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Assessment of the sensitizing capacity and allergenicity of enzymatic cross‐linked arginine kinase, the crab allergen
Author(s) -
Fei DanXia,
Liu QingMei,
Chen Feng,
Yang Yang,
Chen ZhongWei,
Cao MinJie,
Liu GuangMing
Publication year - 2016
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.201500936
Subject(s) - arginine kinase , degranulation , immunoglobulin e , chemistry , allergen , sensitization , food allergy , biochemistry , enzyme , mast cell , allergy , antibody , arginine , immunology , biology , receptor , amino acid
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.