PURIFICATION AND PROPERTIES OF PYRANOSE OXIDASE FROM BASIDIOMYCETOUS FUNGUS-52

Pyranose oxidase was purified from the crude extract of basidiomycetous fungus No. 52 about 74fold to a single protein band on polyacrylamide gel electrophoresis with an overall yield of 23 %. The molecular weight of the native enzyme was about 300,000 on gel filtration and 69,000 on SDSpolyacrylamide gel electrophoresis. Its isoelectric point was pH 6.3. The enzyme activity showed high stability over a wide pH range of 5.5-9.0 and below 50°C, and 60%of its initial activity remained even after heating at 70°C. The enzyme was inactivated by Ag +, Hg2+, and Cu2+. The enzyme contained FAD covalently bound to the protein and was a glycoprotein containing about 0.7% carbohydrate. © 1990 by the Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.