高压处理对主要过敏原牛β-乳球蛋白的结构和潜在致敏性的影响。
Effects of high hydrostatic pressure on the structure and potential allergenicity of the major allergen bovine β-lactoglobulin.
机构信息
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, PR China; School of Food Science & Technology, Nanchang University, Nanchang 330031, PR China; Jiangxi-OAI Joint Research Institute, Nanchang University, Nanchang 330047, PR China.
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, PR China; School of Food Science & Technology, Nanchang University, Nanchang 330031, PR China.
出版信息
Food Chem. 2017 Mar 15;219:290-296. doi: 10.1016/j.foodchem.2016.09.153. Epub 2016 Sep 27.
Bovine β-lactoglobulin (β-Lg) is recognized as a significant milk allergen in several countries. In this study, β-Lg was isolated and treated with high hydrostatic pressure (HHP) at 100, 200, 300, 400, and 500MPa. The allergenic properties of the HHP-treated β-Lg were characterized by indirect competitive enzyme-linked immunosorbent assay with anti-β-Lg rabbit antibody and the sera of patients allergic to cows' milk. The conformation of the HHP-treated β-Lg was examined with ultraviolet absorption spectroscopy, endogenous fluorescence spectroscopy, exogenous fluorescence spectroscopy, and circular dichroism spectroscopy analyses. The results indicated that IgG binding increased with treatment pressure, and IgE binding was lowest at 200MPa and highest at 400MPa. The tertiary structure of β-Lg changed significantly after HHP, whereas the primary and secondary structures remained stable. Overall, this study suggests that the conformational changes in HHP-treated β-Lg contribute to its altered allergenicity.
牛β-乳球蛋白（β-Lg）被认为是一些国家的重要牛奶过敏原。在这项研究中，β-Lg 被分离出来，并在 100、200、300、400 和 500MPa 的高压处理下进行了处理。用抗β-Lg 兔抗体和对牛奶过敏的患者的血清，通过间接竞争酶联免疫吸附试验对高压处理的β-Lg 的变应原性进行了表征。用紫外吸收光谱、内源荧光光谱、外源荧光光谱和圆二色性光谱分析检查了高压处理的β-Lg 的构象。结果表明，IgG 结合随处理压力的增加而增加，而 IgE 结合在 200MPa 时最低，在 400MPa 时最高。高压处理后β-Lg 的三级结构发生了显著变化，而一级和二级结构保持稳定。总的来说，这项研究表明，高压处理的β-Lg 的构象变化导致其变应原性发生改变。
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