Partial Purification and Some Properties of Extracellular Asparaginase from Candida utilis

Abstract

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 abie 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. © 1977, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.