罗汉果蛋白酶的分离纯化和部分性质研究

Study on the Seperation,Purification and some Properties of the Protease from the Fruits of Siraitia Grosvenorii

对罗汉果蛋白酶的分离纯化和部分性质进行研究。利用硫酸铵盐析、离子交换和凝胶过滤柱层析对罗汉果蛋白酶进行了分离纯化,对纯化所得的酶进行了分子量和等电点测定。结果表明,纯化酶为电泳纯,回收率为4.2%,纯化倍数为31.1,凝胶过滤层析和SDS-PAGE电泳测得酶的分子量分别为40.3 ku和39.0 ku,等电聚焦电泳测得其等电点为8.55。

To study the seperation, purification and some properties of the protease from the fruits of siraitia grosvenorii. The protease was purified by using ammonium sulfate precipitation, ion exchange and gel filtration chromatography. At the same time, molecular weight and isoelectric point of the purified protease were also studied. The protease was purified to homogeneity with 31.1 - fold purification and a final yield of 4.2 %. The molecular weight was 40.3 ku and 39.0 ku as determined by gel filtration and SDS-PAGE respectively. The isoelectric point was pH 8.55 determined by IEF-PAGE.