Analysis on MTGase catalysed cross-linked products of Ara h 2: structure and immunoreactivity

Analysis on MTGase catalysed cross-linked products of Ara h 2: structure and immunoreactivity
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MTGase 催化 Ara h 2 交联产物的结构和免疫反应性分析

DOI:
10.1080/09540105.2018.1529739
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发表时间:
2018-01-01
影响因子:
3
通讯作者:
Chen, Hongbing
Chen, Hongbing
中科院分区:
农林科学3区
文献类型:
--
作者:
Chang, Xuejiao;Wu, Zhihua;Chen, Hongbing

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花生是八大食物过敏原之一。Ara h 2是其主要过敏原,花生过敏患者血清中90%以上的IgE可识别Ara h 2。微生物转氨酶(MTGase)催化交联可降低Ara h 2的致敏性。交联反应既发生在分子间,也发生在分子内,可得到不同分子量的产物。本研究将MTGase催化交联后的产物分离为低分子量Ara h 2(LP Ara h 2)和高分子量Ara h 2(HP Ara h 2),并对各部分的结构、消化率、IgG和IgE结合能力进行了分析。与LP-Ara h 2相比,HP-Ara h 2具有结构更疏松、消化率更高、免疫原性更低的特点。通过控制反应条件得到不同的产物,可以使蛋白质脱敏过程得到更好的效果。
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.