Soybean protein is considered as a main food allergen. This study illustrates the effects of a combination of high hydrostatic pressure (HHP) with heat treatment on soybean protein allergen. The main allergic protein β-conglycinin was isolated from low-temperature defatted soybean meal by the alkali-soluble acid precipitation method. The antigenicity and structure of β-conglycinin treated by HHP combined with heat treatment were analyzed by enzyme-linked immunosorbent assay (ELISA), western blot, non-reduced SDS-PAGE, Fourier transform infrared spectroscopy (FTIR), and fluorescence spectra. The antigenicity and immunogenicity of β-conglycinin was reduced significantly after HHP combined with heat treatment. Compared with the untreated protein, the antigenicity of β-conglycinin was lower, and it was reduced by 87.04% at 400 MPa and 100 °C for 20 min. The secondary structure of β-conglycinin changed after the combined treatment. The contents of α-helix and β-sheet decreased, but the contents of β-turn and random coils increased. The structure of the protein changed from order to disorder. Fluorescence spectroscopy showed that β-conglycinin exposed more hydrophobic groups after the combination treatment. HHP combined with heat treatment reduced the antigenicity of β-conglycinin by changing its conformation.

中文翻译：

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高静水压联合热处理对β-伴大豆球蛋白抗原性和构象的影响

大豆蛋白被认为是主要的食物过敏原。这项研究说明了高静水压（HHP）与热处理相结合对大豆蛋白过敏原的影响。采用碱溶酸沉淀法从低温脱脂豆粕中分离出主要的过敏蛋白β-伴大豆球蛋白。通过酶联免疫吸附测定（ELISA），蛋白质印迹，非还原SDS-PAGE，傅立叶变换红外光谱（FTIR）和荧光光谱分析了H​​HP结合热处理后β-伴大豆球蛋白的抗原性和结构。β的抗原性和免疫原性HHP结合热处理后，-conglycinin显着降低。与未处理的蛋白质相比，β-伴大豆球蛋白的抗原性较低，并且在400 MPa和100°C下20分钟降低了87.04％。联合治疗后β-伴大豆球蛋白的二级结构发生了变化。的内容α螺旋和β片层减少，但内容β转角和无规卷曲增加。蛋白质的结构从有序变为无序。荧光光谱显示，联合处理后β-伴大豆球蛋白暴露出更多的疏水基团。HHP结合热处理降低了β的抗原性-conglycinin通过改变其构象。