Analysis on MTGase catalysed cross-linked products of Ara h 2: structure and immunoreactivity
Peanut is ranked among the eight major food allergens. Ara h 2 is its major allergen, recognized by more than 90% of serum IgE from peanut-allergic patients. Cross-linking catalysed by microbial transglutaminase (MTGase) is proved to be feasible to decrease the allergenicity of Ara h 2. The crosslin...
| Үндсэн зохиолчид: | , , , , , , , |
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| Формат: | Өгүүллэг |
| Хэл сонгох: | English |
| Хэвлэсэн: |
Taylor & Francis Group
2018-01-01
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| Цуврал: | Food and Agricultural Immunology |
| Нөхцлүүд: | |
| Онлайн хандалт: | http://dx.doi.org/10.1080/09540105.2018.1529739 |
| Тойм: | Peanut is ranked among the eight major food allergens. Ara h 2 is its major allergen, recognized by more than 90% of serum IgE from peanut-allergic patients. Cross-linking catalysed by microbial transglutaminase (MTGase) is proved to be feasible to decrease the allergenicity of Ara h 2. The crosslinking reaction occurred both inter- and intra-molecular could gain products with different molecular weights. In this study, after MTGase catalysed crosslinking, the products were separated into low molecular weight part of Ara h 2 (LP-Ara h 2) and high molecular weight part of Ara h 2 (HP-Ara h 2), and the structure, digestibility, IgG and IgE binding capability of each part were analysed. Compared with LP-Ara h 2, HP-Ara h 2 was found to have looser structure, higher digestion rate and corresponding lower immunogenicity. By controlling the reaction condition to get different products, the protein desensitization processes would get a better result. |
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| ISSN: | 0954-0105 1465-3443 |