Purification and characterization of catalase from chard (Beta vulgaris var. cicla)

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dc.contributor.authorDinçer A.
dc.contributor.authorAydemir T.
dc.date.accessioned2024-07-22T08:25:30Z
dc.date.available2024-07-22T08:25:30Z
dc.date.issued2001
dc.description.abstractCatalase is a major primary antioxidant defence component that primarily catalyses the decomposition of H2O2 to H2O. Here we report the purification and characterization of catalase from chard (Beta vulgaris var. cicla). Following a procedure that involved chloroform treatment, ammonium sulfate precipitation and three chromatographic steps (CM-cellulose, Sephadex G-25, and Sephadex G-200), catalase was purified about 250-fold to a final specific activity of 56947 U/mg of protein. The molecular weight of the purified catalase and its subunit were determined to be 235 000 and 58 500 daltons, indicating that the chard catalase is a tetramer. The absorption spectra showed a soret peak at 406 nm, and there was slightly reduction by dithionite. The ratio of absorption at 406 and 275 nanometers was 1.5, the value being similar to that obtained for catalase from other plant sources. In the catalytic reaction, the apparent Km value for chard catalase was 50 mM. The purified protein has a broad pH optimum for catalase activity between 6.0 and 8.0. The enzyme had an optimum reaction temperature at 30°C. Heme catalase inhibitors, such as azide and cyanide, inhibited the enzyme activity markedly and the enzyme was also inactivated by β-mercaptoethanol, dithiothreitol and iodoacetamide.
dc.identifier.DOI-ID10.1080/14756360109162366
dc.identifier.issn87555093
dc.identifier.urihttp://akademikarsiv.cbu.edu.tr:4000/handle/123456789/20458
dc.language.isoEnglish
dc.publisherHarwood Academic Publishers GmbH
dc.subjectBeta vulgaris
dc.subjectBeta vulgaris
dc.subjectBeta vulgaris cicla
dc.subjectLabrus
dc.subjectammonium sulfate
dc.subjectantioxidant
dc.subjectazide
dc.subjectcatalase
dc.subjectchloroform
dc.subjectcyanide
dc.subjectdithionite
dc.subjectdithiothreitol
dc.subjecthydrogen peroxide
dc.subjectiodoacetamide
dc.subjectmercaptoethanol
dc.subjectsephadex
dc.subjectwater
dc.subjectabsorption spectroscopy
dc.subjectarticle
dc.subjectbeet
dc.subjectcatalysis
dc.subjectchard
dc.subjectchemical procedures
dc.subjectchromatography
dc.subjectdecomposition
dc.subjectenzyme activity
dc.subjectenzyme analysis
dc.subjectenzyme inactivation
dc.subjectenzyme purification
dc.subjectenzyme subunit
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectpH
dc.subjectplant
dc.subjectprecipitation
dc.subjectpriority journal
dc.subjecttemperature
dc.titlePurification and characterization of catalase from chard (Beta vulgaris var. cicla)
dc.typeArticle

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