Purification and properties of the β‐fructofuranosidase from Kluyveromyces fragilis

FEBS Letters

Workman, Wesley E.²  Day, Donal F.¹ 

[1] Audubon Sugar Institute, Louisiana State University, Baton Rouge, LA 70803, USA;Dept. of Microbiology, Louisiana State University, Baton Rouge, LA 70803 USA

关键词: β-Fructofuranosidase;    Invertase;    Inulinase;    2;    5-Anhydro-D-mannitol;   

DOI  :  10.1016/0014-5793(83)80927-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The β-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°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.

【 授权许可】

Unknown