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Influence of thermal processing on the allergenicity of peanut proteins

机译:热处理对花生蛋白的致敏性的影响

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Peanuts are one of the most common and severe food allergens. Nevertheless, the occurrence of peanut allergy varies between countries and depends on both the exposure and the way peanuts are consumed. Processing is known to influence the allergenicity of peanut proteins. The aim of this study was to assess the effect of thermal processing on the IgE-binding capacity of whole peanut protein extracts and of the major peanut allergens Ara h 1 and Ara h 2. Whole proteins, Ara h 1, and Ara h 2 were extracted and purified from raw, roasted and boiled peanuts using selective precipitation and multiple chromatographic steps, and were then characterized by electrophoresis and mass spectrometry. The immunoreactivity of whole peanut extracts and purified proteins was analyzed by the enzyme allergosorbent test (EAST) and EAST inhibition using the sera of 37 peanut-allergic patients. The composition of the whole protein extracts was modified after heat processing, especially after boiling. The electrophoretic pattern showed protein bands of low molecular weight that were less marked in boiled than in raw and roasted peanuts. The same low-molecular-weight proteins were found in the cooking water of peanuts. Whole peanut protein extracts obtained after the different processes were all recognized by the IgE of the 37 patients. The IgE-binding capacity of the whole peanut protein extracts prepared from boiled peanuts was 2-fold lower than that of the extracts prepared from raw and roasted peanuts. No significant difference was observed between protein extracts from raw and roasted peanuts. It is noteworthy that the proteins present in the cooking water were also recognized by the IgE of peanut-allergic patients. IgE immunoreactivity of purified Ara h 1 and Ara h 2 prepared from roasted peanuts was higher than that of their counterparts prepared from raw and boiled peanuts. The IgE-binding capacity of purified Ara h 1 and Ara h 2 was altered by heat treatment and in particular was increased by roasting. However, no significant difference in IgE immunoreactivity was observed between whole protein extracts from raw and roasted peanuts. The decrease in allergenicity of boiled peanuts results mainly from a transfer of low-molecular-weight allergens into the water during cooking.
机译:花生是最常见和最严重的食物过敏原之一。但是,花生过敏的发生因国家而异,取决于花生的暴露量和食用方式。已知加工会影响花生蛋白的致敏性。本研究的目的是评估热处理对整个花生蛋白提取物和主要花生过敏原Ara h 1和Ara h 2的IgE结合能力的影响。全蛋白分别为Ara h 1和Ara h 2使用选择性沉淀和多个色谱步骤从生,烤和煮熟的花生中提取和纯化,然后通过电泳和质谱进行鉴定。花生全脂提取物和纯化蛋白的免疫反应性通过酶促过敏吸附试验(EAST)和使用37名花生过敏患者的血清对EAST抑制作用进行分析。整个蛋白质提取物的成分在热处理后,尤其在煮沸后进行了修饰。电泳图谱显示,低分子量的蛋白质条带在煮熟时比在生花生和烘焙过的花生中的标记少。在花生的烹饪水中发现了相同的低分子量蛋白质。在37个患者的IgE中,经过不同过程获得的全花生蛋白提取物均被识别。由煮沸的花生制成的整个花生蛋白提取物的IgE结合能力比由生的和烘烤的花生制成的提取物的IgE结合能力低2倍。从生花生和烤花生中提取的蛋白质之间没有观察到显着差异。值得注意的是,花生过敏患者的IgE也可以识别出烹饪水中存在的蛋白质。由烤花生制成的纯化的Ara h 1和Ara h 2的IgE免疫反应性高于由生花生和煮熟的花生制成的IgE免疫反应性。通过热处理改变了纯化的Ara h 1和Ara h 2的IgE结合能力,特别是通过焙烧提高了其结合力。但是,从生花生和烤花生的全蛋白提取物中,未观察到IgE免疫反应性的显着差异。煮花生的致敏性降低主要是由于烹饪过程中低分子量致敏原转移到水中。

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