Abstract
With the crystalline preparation of alcohol oxidase of Kloeckera sp. No. 2201 grown on methanol as a sole carbon source, some properties of the enzyme were investigated. The visible absorption spectrum showed maxima at 373mμ, 392mμ and 461mμ, t which were bleached by an addition of substrate and were restored by oxygenation. The prosthetic group was identified to be FAD. The enzyme was unstable in acidic pH and higher temperature. The optima of pH and temperature for enzyme activity were pH 8.0 and 35°C, respectively. The Km values were 1.25×10-3M for methanol and 2.5×10-3M for ethanol. The enzyme oxidized lower primary alcohols to the corresponding aldehydes and hydrogen peroxide.
