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Purification and characterization of peroxidase from sweet gourd (Cucurbita moschata Lam. Poiret)

ArticleAçık Erişim

Özet

Peroxidase (EC 1.11.1.7; donor: hydrogen peroxide oxidoreductase) is an oxidoreductase enzyme found in many fruits and vegetables. This enzyme was purified from sweet gourd (Cucurbita moschata Lam. Poiret) by ammonium sulphate precipitation and CM-Sephadex ion-exchange chromatography. Furthermore, optimum pH, optimum temperature, optimum ionic strength, stable pH, and stable temperature conditions were determined as 7.2, 50°C, 0.4 M, 8.0, and 40°lC, respectively. The molecular weight (MW) of the enzyme was estimated to be 85 kDa by SDS-PAGE method. The values of Km and Vmax were calculated from the Lineweaver-Burk graph for guaiacol/H2O2 substrate patterns. © 2012 Copyright Taylor and Francis Group, LLC.

Anahtar Kelimeler

ChromatographyElectrophoresisPeroxidasePurificationSweet gourdCitrullus colocynthisCucurbitaCucurbita moschataAmmonium compoundsEnzymesHydrogen peroxideIon exchangeIonic strengthAmmonium sulphateIon-exchange chromatographyOptimum pHOptimum temperatureOxidoreductasesSDS-PAGESubstrate patternTemperature conditions
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Tam Kayıt
AlanDeğerDil
dc.contributor.authorKoksal, Ekrem
dc.contributor.authorBursal, Ercan
dc.contributor.authorAggul, Ahmet Gokhan
dc.contributor.authorGulcin, Ilhami
dc.date.accessioned2026-10-18T20:30:44.468769683Z
dc.date.available2026-10-18T20:30:44.468769683Z
dc.date.issued2012
dc.description.abstractPeroxidase (EC 1.11.1.7; donor: hydrogen peroxide oxidoreductase) is an oxidoreductase enzyme found in many fruits and vegetables. This enzyme was purified from sweet gourd (Cucurbita moschata Lam. Poiret) by ammonium sulphate precipitation and CM-Sephadex ion-exchange chromatography. Furthermore, optimum pH, optimum temperature, optimum ionic strength, stable pH, and stable temperature conditions were determined as 7.2, 50°C, 0.4 M, 8.0, and 40°lC, respectively. The molecular weight (MW) of the enzyme was estimated to be 85 kDa by SDS-PAGE method. The values of Km and Vmax were calculated from the Lineweaver-Burk graph for guaiacol/H2O2 substrate patterns. © 2012 Copyright Taylor and Francis Group, LLC.
dc.identifier.doi10.1080/10942912.2010.513216
dc.identifier.eissn1532-2386
dc.identifier.endpage1119
dc.identifier.issn1532-2386
dc.identifier.issue5
dc.identifier.scopus2-s2.0-84865511228
dc.identifier.startpage1110
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/ebyu/15890
dc.identifier.volume15
dc.identifier.wosWOS:000308025300015
dc.language.isoen
dc.publisherTAYLOR & FRANCIS INC
dc.relation.ispartofInternational Journal of Food Properties
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectChromatography
dc.subjectElectrophoresis
dc.subjectPeroxidase
dc.subjectPurification
dc.subjectSweet gourd
dc.subjectCitrullus colocynthis
dc.subjectCucurbita
dc.subjectCucurbita moschata
dc.subjectAmmonium compounds
dc.subjectEnzymes
dc.subjectHydrogen peroxide
dc.subjectIon exchange
dc.subjectIonic strength
dc.subjectAmmonium sulphate
dc.subjectIon-exchange chromatography
dc.subjectOptimum pH
dc.subjectOptimum temperature
dc.subjectOxidoreductases
dc.subjectSDS-PAGE
dc.subjectSubstrate pattern
dc.subjectTemperature conditions
dc.titlePurification and characterization of peroxidase from sweet gourd (Cucurbita moschata Lam. Poiret)
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus48
rdl.citation.wos46
rdl.oa.statusgreen
rdl.source.indexSCOPUS
rdl.source.indexWOS
rdl.wos.indexScience Citation Index Expanded (SCI-EXPANDED)