91桃色

Abstract

L-asparaginase is a chemotherapeutic enzyme that catalyzes the conversion of L-asparagine to L-aspartate and ammonia. The important application of the L-asparaginase enzyme is in the treatment of acute lymphoblastic leukemia, Hodgkin disease, acute myelocytic leukemia, chronic lymphocytic leukemia, lymphosarcoma treatment, reticulosarcoma and melanosarcoma. L-asparaginase is widely distributed among prokaryotes and eukaryotes and since the large amount of this enzyme drug has been needed for pharmacological and clinical tests, microbial sources are found to be best for the bulk production of L-asparaginase. In the present study, the L-asparaginase from Erwinia carotovora MTCC 1428 was purified and used for the killing of Hep-2C cell line. Sonication of the resting cells was carried out to release the intracellular L-asparaginase and cell free extract was subjected to acid precipitation. Sulphopropyl Sephadex was used for further purification of enzyme. The 24% yield of the L-asparaginase was obtained after single step purification. The specific activity of the purified enzyme was found to be 0.37 IU/mg and the electrophoresis results suggest that the L-asparaginase of E. carotovora MTCC 1428 exists in the form of dimmer of dimmers. Moreover, the purified L-asparaginase from E. carotovora MTCC 1428 devoid of glutaminase activity. The L-asparaginase purified from E. carotovora MTCC 1428 showed better in vitro toxicity on Hep-2C cell lines (84% survival) in comparison to commercial L-asparaginase preparation (90% survival) obtained from E. coli.

Biography

Sarita Devi has completed her PhD in the year 2012 at the age of 29 years from Himachal Pradesh University. She has published many papers in the journals on international repute.