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Purification and characterization of peroxidase from sweet gourd (Cucurbita moschata Lam. Poiret)Koksal, EkremBursal, ErcanAggul, Ahmet GokhanGulcin, IlhamiChromatographyElectrophoresisPeroxidasePurificationSweet gourdCitrullus colocynthisCucurbitaCucurbita moschataAmmonium compoundsEnzymesHydrogen peroxideIon exchangeIonic strengthAmmonium sulphateIon-exchange chromatographyOptimum pHOptimum temperatureOxidoreductasesSDS-PAGESubstrate patternTemperature conditionsPeroxidase (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.TAYLOR & FRANCIS INC2012Articlehttps://rdlopen.rawdatalibrary.net/r/ebyu/15890https://doi.org/10.1080/10942912.2010.5132161532-2386enInternational Journal of Food Propertiesinfo:eu-repo/semantics/openAccessinfo:eu-repo/semantics/articlehttps://ebyu-rdlopen.rawdatalibrary.net/tr/items/ebyu/15890