罗汉果蛋白酶的部分性质研究

Study on some properties of the protease from the fruit of Siraitia grosvenorii

对罗汉果蛋白酶的部分性质进行了研究。结果表明:罗汉果蛋白酶在220nm和280nm有明显紫外吸收;其粗酶在分子量为50～100ku范围内酶活占总的56%以上;该酶对酪蛋白水解能力强,对牛血清白蛋白和卵蛋白等水解能力弱;Cu2+和Tritonx-100对罗汉果蛋白酶有强抑制作用,而Fe3+、Mg2+和Na2B4O7.10H2O能明显激活酶的活性,其它所实验的金属离子和化学试剂对蛋白酶有部分抑制作用,或作用不明显。

To study some properties of the protease from the fruits of Siraitia grosvenorii.The results showed that the protease had obvious ultraviolet absorption between 220nm and 280nm,the relative activity reached 56% of all within the molecular scope of 50-100ku of its crude enzyme,the ability of enzymatic hydrolysis of casein was strong but it was weak of the other proteins such as bovine serum albumin and ovalbumin.The results also showed that Fe3＋, Mg2＋ and Na2B4O7·10H2O had obvious activation, meanwhile, Cu2＋ and Triton x-100 inhibited the activity of the protease obviously, but the influences of the other metal ions and chemical reagents that were not obviously discussed.