Peroxidase was extracted from cabbage and was purified 13.14 fold by a three-step process of ammonium sulphate precipitation, dialysis, and gel filtration with a yield of 9.44. The partially purified peroxidase had maximal activity at pH 5.0 and temperature 45˚C. Michaelis constant (Km) and Maximum velocity (Vmax) obtained from Lineweaver-Burk plot of initial velocity data at different concentrations of H2O2 and O-dianisidine were 3.68Mm/ 37.04U and 9.89mM/ 28.57U, respectively. The partially purified peroxidase from cabbage decolorized many synthetic Azo and Vat dyes, with Azo tryptan blue having highest decolorization of 88.62% while vat orange II showed 12% decolorization, after contact time of one hour. This suggests that peroxidase from cabbage has the potential to decolorize synthetic dyes.
