European Journal of Biotechnology and Bioscience

Authors
J. Archana rani, P. Raja rao

Abstract
L-asparaginases are anti-cancer agent used in the lymphoblastic leukemia chemotherapy. L-asparaginase is hydrolytic enzyme and is produced by a large number of microorganisms. In the present study, L-Asparaginase produced by Aspergillus nidulans isolated from a soil sample collected from Nallamala forest, India, was purified and characterized. The enzyme was purified by ammonium sulphate precipitation, dialysis, DEAE-cellulose ion-exchange chromatography and sephadex G-100 gel filtration. The molecular mass of the purified chitinase was estimated to be 46 kDa by SDS-PAGE. It was optimally active at pH of 6 and at 40 °C. The enzyme was stable from pH 5 to 8, and up to 50 °C. Among the metals that were tested, the Fe2+, Hg2+, Mn2+ and Co2+ completely inhibited the enzyme activity. The enzyme was less sensitive to Al3+, Ca2+, Cu2+, and Zn2+. The purified L-Asparaginase showed superoxide and hydrogen peroxide scavenging capacity which enables anticancer property.