毕赤酵母表达重组纳豆激酶的分离纯化  

Purification of recombinant nattokinase from genetically engineered Pichia pastoris

作　　者：许芳[1] 闫达中[1] 杨艳燕[2] 

机构地区：[1]武汉工业学院生物与制药工程学院,湖北武汉430023 [2]湖北大学生命科学学院,湖北武汉430062

出　　处：《中国酿造》2009年第12期35-37,共3页China Brewing

摘　　要：采用硫酸铵分级沉淀、Sephadex G-100柱层析以及冷冻干燥等步骤,对毕赤酵母基因工程菌发酵液中的纳豆激酶进行分离纯化,得到电泳纯的有溶栓活性的纳豆激酶。冷冻干燥品在SDS-PAGE胶上呈一条蛋白质带,其酶的比活力提高到610.64U/mg,纯度为粗酶液的15.92倍。Nattokinase with electrophoretsis activity was separated and purified by ammonium sulfate precipitation, Sephadex G-100 gel filtration and freeze drying from genetically engineered Pichia pastoris. The purified enzyme had only one protein band in SDS-PAGE and activity of nattokinase was 610.64 U/mg, which was 15.92 times as the crude enzyme.

关 键 词：毕赤酵母 纳豆激酶 分离纯化 

分 类 号：TS201.3[轻工技术与工程—食品科学]