高等学校化学学报

高等学校化学学报

• 研究论文 • 上一篇    下一篇

壳聚糖固定化血管紧张素转化酶及其性质

洪韫嘉, 李谭瑶, 陈波, 姚守拙   

  1. 湖南师范大学, 化学生物学及中药分析省部共建教育部重点实验室, 长沙 410081
  • 收稿日期:2008-02-28 修回日期:1900-01-01 出版日期:2009-02-10 发布日期:2009-02-10
  • 通讯作者: 陈波

Immobilization of Angiotensin Converting-enzyme on Chitosan Microspheres

HONG Yun-Jia, LI Tan-Yao, CHEN Bo*, YAO Shou-Zhuo   

  1. Key Laboratory of Chemical Biology & Traditional Chinese Medicine Research, Ministry of Education, Hunan Normal University, Changsha 410081, China
  • Received:2008-02-28 Revised:1900-01-01 Online:2009-02-10 Published:2009-02-10
  • Contact: CHEN Bo

PDF (PC)

被引次数

24

摘要： 以壳聚糖微球为载体, 戊二醛为交联剂固定化血管紧张素转化酶, 研究了酶固定化的最优条件和固定化酶的性质. 结果表明, 在戊二醛质量分数为2.5%、给酶量为8 mg/mL时, 固定化酶的比活性最大, 为0.085 U/g. 固定化酶在40~50 ℃, pH在7~9之间有最大活性, 其米氏常数Km为2.39 mmol/L. 同时, 固定化酶具有良好的稳定性, 可重复利用.

关键词: 壳聚糖, 血管紧张素转化酶, 固定化酶

Abstract: Chitosan is a polysaccharide which is widely used in enzyme immobilization as a support. Angiotensin converting-enzyme(ACE) is an important member of the rennin-angiotensin-aldosteronesystem which could cause high blood pressure. In this study, ACE was immobilized on chitosan microspheres with glutaraldehyde as cross-linking reagent. The optimum conditions and properties of immobilization enzyme were investigated. The max ratio activity was 0.085 U/g under 2.5% glutaraldehyde and 8 mg/mL soluble enzyme for immobilized enzyme. The optimum pH, temperature and Km of the immobilized enzyme were 7—9, 40—50 ℃ and 2.39 mmol/L. The immobilized ACE show higher thermal stability and can be used repeatedly to a certain extent. It was a fundamental study in order to develop the way of screening ACE inhibitor.

Key words: Chitosan, Angiotensin converting-enzyme, Immobilized enzyme

中图分类号: 

TrendMD: