Immobilization of Amaranthus leaf oxalate oxidase on alkylamine glass.

dc.contributor.authorPundir, C Sen_US
dc.contributor.authorGoyal, Len_US
dc.contributor.authorThakur, Men_US
dc.contributor.authorBhargava, A Ken_US
dc.date.accessioned1999-12-09en_US
dc.date.accessioned2009-05-27T09:28:08Z
dc.date.available1999-12-09en_US
dc.date.available2009-05-27T09:28:08Z
dc.date.issued1999-12-09en_US
dc.description.abstractA membrane bound oxalate oxidase from leaves of Amaranthus spionsus has been partially purified and immobilized on alkylamine glass with a yield of 9.2 mg protein/g support. The enzyme retained 99.4% of initial activity of free enzyme after immobilization. There was no change in the optimum pH (3.5) and Vmax but the temperature for maximum activity was slightly decreased (35 degrees C) and energy of activation (Ea) and Km for oxalate were increased after immobilization. The immobilized enzyme preparation was stable for 6 months, when stored in distilled water at 4 degrees C. Presence of Cl- did not affect the activity of immobilized enzyme.en_US
dc.description.affiliationDepartment of Bio-Sciences, Maharshi Dayanand University, Haryana, India. mdu@mdul.ernet.inen_US
dc.identifier.citationPundir CS, Goyal L, Thakur M, Bhargava AK. Immobilization of Amaranthus leaf oxalate oxidase on alkylamine glass. Indian Journal of Biochemistry & Biophysics. 1999 Dec; 36(6): 449-52en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/27598
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshAdulten_US
dc.subject.meshAmines --chemistryen_US
dc.subject.meshEnzymes, Immobilized --chemistryen_US
dc.subject.meshHumansen_US
dc.subject.meshMaleen_US
dc.subject.meshOxidoreductases --chemistryen_US
dc.subject.meshPlant Leaves --enzymologyen_US
dc.titleImmobilization of Amaranthus leaf oxalate oxidase on alkylamine glass.en_US
dc.typeJournal Articleen_US
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