RESUMO
SCOPE: The enzymatic cross-linking of an allergen by food processing may alter its sensitization potential. In this study, the IgE-binding activity and allergenicity of cross-linked thermal polymerized arginine kinase (CL-pAK) were investigated. METHODS AND RESULTS: The IgE-binding activity and stability of CL-pAK were analyzed by immunological and proteomics methods. The sensitization and potency to induce oral tolerance of CL-pAK were tested using in vivo assays and a cell model. According to the results of inhibition of ELISA, the half inhibitory concentration of AK after cross-linking changed from 1.13 to 228.36 µg/mL. The results of in vitro digestion demonstrated that CL-pAK showed more resistance to gastrointestinal digestion than native AK. Low allergenicity and capacity to induce oral tolerance in mice were shown by the sera levels of AK-specific antibodies and T-cell cytokine production. Exposure of RBL-2H3 cells to CL-pAK compared with AK, resulted in lower levels of mast degranulation and histamine. CONCLUSION: Enzymatic cross-linking with thermal polymerization of AK by tyrosinase and caffeic acid had high potential in mitigating IgE-binding activity and allergenicity, which were influenced by altering the molecular and immunological features of the shellfish protein.