Abstract
Olive oil hydrolyzing fraction (F-3) of Mucor lipase was separated into two fractions, F-3A and F-3B, by means of CM-Sephadex column chromatography. Both fractions were homogeneous and F-3A was crystallized. The pH optimum for olive oil hydrolysis of F-3A was at 9.0 and that of F-3B was at 8.0.
Chain specificities of the both enzymes were different with each other. Sedimentation coefficient (s20, w) of F-3A was 2.8 S and that of F-3B was 3.1S.
Molecular weights calculated from sedimentation equilibrium data were 25, 400 for F-3A and 29, 000 for F-3B.