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.

(a)

(b)