The activity of asparaginase was evaluated at different values of pH and temperature under assay conditions and the
amount of ammonia liberated was determined. Fungal mycelium was separated by filtration crude enzyme was
collected from broth and used for further purification process. Asparaginase yield increased with increase in initial
pH of the medium and thereafter it decreased and enzyme activity was stable at wide array temperature ranging from
400C to 600C. It is suppose that changes in optimum pH and temperature of asparaginase may caused by the charge
of a water-insoluble carrier, a chemical alteration of the enzyme, or some of the enzymatic reactions.
Purification of asparaginase was carried out by four steps as mentioned in methodology, fractioned collected from
Sephadex G50 column were analyzed for asparaginase activity and protein content. Asparaginase Production was
studied in some fungi such as Aspergillus tamarii and Aspergillus terreus these fungi were grown in different
medium having different sources of nitrogen and it was found that A. terreus showed the highest asparaginase
activity (58 U/L) with 2% proline medium [11].
In present study, asparaginase activity found as 1.304 units/ml by Eurotium Sp. from rhizomes of C.longa, which is
less as compared to 3.71 IU/ml by endophytic Fusarium sp. KLIVRb9-1 from Thai medicinal plant [12]. This may
be due to inappropriate culture conditions, needs or ability of microbe for enzyme production. Some endophytes like