This work aimed to investigate the effect of enzymatic cross-linking on the allergenic potential of shrimp tropomyosin (TM), Met e 1. The cross-linked TM with laccase (CL), laccase/caffeic acid (CLC and CLC + ), and transglutaminase (CTG and CTG + ) formed macromolecules and altered the allergen conformation. The IgG/IgE-binding potentials of the cross-linked TM were reduced as confirmed by Western blotting and ELISA. Enzymatic cross-linking improved the gastrointestinal digestibility and induced a lower level of degranulation in RBL-2H3 and KU812 cells. Moreover, cross-linked TM decreased anaphylactic symptoms, as well as reduced the serum levels of IgG1, IgE, histamine, tryptase, and mMCP-1. In spleen cells, CLC + and CTG + downregulated the Th2-related cytokines and upregulated IFN-γ and IL-10. These findings revealed that CTG + has shown more potential than CLC + in mitigating the allergenicity of TM by influencing the conformational structure, enhancing the digestibility, decreasing the cellular degranulation process, and positively modulating the Th1/Th2 immunobalance.

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Compared with native parvalbumin, recombinant β-parvalbumin based on the optimized DNA sequence can be used in fish allergen confirmation.

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