PURIFICATION AND CHARACTERIZATION OF A GLYCEROL OXIDASE FROM PENICILLIUM SP. TS-622

A novel extracellular glycerol oxidase was purified 39-fold from wheat bran culture of a soil-isolated Penicillium strain TS-622 with an ove rall yield of 3%. The addition of Triton X-100 into the extraction buf fer improved the extraction yield by 90 times, indicating that the enz yme is bound to the cell surface. The molecular weight of this enzyme was 400,000 as determined by size-exclusion high-performance liquid ch romatography. The optimum pH was from 6 to 7 and the optimum temperatu re was 45 degrees C. This enzyme showed high specificity toward dihydr oxyacetone and glycerol. It was inhibited by KCN, NaN3, and hydroxylam ine.