摘要
大豆球蛋白(7S)和β-伴大豆球蛋白(11S)是大豆中两种主要的贮藏蛋白,在结构和功能特性上具有很大的差异,广泛应用于食品及非食品领域。传统分离大豆蛋白组分的方法都需要添加还原剂,其残留成为影响人体健康的安全隐患。利用微量凯氏定氮方法比较了微小毛霉凝乳酶作用于大豆蛋白和牛奶蛋白后产生的凝聚效果,发现其对大豆蛋白和牛奶蛋白有着不同的蛋白沉淀率。进一步试验表明:微小毛霉凝乳酶具有特异性的凝聚大豆蛋白11S组分的特性,且这种分离作用与酶反应降低了蛋白溶液的pH值无关。因此,微小毛霉凝乳酶可以用于大豆蛋白7S和11S组分的分离。
The major storage proteins in soybeans are glycinin and β-conglycinin, which play important roles in food and nonfood soy protein products due to their different functional properties. In conventional methods, reductants which were bad for consumer health were commonly used to separate soybean glycinin and β-conglycinin. In this study,Rennase made from Mucor pusillus was found to have different characteristics in clotting milk proteins and soy proteins by micro- Kjeldahl method. Rennase was found to clot 11S fraction particularly by further researches. The separation was proved not due to the pH value decreasing caused by the rennase simply and may be relevant to the special dotting effect of rennase,and this characteristic could be used to separating 7S and 11S fractions.
出处
《大豆科学》
CAS
CSCD
北大核心
2008年第4期654-658,共5页
Soybean Science
