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L-asparaginase is one of the protein drugs for countering leukemia and lymphoma. A major challenge in the therapeutic potential of the enzyme is its immunogenicity, low-plasma half-life and glutaminase activity that are found to be the reasons for toxicities attributed to asparaginase therapy. For addressing these challenges, several research and developmental activities are going on throughout the world for an effective drug delivery for treatment of cancer. Hence there is an urgent need for the development of asparaginase with improved properties for efficient drug delivery. The strategies selected should be economically viable to ensure the availability of the drug at low cost. The current review addresses various strategies adopted for the production of asparaginase from different sources, approaches for increasing the therapeutic efficiency of the protein and new drug delivery systems for L-asparaginase., (Copyright © 2017. Published by Elsevier Ltd.)

Escherichia coli L-asparaginases have great significance in the treatment of leukemia. Consequently, there is considerable interest in engineering this enzyme for improving its stability. In this work, the effect of surface charge on the stability of the enzyme l-asparaginase II was studied by site-directed mutagenesis of the cloned ansB gene from Escherichia sp. Replacement of two positively charged residues (K139 and K207) on the surface loops with neutral and reverse charges resulted in altered thermo stability in designed variants. Neutral charge substitutions (K139A and K207A) retained greater tolerance and stability followed by negative charge substitutions (K139D and K207D) compared to control mutant K139R and wild enzyme. From the results, it was concluded that the optimization of surface charge contributed much to the thermal properties of proteins without affecting the structure., (Copyright © 2013 Elsevier Inc. All rights reserved.)