The properties of catalase, obtained by DEAE-Sephadex chromatography and gel filtration on Sephadex G-200 from a methanol-utilizing yeast, Candida N-16, are examined. Catalase activity was assayed by measuring a change of absorbance at 240 nm based on the decomposition of H2O2. The reaction mixture contained an enzyme preparation and 100 .mu.mol of phosphate buffer, pH 7.3, in a total volume of 3 ml. Incubation was carried out at 25.degree. C; protein was determined by the method of Lowry et al., using bovine serum albumin. Properties were similar to those previously reported for baker''s yeast.