ISSN 1017-2548(Print)
ISSN 2234-8530(Online)
Volume 23, Number 3
JKCSEZ 23(3)
June 20, 1979 

A purification technique of glucose oxidase was developed. Using the gluconyl-ω-aminohexyl Sepharose affinity chromatography, it was partially purified 14.6 folds with 79.7% yield. With the combination of the affinity chromatography and Sepharose 6B gel filtration, the enzyme was purified 27.2 folds from the broth with 74.1% yield. The final purified preparation showed 90.83 U of glucose oxidase activity per mg of protein and a single band by 7% polyacrylamide gel electrophoresis. The absorption spectrum and substrate specificity of the enzyme were studied and the fianal preparation showed the optimal pH between 5.6 and 6.0, the optimal temperature at 40℃, 8.5 × 10-3 M of Km for D-glucose, and 3.43 kcal/mole of the activation energy.