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

作　　者：高波[1] 陈静[1] 朱广山[1] 傅学奇[2] 王春雷[1] 裘式伦[1] 

机构地区：[1]吉林大学化学学院无机合成与制备化学国家重点实验室,吉林大学生命科学学院长春130012 [2]吉林大学生命科学学院,长春130012

出　　处：《高等学校化学学报》2004年第11期1998-2000,共3页Chemical Journal of Chinese Universities

基　　金：国家自然科学基金 (批准号 :2 9873 0 17和 2 0 10 10 0 4);国家"九七三"计划项目 (批准号 :G2 0 0 0 0 775 0 7)资助

摘　　要：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.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.

关 键 词：介孔材料MCFs 青霉素酰化酶 活性 稳定性 

分 类 号：Q814.2[生物学—生物工程]