Purification and preliminary characterization of L-asparaginase from Erwinia aroideae NRRL B-138.

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dc.contributor.authorTiwari, Nen_US
dc.contributor.authorDua, R Den_US
dc.date.accessioned1996-10-01en_US
dc.date.accessioned2009-05-27T09:27:07Z
dc.date.available1996-10-01en_US
dc.date.available2009-05-27T09:27:07Z
dc.date.issued1996-10-01en_US
dc.description.abstractL-Asparaginase (L-asparagine amidohydrolase EC 3.5.1.1) from Erwinia aroideae NRRL B-138 has been purified to apparent homogeneity by ammonium sulphate precipitation, chromatography on sulfopropyl-sephadex C-50 and sephadex G-200 with 22% recovery and 567-fold purification. The enzyme obtained from sulfopropyl-sephadex C-50 was unstable and lost activity within a few hours. Addition of glycerol helped in restoring the activity of the enzyme. The enzyme has an apparent molecular mass of approximately 155 kDa and has four subunits of identical molecular mass of approximately 38 kDa. The K(m) for L-asparagine is 2.8 x 10(-3) M. Enzyme shows optimal activity at 45 degrees C and pH 8.2. Energy of activation as determined from Arrhenius plot was 9.1 kcal/mol. Substrate L-asparagine and analogue L-glutamine, D-asparagine and 6 diazo-5-oxo-L-norleucine provide full protection to the enzyme against thermal denaturation.en_US
dc.description.affiliationDepartment of Chemistry, Indian Institute of Technology, Hauz Khas, New Delhi.en_US
dc.identifier.citationTiwari N, Dua RD. Purification and preliminary characterization of L-asparaginase from Erwinia aroideae NRRL B-138. Indian Journal of Biochemistry & Biophysics. 1996 Oct; 33(5): 371-6en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/27548
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshAsparaginase --chemistryen_US
dc.subject.meshEnzyme Stabilityen_US
dc.subject.meshErwinia --enzymologyen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshKineticsen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshThermodynamicsen_US
dc.titlePurification and preliminary characterization of L-asparaginase from Erwinia aroideae NRRL B-138.en_US
dc.typeJournal Articleen_US
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