节点文献
介孔材料MCFs的合成及组装青霉素酰化酶的性质研究
Immobilization and Property of Penicillin G Acylase in the Channel of Silica Mesoporous Material MCFs
【Abstract】 Silica mesoporous material MCFs with 16.0 nm pore sizes was prepared by using non-ionic block copolymers and the swelling agents, and was used as the support for the immobilization of enzyme. Penicillin G acylase, an enzyme, was assembled in the channel of MCFs by immersion method. The activity and stability of immobilized penicillin G acylase were studied. It was found that the activity and stability of the immobilized penicillin G acylase increased significantly compared to those of free enzyme. The optimum reaction temperature is 60 ℃. After incubation at 60 ℃ for 1 h, the activity of these immobilized penicillin G acylase remains 69%. These results showed that thermostability and durability on heating of the immobilized penicillin G acylase in MCFs was improved remarkably. The silica mesoporous material MCFs with 3-dimensional channel structure is a good support for the immobilization of enzyme.
【Key words】 Mesoporous material MCFs; Penicillin G acylase; Activity; Stability;
- 【文献出处】 高等学校化学学报 ,Chemical Research In Chinese Universities , 编辑部邮箱 ,2004年11期
- 【分类号】TQ465
- 【被引频次】45
- 【下载频次】399