Study of physicochemical and kinetics features of peroxidase isolated fromhoary cress (Cardaria draba L.)

New peroxidase may be versatile was investigated in different parts of hoary cress. Roots regarded as a rich source of enzyme (2095.23 U mg-1) comparison in other botanical parts. Peroxidase was purified from roots by ammonium sulfate, dialysis and Sephadex G-100 gel filtration, showed final degree of purity and recovery 2.70 and 45.11% respectively. Molecular mass, optimum of pH, temperature and time of enzymatic reaction were 56.234 kDa, 6.5, 40oC, 3 min. respectively. Km and Vmax were estimated of each substrate (guaiacol and hydrogen peroxide), noticed high affinity to hydrogen peroxide. Competitive sodium azide inhibitor was suppressed peroxidase totally at 90 mM.