摘要
采用化学改性的壳聚糖为载体,共价法偶联胰蛋白酶,制成抑酶肽亲和吸附剂,将其直接亲和层析牛肺提取液,分离、纯化高比活力的抑酶肽。抑酶肽抑制比活力为71 428 BAEE.mg-1,酶活性回收率为62.5%。该方法质量稳定,成本较低,吸附剂机械强度高,抗污染能力较强,非特异性吸附较小,可反复使用,价格低廉,适于应用。
Trypsin was covalently linked with chemical modified granule chitosan and was used to isolate and purify aprotinin from the extract of cattle lungs by affinity chromatography. Then high-purlty aprotinin was prepared after ultrafiltrating and freeze drying. The result shows： the specific activity of immobilized trypsin on chitosan is 71 428 BAEE/mg, and the activity recovery of trypsin is 62.5%. The purity of aprotinin is high, and it could be used for several times. It is accepted as a simple and stable method suitable for purifying aprotinin with high activity in industrial manufacturing.
出处
《河北工业科技》
CAS
2006年第3期149-151,共3页
Hebei Journal of Industrial Science and Technology
关键词
固定化酶
亲和层析
抑酶肽
壳聚糖
immobilized trypsin on chitosan
affinity chromatography
aprotinin
chitosan
