Immobilization and Property of Penicillin G Acylase in the Channel of Silica Mesoporous Material MCFs

Abstract

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

CLC Number:

Q814.2

TrendMD:

GAO Bo, CHEN Jing, ZHU Guang-Shan, FU Xue-Qi, WANG Chun-Lei, QIU Shi-Lun . Immobilization and Property of Penicillin G Acylase in the Channel of Silica Mesoporous Material MCFs[J]. Chem. J. Chinese Universities, 2004, 25(11): 1998.

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Immobilization and Property of Penicillin G Acylase in the Channel of Silica Mesoporous Material MCFs

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