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

• Published in: Bioinorganic Chemistry and Applications Vol. 2011; no. 2011; pp. 168 - 175
• Main Authors: Yadav, Kapil Deo Singh, Yadava, Sudha, Yadav, Meera, Singh, Sunil Kumar
• Format: Journal Article
• Language: English
• Published: Cairo, Egypt Hindawi Limiteds 01-01-2011; Hindawi Puplishing Corporation; Hindawi Publishing Corporation; Hindawi Limited
• Subjects: Biochemistry; Bioinorganic chemistry; Fungal enzymes; Ion exchange chromatography; Peroxidase; الكيمياء; الكيمياء الحيوية; علم الأحياء
• ISSN: 1565-3633; 1687-479X
• DOI: 10.1155/2011/260802

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 Km values using MnSO4 and H2O2 as the variable substrates in 50 mM lactic acid-sodium lactate buffer pH 4.5 at 30°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 kcat/Km 0.38 μM−1s−1 and 0.44 μM−1s−1, respectively. The pH and temperature optima of the Mn peroxidase were 4 and 26°C, respectively. The purified MnP depolymerises humic acid in presence of H2O2. The purified Mn peroxidase exhibits haloperoxidase activity at low pH.