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Bioinorganic Chemistry and Applications
Volume 2011 (2011), Article ID 260802, 8 pages
Research Article

Coal Depolymerising Activity and Haloperoxidase Activity of Mn Peroxidase from Fomes durissimus MTCC-1173

Department of Chemistry, DDU Gorakhpur University, Gorakhpur 273009, India

Received 21 July 2011; Accepted 7 September 2011

Academic Editor: Spyros Perlepes

Copyright © 2011 Sunil Kumar Singh et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Mn peroxidase has been purified to homogeneity from the culture filtrate of a new fungal strain Fomes durissimus MTCC-1173 using concentration by ultrafiltration and anion exchange chromatography on diethylaminoethyl (DEAE) cellulose. The molecular mass of the purified enzyme has been found to be 42.0 kDa using SDS-PAGE analysis. The 𝐾 π‘š values using MnSO4 and H2O2 as the variable substrates in 50 mM lactic acid-sodium lactate buffer pH 4.5 at 3 0 ∘ C were 59 μM and 32 μM, respectively. The catalytic rate constants using MnSO4 and H2O2 were 22.4 s−1 and 14.0 s−1, respectively, giving the values of π‘˜ c a t / 𝐾 π‘š 0.38 μM−1s−1 and 0.44 μM−1s−1, respectively. The pH and temperature optima of the Mn peroxidase were 4 and 2 6 ∘ C , respectively. The purified MnP depolymerises humic acid in presence of H2O2. The purified Mn peroxidase exhibits haloperoxidase activity at low pH.