节点文献

微生物转谷氨酰胺酶的纯化方法和酶学性质研究

Purification and enzymatic characteristics of microbial transglutaminase

  • 推荐 CAJ下载
  • PDF下载
  • 不支持迅雷等下载工具,请取消加速工具后下载。

【作者】 周楠迪田亚平华子安张雅芬堵国成陈坚

【Author】 ZHOU Nan-di, TIAN Ya-ping, HUA Zian, ZHANG Ya-fen, DU Guo-cheng, CHEN Jian (The Key Laboratory of Industrial Biotechnology, Ministry of Education, Southern Yangtze University, Wuxi, 214036)

【机构】 江南大学工业生物技术教育部重点实验室江南大学工业生物技术教育部重点实验室 无锡214036无锡214036无锡214036

【摘要】 由Streptoverticilliummobaraense发酵生产的转谷氨酰胺酶经过除菌体、超滤浓缩、乙醇沉淀、干燥后得到粗酶产品 ,其活力回收率约 70 %。又经Superdex 75凝胶过滤和Source 30S阳离子交换两步纯化后得到纯酶 ,最终酶活力收率约 37%。酶最适温度为 5 0℃ ,在 4 0℃以下稳定性良好 ;最适 pH为 6 .0 ,pH4 .0~ 8.0时比较稳定。离子强度对酶影响很小。

【Abstract】 Transglutaminase from Streptoverticillium mobaraense was primarily purified after fermentation. After removing mycelia, ultrafiltration, precipitation and lyophilization, transglutaminase was potential to use in food industry. The recovery of activity was about 70% after separation. And then the enzyme was further purified through gel filtration on Superdex75 and cation exchange on Source 30S. The final recovery of activity was about 37%. The optimal temperature of transglutaminase was 52℃ and it was stable below 40℃. The optimal pH was about 6.0 and the enzyme was most stable between pH 4.0~8.0. Ionic strength gave little effect on enzyme activity.

  • 【文献出处】 工业微生物 ,Industrial Microbiology , 编辑部邮箱 ,2004年03期
  • 【分类号】TQ920
  • 【被引频次】27
  • 【下载频次】754
节点文献中: 

本文链接的文献网络图示:

本文的引文网络