujian 361100,China
出 处:《Food Science and Human Wellness》2024年第6期3697-3707,共11页食品科学与人类健康(英文)
基 金:supported by the National Natural Scientific Foundation of China(32072336,32472449).
摘 要:Oyster,as a common aquatic food,play an important role in shellfish allergy.In this study,2 tropomyosin(TM)isoforms TM-αand TM-β(TM-α/-β)in Alectryonella plicatula were identified.The sequences of 852 bp encoding 284 amino acids of TM-α/-βand 2 recombinant proteins were obtained,respectively.There were 12 amino acid differences between TM-α/-β.The results of immunological experiments indicated that TM-βhad stronger immunobinding activity and immunoreactivity than those of TM-α.Structural analysis showed that TM-βhad moreα-helix and higher surface hydrophobicity than TM-α.Sequences and epitopes alignment with shellfish TMs revealed that amino acids of TM-βwere more frequently recognized as IgE epitopes in other shellfish TMs than TM-α.Differences in structure and sequence account for the higher immunological activity of TM-βcompared to TM-α.These findings provide a theoretical basis for enriching the understanding of shellfish TM and accurate diagnosis of allergic components.
关 键 词:Alectryonella plicatula ALLERGEN Immunological activity ISOFORMS TROPOMYOSIN
分 类 号:TS254.1[轻工技术与工程—水产品加工及贮藏工程]
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