Journal
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
Volume 96, Issue 10, Pages 3567-3574Publisher
WILEY
DOI: 10.1002/jsfa.7542
Keywords
Ara h 2; cross-linking; digestibility; antigenicity; allergenicity
Funding
- National High Technology Research and Development Program of China (863 Program) [2013AA102205]
- National Natural Science Foundation of China [21162019]
- Key Program of Natural Science Foundation of Jiangxi Province, China [20133ACB20009]
- Young Scientists Training Project of Jiangxi Province, China [20142BCB23007]
- Research Program of State Key Laboratory of Food Science and Technology [SKLF-ZZA-201302, SKLF-ZZB-201514]
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BACKGROUND: Peanut is one of the eight major food allergens. Its allergen, Ara h 2, can be recognized by over 90% of serum IgE samples from peanut-allergic patients. Therefore, reducing the allergenicity of Ara h 2 is especially important. RESULTS: In to modify Ara h 2. After crosslinking, the microstructure, digestibility, IgG binding capability and IgE binding capability of Ara h 2 were analyzed. Cross-linking decreased the potential allergenicity of Ara h 2 by masking the allergen epitope, while the antigenicity of Ara h 2 changed slightly. After crosslinking, the apparent diameter of Ara h 2 was altered from 300 to 1700 nm or 220 nm, indicating that polymerization could either be inter-or intramolecular. Regarding digestibility, crosslinked Ara h 2 was relatively more easily digested by gastric fluid compared with the untreated Ara h 2, but much more difficult in the intestinal fluid. CONCLUSION: The crosslinking reaction catalyzed by PPO, as a non-thermal process, may be beneficial for avoiding food allergy. The reaction could mask allergen epitopes, decreasing the allergenicity of Ara h 2. (C) 2015 Society of Chemical Industry
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