Partial Purification and Some Properties of Extracellular Asparaginase from Candida utilis

Extracellular asparaginase from Candida utilis was partially purified by precipitation with acetone and by column chromatography on DEAE Sephadex A-50 and Sephadex G-200. The specific activity of the enzyme preparation was 3900 units per mg of protein. Candida asparaginase characteristically had deaminating activity for d-asparagine as well as for l-asparagine. But this enzyme was not able to hydrolyzed l- or d-glutamine. SH inhibitor, chelating agents and metal ions did not show any inhibition or activation of l-asparaginase activity. Optimum pH was about 6 for both l- and d-asparagine. This asparaginase was stable between pH 4 and pH 10 in heating for 10 min at 50°C.