Yarrowia lipolytica, a species of yeast, produced extracellular lipases, when it was grown in liquid media containing both olive oil and casein. The major part of the extracellular lipases, termed Lipase A, was purified and showed a sigle band with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weight and sugar content of Lipase A were estimated to be 39,000 and 10% as mannose, respectively. The amino acid sequence of the N-terrninal was demonstrated to be VYTSTET(A)XIDDE(A)YXFF-. These data are similar to those of Lipase I, one of the cell-bound lipases, which was produced by the same yeast with the media containing olive oil, but casein being omitted; however, Lipase A is considered to be different from Lipase I, because Lipase A contained significantly a less amount of hydrophobic amino acids than Lipase I.