title: Effect of transglutaminase-catalyzed glycosylation on the allergenicity and conformational structure of shrimp (Metapenaeus ensis) tropomyosin.
abstract: Tropomyosin (TM), a myofibrillar protein, is a major allergen in shrimp. The aim of this study was to evaluate the effect of transglutaminase (TGase)-catalyzed glycosylation on the potential allergenicity and conformational structure of TM in Metapenaeus ensis. Results showed that glycosylation of TM induced unfolding of the primary protein structure followed by loss of the secondary structure. Cleavage of certain free amino groups was observed during TGase-catalyzed glycosylation. The glycosylation rate correlated with reaction temperature. Western blotting and indirect ELISA with TM-specific polyclonal antibodies from rabbit and sera from patients allergic to shrimp demonstrated that antigenicity and potential allergenicity of TM decreased, which correlated well with the conformational changes in its structure. Considering TGase is widely utilized in the food industry, these results indicate that TGase-catalyzed glycosylation has the potential to serve as a mild method for reducing the allergenicity of shrimp products.
authors.affiliation: Laboratory of Food Safety, College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China.
authors.forename: Fangzhou
authors.initials: F
authors.lastname: Yuan
authors.affiliation: Laboratory of Food Safety, College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China.
authors.forename: Liangtao
authors.initials: L
authors.lastname: Lv
authors.affiliation: Laboratory of Food Safety, College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China. Electronic address: lizhenxing@ouc.edu.cn.
authors.forename: Zhenxing
authors.initials: Z
authors.lastname: Li
authors.affiliation: Laboratory of Food Safety, College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China.
authors.forename: Nasha
authors.initials: N
authors.lastname: Mi
authors.affiliation: Department of Dermatological, Qingdao Municipal Hospital, Qingdao 266000, China.
authors.forename: Hairong
authors.initials: H
authors.lastname: Chen
authors.affiliation: Laboratory of Food Safety, College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China.
authors.forename: Hong
authors.initials: H
authors.lastname: Lin
mesh_terms: D000485:Allergens / Q000276:immunology; D000818:Animals; D015153:Blotting, Western; D004797:Enzyme-Linked Immunosorbent Assay; D006031:Glycosylation; D006801:Humans; D033561:Penaeidae / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011817:Rabbits; D012758:Shellfish / Q000032:analysis*; D000067208:Shellfish Hypersensitivity / Q000276:immunology*; D011503:Transglutaminases / Q000378:metabolism*; D014335:Tropomyosin / Q000737:chemistry* / Q000276:immunology*
chemical_list: D000485:Allergens; D014335:Tropomyosin; D011503:Transglutaminases
keywords: 1-Anilino-8-naphthalene-sulfonate (PubChem CID: 1369); 3,3′,5,5′-Tetramethylbenzidine (PubChem CID: 41206); Acrylamide (PubChem CID: 6579); Allergenicity; Brilliant Blue R (PubChem CID: 61365); DL-Dithiothreitol (PubChem CID: 446094); Glucosamine; Glycosylation; Shrimp tropomyosin; Transglutaminase; Tween 20 (PubChem CID: 443314); o-Phthalaldehyde (PubChem CID: 4807)