Summary: Two enzymes that hydrolysed lactose were purified essentially to homogeneity from cell extracts of the oleaginous yeast . One enzyme of 120000 had properties typical of a β-galactosidase (EC It hydrolysed lactose, lactulose and nitrophenyl-β--galactosides. The enzyme required K or Rb for activity, and other monovalent cations tested were not effective. Enzyme activity was abolished by EDTA and stimulated by Mg, Mn and Ca. The β-galactosidase was induced by lactose, galactose, lactulose and lactobionic acid. The other enzyme, a β-glycosidase (EC of 52000 showed no ionic requirements and it hydrolysed lactose, nitrophenyl-β--galactosides, 4-nitrophenyl-β--glucoside, cellobiose, laminaribiose, laminaritriose and sophorose, but not gentiobiose, 4-nitrophenyl-β--mannoside or sucrose. This enzyme was induced by lactose, galactose and lactulose, and also by cellobiose.


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