Workman W E, Day D F
FEBS Lett. 1983 Aug 22;160(1-2):16-20. doi: 10.1016/0014-5793(83)80927-2.
The beta-fructofuranosidase from Kluyveromyces fragilis was purified to one band on electrophoresis by 3 different methods. Two of the preparations were found to be impure by isoelectric focusing. This demonstrates the need for more than one criteria of homogeneity when purifying this enzyme. The enzyme was found to be a glycoprotein, stable at 50 degrees C, with a pH optimum of 4.5. The cations Hg2+, Ag+, Cu2+ and Cd2+ exhibited a marked inhibition of the enzyme. Competitive inhibition was observed with the fructose analog 2,5-anhydro-D-mannitol suggesting that the enzyme is inhibited by the furanose form of fructose.
来自脆壁克鲁维酵母的β-呋喃果糖苷酶通过3种不同方法纯化至电泳呈现单一条带。通过等电聚焦发现其中两种制剂不纯。这表明在纯化该酶时需要不止一种均一性标准。该酶被发现是一种糖蛋白，在50℃稳定，最适pH为4.5。阳离子Hg2+、Ag+、Cu2+和Cd2+对该酶表现出显著抑制作用。观察到果糖类似物2,5-脱水-D-甘露糖醇存在竞争性抑制，表明该酶被果糖的呋喃糖形式所抑制。
