Purification and Characterization of Peroxidase from Brassica oleracea var. Acephala
Corresponding Author(s) : Lhami Gulcin
Asian Journal of Chemistry,
Vol. 17 No. 4 (2005): Vol 17 Issue 4
Abstract
Peroxidase enzyme was extracted and purified from Brassica oleracea var. acephala through ammonium sulfate precipitation, dialysis and CM-Sephadex ion-exchange chromatography. The molecular weight of this enzyme was found to be 95 kDa by an SDS-PAGE electrophoresis. Optimum temperature, optimum pH and stable pH of this enzyme were found as 40°C, pH 7.5 and pH 6.5, respectively. The enzyme had KM values of 5.5 and 1 mM for guaiacol and H2O2, respectively. KM values for pyrogallol and H2O2 was found to be 1.92 and 1.25 mM. In contrast KM values, each of guaiacol/H2O2 and pyrogallol/H2O2 pairs were 5000 and 833.33 EU/mL, respectively.
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