高等学校化学学报 ›› 1991, Vol. 12 ›› Issue (5): 703.

• 论文 • 上一篇    下一篇

枯草芽孢杆菌86315α-淀粉酶的研究(Ⅰ)--热稳定性研究

史永昶, 姜涌明, 隋德新, 吴燕   

  1. 江苏农学院生化教研室, 225001
  • 收稿日期:1990-06-21 出版日期:1991-05-24 发布日期:1991-05-24
  • 通讯作者: 姜涌明

Studies on a-Amylase from Bacillus Subtilis 86315(Ⅰ)--The Thermal Stability of a-Amylase

Shi Yong-chang, Jiang Yong-ming, Sui De-xin, Wu Yan   

  1. Department of Biochemistry, Jiangsu Agricultural College, Yangzhou, 225001
  • Received:1990-06-21 Online:1991-05-24 Published:1991-05-24

摘要: 研究了温度对枯草芽抱杆菌86315α-淀粉酶的活性和荧光光谱的影响.发现该酶在50℃以下是稳定的;70℃加热10min,酶活性全部丧失,荧光光谱发生了较大的变化;在0.02mol/LCaCl2和0.02mol/LNaCI同时存在下,70℃加热10min,酶活性保持不变,其光谱接近天然态酶的荧光光谱.实验表明,一定比例的CaCl2和NaCl能够较好地稳定α-淀粉酶的构象,从而大大提高其热稳定性。

关键词: 枯草芽孢杆菌86315, &alpha, -淀粉酶, 热稳定性, 荧光光谱

Abstract: The thermal stability and the fluorescence spectra of α-amylase from bacillus subtilis 86315 are studied in this paper. The enzyme is stable below 50℃. Heated at 70℃ for 10 min the enzyme loses its all activity, at the same time, a considerable change of its fluorescence spectra was observed. The α-amylase in the solution including 0. 02 mol/L CaCl2and 0. 02 mol/L NaCl retains its activity on heating at 70℃ for 10 min, and its fluorescence spectrum is close to that of the native enzyme. The experimental results show that a proper ratio of CaClz to NaCl could stabilize the conformation of a-amylase, thus raising its thermal stability greatly.

Key words: Bacillus subtilis86315, α-Amylase, Thermal stability, Fluorescence spectra

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