食品科学 ›› 2008, Vol. 29 ›› Issue (4): 272-277.

• 生物工程 • 上一篇    下一篇

Aspergillus ficuum菊粉酶酶学性质的研究

 王静, 金征宇, 孙宝国, 曹雁平   

  1. 京工商大学化学与环境工程学院; 江南大学食品学院; 北京工商大学化学与环境工程学院;
  • 出版日期:2008-04-15 发布日期:2011-08-24

Characteristics of Exoinulinase and Endoinulinase from Aspergillus ficuum

 WANG  Jing, JIN  Zheng-Yu, SUN  Bao-Guo, CAO  Yan-Ping   

  1. 1.College of Chemistry and Environment Engineering, Beijing Technology and Business University; 2.School of Food Science and Technology, Jiangnan University
  • Online:2008-04-15 Published:2011-08-24

摘要: 本实验对Aspergillus ficuum产菊粉酶体系中的外切菊粉酶和内切菊粉酶的酶学性质进行了研究,研究表明二者酶学性质非常相似:两种酶的最适反应温度均在45℃左右;外切菊粉酶的最适反应pH为4.5,内切菊粉酶为pH5.0;Ag+完全抑制两种酶的活性,Fe2+和Al3+对两种酶有较强的抑制作用,尤其是外切菊粉酶,Mg2+对两种酶有激活作用;实验还对两种酶的动力学常数进行了测定和比较。

关键词: 外切菊粉酶, 内切菊粉酶, 酶学性质, Aspergillus ficuum

Abstract: Characteristics of two types of inulin-degrading enzymes from Aspergillus ficuum were studied. The optimum reaction temperature of endo- and exo-inulinase were around 45 ℃. The optimum reaction pH of endo-inulinase was 5.0, and that of exo-inulinase was 4.5. Both of them were stable within the pH range 4.0~8.0 and below the temperature 50 ℃. The metal ions had the different level influences on the purified enzymes. Endo-and exo-inulinase activities were completely inhibited by Ag+, and obviously by Fe2+ and Al3+, while Mg2+ had an activating effect. In addition the kinetic constants of the two enzymes were also studied.

Key words: exoinulinase, endoinulinase, characteristic, Aspergillus ficuum