摘要
采用大容量(250×4mL)低速(5300×g)离心机分离β-伴大豆球蛋白和大豆球蛋白,进行碱溶条件、酸沉条件等条件的研究。结果表明:提取蛋白的碱性溶液(pH8.5的Tris-HCl溶液)离心效果较佳,沉淀大豆球蛋白pH6.4为佳,沉淀β-伴大豆球蛋白pH4.8为佳,用pH5.0沉淀杂蛋白离心分离效果较好;每一个待离心的浊液,在离心之前4℃冷藏2h以上,对离心效果的提高十分有效;采用最佳条件,从300g脱脂豆片分离大豆球蛋白和β-伴大豆球蛋白,收率分别为6.8%和2.2%,用SDS-PAGE电泳实验方法测定大豆球蛋白和β-伴大豆球蛋白样品纯度分别为89.1%和78.9%。因此该低速离心法较适合数十克级别的β-伴大豆球蛋白和大豆球蛋白的分离。
β-conglycinin and glycinin were separated by large-capacity（250×4 mL） low-speed（5300×g） centrifugation at the condition of alkali dissolution and acid precipitation.Results indicated that better centrifugation efficiency of soybean protein was in pH 8.5 Tris-HCl solution;The optimal pH values for precipitating glycinin and β-conglycinin were 6.4 and 4.8,respectively.Meanwhile,the optimal pH for removing the impure proteins was 5.0.The enhancement of entrifugation efficiency was achieved by keeping turbid liquid at 4 ℃ for more than 2 h before centrifugation.Under the optimal conditions,the yields of glycinin and β-conglycinin were 6.8% and 2.2%,respectively.The purities of separated proteins determined by SDS-PAGE were 89.1% and 78.9%.Low-speed centrifugation is suitable for separating β-conglycinin and glycinin.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2011年第6期11-15,共5页
Food Science
基金
黑龙江省自然科学基金重点项目(ZD200902)
