Influence of nonthermal extraction technique and allergenicity characteristics of tropomyosin from fish (Larimichthys crocea) in comparison with shrimp (Litopenaeus vannamei) and clam (Ruditapes philippinarum)

• Published in: Food chemistry Vol. 309; p. 125575
• Main Authors: Xu, Li Li, Lin, Hong, Li, Zhen Xing, Ahmed, Ishfaq, Pramod, S.N., Lin, Hang, Lv, Liang Tao, Tian, Sheng Lan, Yu, Zhi Wen
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 30.03.2020
• Subjects: Adult; Allergenicity; Allergens - immunology; Animals; Bivalvia - chemistry; Bivalvia - metabolism; Child; Child, Preschool; clams; cross reaction; Cross Reactions; Cross-reactivity; Enzyme-Linked Immunosorbent Assay; Female; fish; Food Hypersensitivity; food processing; Humans; hydrophobicity; IgG/IgE binding; Immunoglobulin E; Immunoglobulin G; Larimichthys crocea; Litopenaeus vannamei; Male; Middle Aged; Nonthermal extraction; patients; Penaeidae - chemistry; Penaeidae - metabolism; Perciformes - metabolism; protein structure; Ruditapes philippinarum; Seafood - analysis; sequence homology; shrimp; signs and symptoms (animals and humans); Structure; Tropomyosin; Tropomyosin - immunology; tropomyosins; Young Adult; Allergenicity; Structure; Tropomyosin; Cross-reactivity; Nonthermal extraction; IgG/IgE binding
• ISSN: 0308-8146; 1873-7072; 1873-7072
• DOI: 10.1016/j.foodchem.2019.125575

•Developed a nonthermal extraction technique of high purity for fish-TM, shrimp-TM and clam-TM.•Studied that structure and IgG/IgE binding of raw and boiled fish-TM, shrimp-TM and clam-TM in system.•IgG/IgE binding assay showed high cross reactivity between shrimp-TM and clam-TM.•Fish-TM could have IgE binding ability being dependent on the source and quality of human serum to some degree.•Further confirmed that there were no significant differences of antigenicity between raw and boiled TM. Recent reports showed that patients could be sensitized to fish tropomyosin (TM), who exhibited clinical symptoms. However, little information is available on differences in TM immune cross-reactivity among fish, shrimp and clam. Moreover, allergenicity might change during the food processing owing to the change of protein structure. In this study, we developed a nonthermal extraction technique to purified TM, IgG/IgE binding, cross-reactivity and structures were compared. Results showed that raw and boiled fish-TM were not cross reactive and had weak recognition of shrimp, while, shrimp-TM and clam-TM were cross reactive. The ELISA further confirmed that fish-TM was not able to trigger allergic immune response in shrimp sensitive subjects, while, surface hydrophobicity of fish-TM was higher. The study demonstrated that fish-TM, being with high sequence similarity, did not have cross-reactivity with shrimp and clam-TM. They could have a variable degree of IgE binding depending on subject sensitivity and allergenicity.