{"title":"High Efficiency, Selectivity against Cancer Cell Line of Purified L-Asparaginase from Pathogenic Escherichia coli","authors":"Hazim Saadoon Aljewari, Mohammed Ibraheem Nader, Abdul Hussain M. Alfaisal, NatthidaWeerapreeyakul, Sahapat","volume":41,"journal":"International Journal of Pharmacological and Pharmaceutical Sciences","pagesStart":199,"pagesEnd":205,"ISSN":"1307-6892","URL":"https:\/\/publications.waset.org\/pdf\/15807","abstract":"L-asparaginase was extracted from pathogenic\r\nEscherichia coli which was isolated from urinary tract infection\r\npatients. L-asparaginase was purified 96-fold by ultrafiltration, ion\r\nexchange and gel filtration giving 39.19% yield with final specific\r\nactivity of 178.57 IU\/mg. L-asparaginase showed 138,356\u00b11,000\r\nDalton molecular weight with 31024\u00b1100 Dalton molecular mass.\r\nKinetic properties of enzyme resulting 1.25\u00d710-5 mM Km and\r\n2.5\u00d710-3 M\/min Vmax. L-asparaginase showed a maximum activity\r\nat pH 7.5 when incubated at 37 \u00baC for 30 min and illustrated its full\r\nactivity (100%) after 15 min incubation at 20-37 \u00baC, while 70% of its\r\nactivity was lost when incubated at 60 \u00baC. L-asparaginase showed\r\ncytotoxicity to U937 cell line with IC50 0.5\u00b10.19 IU\/ml, and\r\nselectivity index (SI=7.6) about 8 time higher selectivity over the\r\nlymphocyte cells. Therefore, the local pathogenic E. coli strains may\r\nbe used as a source of high yield of L-asparaginase to produce anti\r\ncancer agent with high selectivity.","references":"[1] El-Bessoumy A A, Sarhan M, and Mansour J. Production, Isolation, and\r\nPurification of L-asparaginase from Pseudomonas aeruginosa 50071\r\nUsing Solid-state Fermentation. J Biochem Mol Biol. 2001;37:387-\r\n393.\r\n[2] Borek, D. and Jask\u251c\u00f4lski, M., Sequence analysis of enzymes with\r\nasparaginase activity. 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