Abstract
l-asparaginase (EC 3.5.1.1) is an important antineoplastic agent, used in the acute lymphoblastic leukemia chemotherapy and well known as food processing aid for reducing the acrylamide formation in starch rich foods. In the present study, we have cloned, expressed and purified recombinant l-asparaginase II of Erwinia carotovora subsp. atroseptica SCRI 1043 in E. coli. To study the best condition for performance of recombinant enzymes, pH and temperature of process conditions were optimized using response surface methodology. Optimal pH and temperature for enzyme were found to be 7.79 and 47.21 °C. Furthermore, the purified recombinant enzyme was subjected to thermal deactivation studies. pH and thermal stability of enzyme was studied at various combinations of pH and temperature. In addition, thermodynamic parameters of recombinant l-asparaginase II were evaluated. It was observed that recombinant l-asparaginase II enzyme is more stable at pH 8.5 at 35 °C relatively pH 6.5, 7.5 and 9.5. It was also observed that recombinant l-asparaginase II is more stable at pH 8.5 than pH 9.6 and 7.6 at higher temperature.
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