Aspergillus ficuum菊粉酶酶学性质的研究  

Characteristics of Exoinulinase and Endoinulinase from Aspergillus ficuum

作　　者：王静[1] 金征宇[2] 孙宝国[1] 曹雁平[1] 

机构地区：[1]北京工商大学化学与环境工程学院,北京100037 [2]江南大学食品学院,江苏无锡214122

出　　处：《食品科学》2008年第4期272-277,共6页Food Science

基　　金：国家自然科学基金项目(20376029);教育部科学技术研究重点项目(104258);北京市优秀人才培养资助项目(20071D0500300141)

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,Fe^2+和Al^3+对两种酶有较强的抑制作用,尤其是外切菊粉酶,Mg^2+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。Characteristics of two types of inulin-degrading enzymes from Aspergillusficuum 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 Fe^2＋ and Al^3＋, while Mg^2＋ had an activating effect. In addition the kinetic constants of the two enzymes were also studied.

关 键 词：外切菊粉酶 内切菊粉酶 酶学性质 ASPERGILLUS ficuum 

分 类 号：TS201.2[轻工技术与工程—食品科学]