Abstract
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 interand 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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Chang, X., Wu, Z., Zhao, R., Zhang, Y., Li, X., Yang, A., … Chen, H. (2018). Analysis on MTGase catalysed cross-linked products of ara h 2: Structure and immunoreactivity. Food and Agricultural Immunology, 29(1), 1197–1208. https://doi.org/10.1080/09540105.2018.1529739
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