L-Asparaginase (E.C.3.5.1.1) is an important natural product that possesses a
broad spectrum of antitumor activity. In the present study, L-asparaginase partially
purified from local isolate of Escherichia coli that were grown aerobically for four
hours and anaerobically for 18hrs on M9 medium contain L-asparagine as sole
nitrogen source. Extraction of the enzyme was done by sonication. Qualitative and
quantitative assays for L-Asparaginase production were determined using
colorimetric and nesslerization methods respectively. The purification steps involve
dialysis of crude extract and DEAE-Cellulose Ion exchange chromatography. The
enzyme was purified 3.39-folds and showed a final specific activity of 0.18 U/mg
with a 41% yield. The crude extract and DEAE-Cellulose fractions showed slight
growth inhibition against RD cell line (human rhambdomyo sarcoma).