Abstract
Lignin peroxidase from the culture filtrate of Lenzitus betulina MTCC-1183 has been purified to homogeneity using concentration by ultrafiltration and anion exchange chromatography on DEAE cellulose. The molecular weight of the purified lignin peroxidase using SDS-PAGE analysis was 43 kDa. Specific activity of the enzyme was 29.58 IU/mg. The K m values for veratryl alcohol and H2O2 for the purified enzyme were 54 and 81 μM, respectively. The k cat value of the purified enzyme was 2.3 s−1 using 3,4-dimethoxybenzyl alcohol as the substrate. The optimal conditions for the lignin peroxidase assay were detected at pH 2.4 and 22°C. Thermal stability of the purified enzyme has also been studied and its activation energy for deactivation was 287 kJ/mol. The purified lignin peroxidase depolymerised humic acid in presence of H2O2. Depolymerisation of coal by the L. betulina MTCC-1183 has been demonstrated using humic acid as a model of coal.
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Published in Russian in Prikladnaya Biokhimiya i Mikrobiologiya, 2012, Vol. 48, No. 6, pp. 646–652.
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Yadav, M., Singh, S.K. & Yadava, S. Purification, characterisation and coal depolymerisation activity of lignin peroxidase from Lenzitus betulina MTCC-1183. Appl Biochem Microbiol 48, 583–589 (2012). https://doi.org/10.1134/S0003683812050146
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DOI: https://doi.org/10.1134/S0003683812050146