大豆科学2013，Vol.32Issue(1)：89-92,97,5.
大豆胰蛋白酶抑制因子的分离纯化
Extraction and Purification of Soybean Trypsin Inhibitor
摘要
Abstract
In this paper,soybean meal was used as raw material. The crude extract of the soybean trypsin inhibitor( STI) was obtained by the extraction of phosphoric acid buffer (pH7. 6) , thermal denaturation(65℃ )and ammonium sulfate precipitation. Then this extract was purified by DE-52 ion exchange,affinity chromatography and sephadex G-75 gel filtration. The results showed that the specific activity of soybean trypsin inhibitor reached 4 600 U·mg-1 and purification factor of 73.85 was obtained. The purified STI gave two protein bands in SDS-PAGE eleclrophoresis. Its molecular weights were estimated to be 21.92 and 20.04 kDa. Due to the ease and simpleness of the procedure and high efficiency, the method has an important reference value to research and production of soybean trypsin inhibitor.关键词
大豆/胰蛋白酶抑制因子/分离/提取/纯化Key words
Soybean/Trypsin inhibitor/Seperation/Extraction/Purification分类
农业科技引用本文复制引用
谷春梅,韩玲玲,曲洪生,宋鑫秀,赵琳琳,潘姝,秦贵信..大豆胰蛋白酶抑制因子的分离纯化[J].大豆科学,2013,32(1):89-92,97,5.基金项目
国家自然科学基金项目(31000769) （31000769）
