Coal Depolymerising Activity and Haloperoxidase Activity of Mn Peroxidase from Fomes durissimus MTCC-1173
Figure 2
Michaelis-Menten and double reciprocal plots using (a) MnSO4 and H2O2 as the variable substrates, respectively. The reaction one mL contained “5 μg of the enzyme (specific activity 4 IU/mg) in 50 mM lactic acid-sodium lactate buffer pH 4.5 at 30°C”. In (a) H2O2 was fixed at 100 μM and in (b) MnSO4 was fixed at 100 μM for purified Mn peroxidase using MnSO4 as the variable substrate at the fixed 50 μM concentration of H2O2. Details given in Section 2.
