Abstract
The intracellular enzyme, L-asparaginase, from aerobically grown Erwinia aroideae NRRL B-138 has been purified and some of its properties studied. Sonic treatment permitted recovery of 95% of L-asparaginase from cells. The crude cell lysate was purified 167-fold by means of ammonium sulfate fractionation and column chromatography on hydroxylapatite–cellulose, and DEAE–Sephadex. The specific activity of the most active fraction of L-asparaginase is 256 IU/mg protein. The enzyme has a broad pH activity profile with maximum at pH 9.0–9.5. The optimum temperature for enzyme reaction was determined to be 41 °C. The apparent activation energy is 11 000 cal/mole. The molecular weight of L-asparaginase was estimated by gel filtration to be 108 000.
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