عزل ودراسة خواص انزيم البيروكسيديز من نبات اللهانة المحلي ( Brassica oleracea Var. capitate L.)

Abstract

The research was conducted by isolation of peroxidase from cabbage (Brassica oleracea Var. capitate L) using different biochemical techniques. It was shown that using gel filtration chromatography on sephadex G-75, the solution of proteinous precipitate produced by ammonium sulphate saturation contains two proteinous peaks. The first peak obtained maximum specific activity (24) folds of purification while the second peak obtained minimum specific activity Further more the comparative molecular weight of partially purified peroxidase (first proteinous peak) using gel filtration was found to be (40000+2000) Dalton. The research was also concerned with determination the optimum conditions of peroxidase as maximum activity was obtained by using sodium phosphate buffer (100mM) at PH(7.0) with optimum temperature (50)C,the incubation time was one minute and the[s] was (20)mM by using linweaver-Burk plot was found that the Vmax and Km have the values of (0.4) µmol /ml /min of proteinous solution and (11.0- 11.5)mM respectively The results also indicated that the activity of enzyme decreased gradually to 63% and 55% when the enzyme stored for (28) day at 4C and 30-35C respectively.