高等学校化学学报 ›› 2004, Vol. 25 ›› Issue (11): 1998-2000.

• 研究简报 • 上一篇    下一篇

介孔材料MCFs的合成及组装青霉素酰化酶的性质研究

高波1,2, 陈静1, 朱广山1, 傅学奇2, 王春雷1, 裘式伦1   

  1. 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, 长春130012;
    2. 吉林大学生命科学学院, 长春130012
  • 收稿日期:2003-12-16 出版日期:2004-11-24 发布日期:2004-11-24
  • 基金资助:

    国家自然科学基金(批准号:29873017和20101004);国家“九七三”计划项目(批准号:G2000077507)资助

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

GAO Bo1,2, CHEN Jing1, ZHU Guang-Shan1, FU Xue-Qi2, WANG Chun-Lei1, QIU Shi-Lun1   

  1. 1. State Key Laboratory of Inorganic Synthesis and Preparative Chemistry, College of Chemistry, Changchun 130023, China;
    2. College of Life Science, Jilin University, Changchun 130023, China
  • Received:2003-12-16 Online:2004-11-24 Published:2004-11-24

关键词: 介孔材料MCFs, 青霉素酰化酶, 活性, 稳定性

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

中图分类号: