微生物谷氨酰胺转胺酶(MTG)的分离纯化  

Separation and Purification of Microbial Transglutaminase

作　　者：何冬兰[1] 秦三敏[1] 彭宝玉[1] 李华丽[1] 

机构地区：[1]中南民族大学生命科学学院,武汉430074

出　　处：《中南民族大学学报（自然科学版）》2009年第1期35-37,共3页Journal of South-Central University for Nationalities：Natural Science Edition

基　　金：湖北工业大学湖北省工业微生物重点实验室开放基金资助项目(301;21619);中南民族大学自然科学基金资助项目(YZY02009)

摘　　要：利用产谷氨酰胺转胺酶的H-197菌株发酵产生MTG,发酵液通过高速离心、冷冻浓缩、乙醇沉淀、冷冻干燥,制得粗酶粉,粗酶粉溶解后经过Sephadex G-75柱得到较纯酶样.结果表明:经冷冻浓缩、乙醇沉淀后其活力回收率为44.6%,酶的比活为0.83 U/mg,较浓缩前增加了2.43倍;粗酶经Sephadex G-75凝胶过滤层析后得到较纯的酶,酶的比活力为1.44 U/mg,最终纯化倍数达7.08.The microbial transglutaminase(MTG) was separated and purified from the culture solution of the transglutaminase-producing strain of H-197.The crude enzyme power was prepared from the fermentation culture through ultracentrifugation,freeze concentration,precipitation with ethanol and freeze-drying.The specific activity and total protein recovery rate of MTG was about 0.83 U/mg and 44.6 % respectively,which was higher by about 2.4 times more than the pre-concentration sample.The crude enzyme power was furthe...

关 键 词：谷氨酰胺转胺酶 分离 纯化 SEPHADEX G-75凝胶 

分 类 号：TQ925[轻工技术与工程—发酵工程]