Extracellular Asparaginase from Candida utilis, Its Properties as Glycoprotein and Antitumor Activities

Abstract

Purified Candida asparaginase was proved to be homogeneous by gel filtration, ultracentrifugation and disc electrophoresis. The enzyme was found to have properties as glycoprotein containing mannose. The ratio of mannose to protein was 1 to 2 in purified enzyme. Specific activity was 5500 units per mg of protein. Isoelectric point was pH 4 to 4.5 and sedimentation coefficient was found to be about 8.2 S. Antitumor activity of Candida asparaginase was inferior to E. coli enzyme. It was thought as the reason why the Candida asparaginase had less affinity to L-asparagine and it was cleared faster from the blood than E. coli asparaginase.