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Issue 3, 2017
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Ara h 2 cross-linking catalyzed by MTGase decreases its allergenicity

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Abstract

Peanuts, whose major allergen is Ara h 2, are included among the eight major food allergens. After reduction using dithiothreitol (DTT), cross-linking of Ara h 2 could be catalyzed by microbial transglutaminase (MTGase), a widely used enzyme in the food industry. In this study, Ara h 2 cross-linking was catalyzed by MTGase after it was reduced by DTT. Using mass spectrometry and PLINK software, five cross-linkers were identified, and five linear allergen epitopes were found to be involved in the reactions. The IgE binding capacity of cross-linked Ara h 2 was found to be significantly lower compared to that of native and reduced Ara h 2. After simulated gastric fluid (SGF) digestion, the digested products of the cross-linked Ara h 2, again, had a significantly lower IgE binding capacity compared to untreated and reduced Ara h 2. Furthermore, reduced and cross-linked Ara h 2 (RC-Ara h 2) induced lower sensitization in mice, indicating its lower allergenicity. Reduction and MTGase-catalyzed cross-linking are effective methods to decrease the allergenicity of Ara h 2. The reactions involved linear allergen epitopes destroying the material basis of the allergenicity, and this might develop a new direction for protein desensitization processes.

Graphical abstract: Ara h 2 cross-linking catalyzed by MTGase decreases its allergenicity

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Publication details

The article was received on 18 Sep 2016, accepted on 07 Feb 2017, published on 09 Feb 2017 and first published online on 09 Feb 2017


Article type: Paper
DOI: 10.1039/C6FO01365A
Citation: Food Funct., 2017,8, 1195-1203
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    Ara h 2 cross-linking catalyzed by MTGase decreases its allergenicity

    Z. Wu, J. Lian, R. Zhao, K. Li, X. Li, A. Yang, P. Tong and H. Chen, Food Funct., 2017, 8, 1195
    DOI: 10.1039/C6FO01365A

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