Purification, properties, and molecular features of glucose oxidase from Aspergillus niger.

摘要: Glucose oxidase [&-D-glucose: oxygen 1-oxidoreductase, EC 1. 3. 4] from Aspergillus niger was purified by DEAE-cellulose chromatography and Sephadex G-200 gel filtration using phosphate buffer, pH 7.0.1. The preparation has a specific activity of 172 μmoles consumed/min/mg enzyme at 30° 5.6, is essentially catalase-free. constituents the are protein (74.0±2.8%), neutral sugar (16. 4±0.3%), amino (2.4±0.5%), 2 moles iron per 160, 000 daltons, in addition to FAD.2. Optical data for newly holoenzyme show that ratio A280/A450 11.1, e enzyme-bound FAD 450nm 1.52×l04.3. (molecular weight, 000) consists two identical subunits with molecular weights 79, 000±4, 000, weight apoenzyme seems be subunit, as shown SDS-polyacrylamide electrophoresis on G-200.4. FHD (flavin-hypoxanthine dinucleotide) coenzymatic equal FAD.