Purification of robust l-asparaginase from capsicum annum and its therapeutic efficacy in leukemia

Medicinal plants used for the treatment of chronic diseases, have attracted the interest of scientists. L-Asparaginase is an extracellular enzyme with biomedical significance. The present article discusses the extraction, purification and characterization of L-asparaginase. Enzyme activity was estimated from Chillies (plant of Solanaceae family). Enzyme titer of 112 U/mL was attained from crude extract of Chillies (Capsicum annum) fruit while purified enzyme after gel filtration provided 61.99% yield, activity of 69.43 U/mL and specific activity of 234 U/mg. L-Asparaginase stability was envisaged at optimal pH of 8.6 in the presence of alkaline buffer. Optimal substrate concentration for L-Asparaginase activity was 200 mMoL. The efficacy of purified enzyme was tracked in vivo model. Normal healthy rats were used as control, which were compared with leukemic rats after treatment with enzyme L-Asparaginase. Eventually after treatment with enzyme extract provided best recovery in leukemic model due to high titer of L-Asparaginase, which bears high antineoplastic activity. It may be employed for chemotherapy in tumors such as acute lymphocytic leukemia.