【作者】 刘楚怡； 薛文通； 李阳；

【Author】 LIU Chu-yi,XUE Wen-tong~*,LI Yang (College of Food Science and Nutritional Engineering,China Agricultural University,Beijing 100083,China)

【机构】 中国农业大学食品科学与营养工程学院；

【摘要】 本文对常见食物过敏原青鱼(Mylopharyngodon piceus)蛋白进行了特异性抗原的识别,并通过模拟肠胃液消化试验,分析了青鱼肌肉中过敏原的消化特性以及消化对过敏蛋白致敏性的影响。本文使用十二烷基硫酸钠.聚丙烯酰胺凝胶电泳(SDS-PAGE)和免疫印记方法(Western-blot)识别青鱼肌肉中过敏原,发现在青鱼主要存在的14条蛋白条带中主要致敏条带为27kDa和17kDa两条。采用美国药典提供的模拟肠液配方,测定熟青鱼蛋白在体外模拟肠胃环境中的消化稳定性。在模拟肠液反应中,生成分子质量为121kDa新致敏蛋白,且致敏性不随消化时间延长而减小。该过敏蛋白具有较高的消化稳定性。更多还原

【Abstract】 The aim of this study was to investigate the major allergens and its thermodynamic stability and in vitro intestinal digestion research of Black Carp(Mylopharyngodon piceus).Water-soluble protein was extracted from fish’s muscle and the relative contents of major allergens were quantified by SDS-PAGE densitometry,and then Immuno-blot was applied in identifying allergens.The Black Carp proteins were heated in water bath under various conditions to determination their thermal stability.In results of the SDS-PAGE,14 protein bands mainly exist in Black Carp muscle proteins,through the methods of Western blot,the major allergen of Black Carp were detected as 27kDa and 17kDa,among these two proteins,27kDa band was on thermal stability,it still has the immunity activity even after 30min of heating boiling.The digestion experiment was developed to represent human intestinal conditions as the method of U.S.Pharmacopeia,it revealed that Black carp proteins were degraded mostly within 1 minute and generated to a new 121kDa sensitization allergic protein.The allergic protein has higher digestive stability.更多还原