Production and purification of choline oxidase from Cylindrocarpon didymum M-1.

The distribution of choline oxidase activity was studied with cell-free extracts of yeasts, molds and actinomycetes.A fungus which was identified as Cylindrocarpon didymum M-1 showed the highest activity.The enzyme was purified from the cell-free extract of C. didymum M-1 by a procedure involving ammonium sulfate fractionation and DEAE-cellulose, hydroxyl apatite and Sephadex G-150 column chromatographies.The enzyme preparation was homo geneous when subjected to disc gel electrophoresis and ultracentrifugation.Sedimentation velocity yielded a value of s020,w =7.6 S. The enzyme showed a typical flavoprotein spectrum of absorption maxima at 276,370 and 454 nm.