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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

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【作者】 高波陈静朱广山傅学奇王春雷裘式伦

【Author】 GAO Bo 1,2, CHEN Jing1, ZHU Guang-Shan1, FU Xue-Qi2, WANG Chun-Lei1, QIU Shi-Lun 1* (1. State Key Laboratory of Inorganic Synthesis and Preparative Chemistry, College of Chemistry, 2. College of Life Science, Jilin University, Changchun 130023, China)

【机构】 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长春130012

【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.

【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
  • 【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
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