coal depolymerising activity and haloperoxidase activity of mn peroxidase from fomes durissimus mtcc-1173煤炭depolymerising活动和haloperoxidase锰过氧化物酶的活性从传染媒介durissimus mtcc - 1173.pdfVIP

Hindawi Publishing Corporation Bioinorganic Chemistry and Applications Volume 2011, Article ID 260802, 8 pages doi:10.1155/2011/260802 Research Article Coal Depolymerising Activity and Haloperoxidase Activity of Mn Peroxidase from Fomes durissimus MTCC-1173 Sunil Kumar Singh, Meera Yadav, Sudha Yadava, and Kapil Deo Singh Yadav Department of Chemistry, DDU Gorakhpur University, Gorakhpur 273009, India Correspondence should be addressed to Meera Yadav, drmeerayadav@rediff 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 SDSanalysis. The K values using MnSO and H O as the m 4 2 2 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 MnSO and H O were 22.4 s−1 and 14.0 s−1, respectively, giving the values of k /K 0.38 μM−1s−1 and 4 2 2 cat m −1 −1