PURIFICATION AND PROPERTIES OF ALCOHOL OXIDASE FROM THE YEAST YARROWIA-LIPOLYTICA H-222

A soluble alcohol oxidase has been isolated and purified from Yarrowia lipolytica H-222 yeasts grown in the presence of n-alkanes. The enzyme exhibited maximal specificity for primary alcohols with chain length ranging from 10 to 18 carbon atoms. The purified preparation of the enzyme had an activity of 19.5 mu mo-les/min per mg protein and pI 5.5. The activity of the oxidase was optimal at pH 9.3. From analysis of the alcohol oxidase activities of the purified enzyme preparation and cell-free extracts of the yeast, we conclude that Y. lipolytica H-222 may contain several alcohol oxidases with distinct substrate specificity.