期刊
MOLECULAR NUTRITION & FOOD RESEARCH
卷 60, 期 7, 页码 1707-1718出版社
WILEY
DOI: 10.1002/mnfr.201500936
关键词
Allergenicity; Arginine kinase; Enzymatic cross-linking; Thermal polymerization; Tyrosinase
资金
- National Natural Scientific Foundation of China [31171660, U1405214]
- Scientific Foundation of Fujian Province [2014N0014]
ScopeThe 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 resultsThe 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 g/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. ConclusionEnzymatic 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.
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