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KMID : 1007519940030040249
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Food Science and Biotechnology
1994 Volume.3 No. 4 p.249 ~ p.252
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Production and Characterization of Extracellular L-Asparaginase from Microorganism
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Kil, Ji-Oeun
Kim, Gi-Nahm/Park, Inshik
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Abstract
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L-Asparaginase (L-asparagine aminohydrolase, EC 3.5.1.1) from Cundidu utilis has been partially purified by ethanol precipitation (20-50%), Sephacryl S-200 gel filtration and DEAE ion exchange chromatography. The optimum temperature and pH of L-asparaginase from Caizdzda utilis were 55℃ and pH 10.5, respectively. The enzyme was extremely stable at wide pH ranges at room temperature. The activation energy of the enzyme was determined to be 3.1 ㎉/mole. The enzyme utilized L-asparagine and D-asparagine, whereas it hydrolyzed L-glutamine and D-glutamine poorly. The Michaelis-Menten constant (K_(??)) of the enzyme with L-asparagine as a substrate was identified as 0.67 mM. Among tested me tal ions , Cu^(++), Cr^(++), and Fe^(++) inhibited the enzyme activity.
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