Assessment of the sensitizing capacity and allergenicity of enzymatic cross-linked arginine kinase, the crab allergen

作者：Fei, Dan-Xia; Liu, Qing-Mei; Chen, Feng; Yang, Yang; Chen, Zhong-Wei; Cao, Min-Jie; Liu, Guang-Ming^*

来源：Molecular Nutrition & Food Research, 2016, 60(7): 1707-1718.

DOI：10.1002/mnfr.201500936

• Allergenicity
• Arginine kinase
• Enzymatic cross-linking
• Thermal polymerization
• Tyrosinase

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.

• 出版日期2016-7
• 单位集美大学