[Immobilization of Citrobacter L-asparaginase in polyacrylamide gel]

Bacterial L-asparaginase, immobilized on polyacrylamide gel, exhibited higher stability to denaturation and to the effect of a proteolytic enzyme. The immobilized enzyme exhibited the pH optimum of activity displaced by one pH unit to the acid side as compared with the free enzyme. The apparent Km value was approximately 200-fold higher as compared with the free L-asparaginase. The immobilized asparaginase hydrolyzed both L- and D-asparagine isomers but the free enzyme was highly stereospecific.