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L-asparaginase has been used for the treatment of different leukemia such as Acute Lymphoblastic Leukemia. Unlike normal cells leukemic cells cannot synthesize asparagine on their own. Therefore, when L-asparaginase is injected into blood it breaks down asparagine to aspartic acid and ammonia and hence tumor cells die due to asparagine starvation. It is produced by both microbes as well as plants. Therefore, in the present study we compared the L-asparaginase extracted from plants as well as microbes. Among the plants S. nigrum showed the highest activity (52 IU/ml) whereas among microbes B. subtilis (MTCC-121) had the highest activity (43.11 IU/ml). Both the enzymes were kinetically characterized and it was found that plant enzyme was stable over pH and temperature variations. The effect of metal ions was same on both the enzymes whereas chelators enhanced the plant enzyme whereas had no effect on microbial enzyme. Plant enzyme showed the highest activity and was more stable to the environmental variations as compared to microbial enzyme.