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Despite the fact that tropomyosin (TM) has highly stable structural characteristics, thermal processing can adversely influence its immunodetection, and the mechanism involved has not been elucidated. Purified TM was heated at various temperatures, and then the IgG/IgE-binding capacity and immunodetection recovery were determined; meanwhile, the structural alterations were analyzed via spectroscopic and molecular dynamics simulation techniques. The obtained results demonstrated that heat-treated TM showed significantly increased IgG/IgE reactivity, confirmed by indirect ELISA and immunoblotting analysis, which might be attributed to the increased structural flexibility, and thus allowed TM to be recognized IgG/IgE easily. However, these structural alterations during thermal processing would contribute to the masking of some epitopes located in TM’s surface due to the presence of curled or folded conformation with a considerable reduction of the solvent-accessible surface and radius of gyration, which primarily caused immunodetection recovery reduction in the sandwich ELISA (sELISA) test. The number of antigen binding sites might play a crucial role in a sandwich immunodetection system for sensitive and precise analysis in processed foods.

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