Peroxidase from leaves of Spinach (Spinacia oleracea): Partial purification and some biochemical properties

ArticleAçık Erişim

Özet

In present study, it is aimed to purify peroxidase (EC 1.11.1.7; donor: Hydrogen peroxide oxidoreductase) from leaves of spinach and determine its some biochemical properties. Peroxidase is an oxidoreductase enzyme produced by a number of organisms. Spinach (Spinacia oleracea L.) is an edible flowering plant in the family of Amaranthaceae and is heavily consumed all over the world. Peroxidase enzyme was purified from Leaves of Spinach (Spinacia oleracea L.) by ammonium sulphate precipitation and CM-Sephadex ion-exchange chromatography. Km (Michaelis constant) and Vmax (The maximum velocity of an enzymatic reaction) values were calculated from the Lineweaver-Burk graph for catechol and guaiacol substrates and the substrate specificity of the enzyme was investigated. The results have shown that guaiacol is a better substrate from catechol for this enzyme. Furthermore, for the guaiacol substrate, optimum pH, optimum temperature, optimum ionic strength, stable pH, conditions were determined. © 2011 Asian Network for Scientific Information.

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RDL Kalıcı Bağlantı (PID)
https://rdlopen.rawdatalibrary.net/r/ebyu/15726Resmi atıflarda kullanılan kalıcı adres
DOI
https://doi.org/10.3923/ijp.2011.135.139Yayıncı resmi DOI adresi
Tam Kayıt
AlanDeğerDil
dc.contributor.authorKöksal, E.
dc.date.accessioned2026-10-18T20:30:34.475616200Z
dc.date.available2026-10-18T20:30:34.475616200Z
dc.date.issued2011
dc.description.abstractIn present study, it is aimed to purify peroxidase (EC 1.11.1.7; donor: Hydrogen peroxide oxidoreductase) from leaves of spinach and determine its some biochemical properties. Peroxidase is an oxidoreductase enzyme produced by a number of organisms. Spinach (Spinacia oleracea L.) is an edible flowering plant in the family of Amaranthaceae and is heavily consumed all over the world. Peroxidase enzyme was purified from Leaves of Spinach (Spinacia oleracea L.) by ammonium sulphate precipitation and CM-Sephadex ion-exchange chromatography. Km (Michaelis constant) and Vmax (The maximum velocity of an enzymatic reaction) values were calculated from the Lineweaver-Burk graph for catechol and guaiacol substrates and the substrate specificity of the enzyme was investigated. The results have shown that guaiacol is a better substrate from catechol for this enzyme. Furthermore, for the guaiacol substrate, optimum pH, optimum temperature, optimum ionic strength, stable pH, conditions were determined. © 2011 Asian Network for Scientific Information.
dc.identifier.doi10.3923/ijp.2011.135.139
dc.identifier.eissn1812-5700
dc.identifier.endpage139
dc.identifier.issn1811-7775
dc.identifier.issue1
dc.identifier.scopus2-s2.0-84856257070
dc.identifier.startpage135
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/ebyu/15726
dc.identifier.volume7
dc.identifier.wosWOS:000294651600019
dc.language.isoen
dc.publisherAsian Network for Scientific Information
dc.relation.ispartofInternational Journal of Pharmacology
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectCharacterization
dc.subjectChromatography
dc.subjectPeroxidase
dc.subjectPurification
dc.subjectSpinach leaves
dc.subjectSubstrate specificity
dc.titlePeroxidase from leaves of Spinach (Spinacia oleracea): Partial purification and some biochemical properties
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus27
rdl.citation.wos22
rdl.oa.statusopen
rdl.source.indexSCOPUS
rdl.source.indexWOS
rdl.wos.indexScience Citation Index Expanded (SCI-EXPANDED)