Coal Depolymerising Activity and Haloperoxidase Activity of Mn Peroxidase from Fomes durissimus MTCC-1173
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...
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| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Wiley
2011-01-01
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| Series: | Bioinorganic Chemistry and Applications |
| Online Access: | http://dx.doi.org/10.1155/2011/260802 |
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| Summary: | 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. |
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| ISSN: | 1565-3633 1687-479X |