Investigating promiscuous organic reactions performed by recombinant L-Asparaginase II.

L-asparaginase II has played important role for ۴۰ years to treat cancer in a person who has juvenile leukemias or lymphomas. Furthermore, the enzyme has become important in food industries and biosensors thechnology. The main goal of this work is to study asparaginase promiscuity in two different contexts, substrate promiscuity and catalytic reaction promiscuity. To achieve this goal we carried out different chemical reactions with asparaginase as biocatalyst and dock different substrates to asparaginase structure via computional analysis. In this way, the induction of recombinant asparaginase experssion in E.Coli , purification of this enzyme from growth culcture, and investigation of kinetic parameters were evaluated and the efficiency of recombinant asparaginase is reported to be ۳.۹×۱۰-۲ mM-۱.min-۱.