介孔材料MCFs的合成及组装青霉素酰化酶的性质研究

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.