Production, Purification and Characterization of a novel L-asparaginase from Acinetobacter baumannii with anticancerous activity

Abstract

L-asparaginase is an enzyme that catalyzes the conversion of L-asparagine to L-aspartate and ammonia. The important application of the L-asparaginase enzyme in using it as chemotherapeutic for its anticarcinogenic potential .In the present study a novel strain, AcinetobacterbaumanniiR7 was explored for the production of extracellular Lasparaginase .This enzyme was purified by single chromatography step to homogenicity with a recovery yield of 77% and 92.9 fold of purification by using isopropanol (1:2) and CM-Sephadex C-50 chromatography. The enzyme appeared as a single protein band on SDS-PAGE gel with a molecular mass corresponding to 160 kDa. The Purified enzyme does not possess any glutaminase activity. The Kmwas calculated as 22 mg/ml and Vmaxas 625 U/mg of protein using Lasparagine as substrate. L-asparaginase purified from AcinetobacterbaumanniiR7 at a concentration of 0.2 mg/ml showed better toxicity on OAW-42 cell line (59 and 51 % survival) for 24 and 48 h, respectively, in comparison with controls, and this result led to increase the benefit by using the enzyme for the treatment of human ovarian cancer.

Cite this paper

@inproceedings{Muslim2014ProductionPA, title={Production, Purification and Characterization of a novel L-asparaginase from Acinetobacter baumannii with anticancerous activity}, author={Sahira Nsayef Muslim}, year={2014} }