Coal Depolymerising Activity and Haloperoxidase Activity of Mn Peroxidase from Fomes durissimus MTCC-1173. (21st November 2011)

• Record Type: Journal Article
• Authors: Singh, Sunil Kumar; Yadav, Meera; Yadava, Sudha; Yadav, Kapil Deo Singh
• Other Names: Perlepes Spyros Academic Editor.
• Is Part Of: Bioinorganic chemistry and applications. Volume 2011(2011)
• Publication Date: 2011-11-21
• Subjects: Bioinorganic chemistry -- Periodicals; Bioinorganic chemistry; Biochemistry; Inorganic Chemistry; Chemistry, Bioinorganic; Periodicals; 572.51
• DOI: 10.1155/2011/260802
• Languages: English
• ISSNs: 1565-3633

Abstract

Abstract : 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. TheK m values using MnSO4 and H2 O2 as the variable substrates in 50 mM lactic acid-sodium lactate buffer pH 4.5 at30 ° C were 59 μ M and 32 μ M, respectively. The catalytic rate constants using MnSO4 and H2 O2 were 22.4 s −1 and 14.0 s −1, respectively, giving the values ofk cat / K m 0.38 μ M −1 s −1 and 0.44 μ M −1 s −1, respectively. The pH and temperature optima of the Mn peroxidase were 4 and26 ° C, respectively. The purified MnP depolymerises humic acid in presence of H2 O2 . The purified Mn peroxidase exhibits haloperoxidase activity at low pH.