摘要
粗酶粉用ＰＨ７．５的Ｔｒｉｓ．ＨＣｌ缓冲剂抽提１６ｈ，提液离心去渣后通过晨光ＣＧＢ－６８５弱碱性阴离子交换树脂柱，经乙醇沉淀及干燥制得精酶粉，酶活总收率４９．６％；酶粉活力达６．７×１０＾５Ｕ／ｇ．
A procedure for purification of neutral proteinase from crude enzyme of Bact7lus subtz7is is reported. The crude enzyme was extracted with Tris. HCl buffer and then purified by ion exchange chromatography with Chengguang CGB-685 resin and followcd by ethanol precipitation. The final product had an activity of 6.7x105 U/g, with a recovery of 49-6%.
出处
《中国医药工业杂志》
CAS
CSCD
北大核心
1994年第5期198-200,共3页
Chinese Journal of Pharmaceuticals
关键词
蛋白酶
离子交换
纯化
neutral proteinase, ion exchange, purification
