Purification and Biochemical Characterization of Peroxidase Isolated from White Cabbage (<i>Brassica Oleracea var. capitata f. alba)</i>

Abstract

Peroxidase enzyme was purified for the first time from white cabbage (Brassica oleracea var. capitata f. alba) in a single step using affinity chromatography and some biochemical characteristics of the purified enzyme were determined. The peroxidase was purified 24.7-fold with an overall recovery of 4.3% and a specific activity of 964.5. The molecular weight of the purified peroxidase was approximately 73.2 kDa as calculated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and it showed maximum activity at pH 6.5 and 30°C. For the guaiacol substrate, the KM and Vmax values were found as 3.19 mM and 0.2 EU/mL, respectively. Additionally, the IC50 and Ki values were determined as 0.517 and 0.994 ± 0.453 mM, respectively, for 4-aminobenzohydrazide. 4-amino benzohydrazide showed non-competitive inhibition.