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交联血管紧张素转化酶聚集体的制备及性质

曾伟秀1,田清青1,2,赵昕1,陈波1*   

  1. (1.湖南师范大学化学生物学中药分析省部共建教育部重点实验室 长沙 410081;
    2.湖南中医药高等专科学校 株洲 412008)
  • 收稿日期:2012-09-18 修回日期:2012-11-20 出版日期:2013-07-10 发布日期:2013-07-10
  • 通讯作者: 陈波，教授; Tel:0731-88865515; Fax:0731-88872046; E-mail:dr-chenpo@vip.sina.com; 研究方向：中药及色谱分析
  • 基金资助:
    国家“863”课题（2010AA023001）国家自然科学基金（20927005，21275049，81274178）湖南省科技计划课题（2010TT1001）和湖南省高校科技创新团队支持计划资助

Preparation and Properties of Cross-linked Angiotensin Converting Enzyme Aggregates

ZENG Weixiu1, TIAN Qingqing1,2, ZHAO Xin1, CHEN Bo1*   

  1. (1.Key Laboratory of Chemical Biology and Traditional Chinese Medicine Research Ministry of Education,Hunan Normal University,Changsha  410081,China;
    2.Hunan Traditional Chinese Medical College,Zhuzhou 412008,China)
  • Received:2012-09-18 Revised:2012-11-20 Published:2013-07-10 Online:2013-07-10
  • Contact: CHEN Bo

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1336

被引次数

2

摘要： 制备了交联血管紧张素转化酶聚集体（ACE-CLEAs），比较了ACE-CLEAs及游离ACE的酶学性质，包括最适酶促反应温度、最适pH值、Km、vmax、温度稳定性及pH稳定性等。 以酶活力回收率为参考，确定了制备ACE-CLEAs的最佳条件为：饱和度为80%的(NH4)2SO4溶液作为沉淀剂，沉淀时间0.5 h，质量分数为0.02%的戊二醛作为交联剂，交联时间1 h。 通过比较酶学性质发现，ACE-CLEAs比游离ACE具有更好的温度稳定性及pH稳定性，且与游离ACE接近的Km值表明，ACE-CLEAs对底物的亲和力与游离酶几乎相当。

关键词: 血管紧张素转化酶, 交联酶聚集体, 固定化

Abstract: Cross-linked angiotensin converting enzyme aggregates(ACE-CLEAs) were prepared and their characteristics were compared with that of free ACE including optimal temperature and pH, Km, vmax, thermal and pH stabilities. Based on the relative activity of immobilized enzyme, the optimal preparation conditions should be as follows:precipitating the enzyme with 80% saturated ammonium sulfate for 0.5 h, and then cross-linking it with 0.02%(mass fraction) glutaraldehyde for 1 h. According to the comparison for enzymology property, ACE-CLEAs had better thermal and pH stabilities than free ACE, and the Km of ACE-CLEAs was close to that of free ACE, suggesting that ACE-CLEAs had an almost equal affinity to enzyme as the free ACE.

Key words: Angiotensin Converting Enzyme, Cross-linked Enzyme Aggregates, Immobilization

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