| Title | Purification and Characterization of Manganese Peroxidase of the White-Rot Fungus Irpex lacteus |
|---|---|
| Author | Kwang-Soo Shin1,*, Young Hwan Kim2, and Jong-Soon Lim3 |
| Address | 1Department of Microbiology, Daejeon University, Daejeon 300-716, Republic of Korea, 2Proteome Analysis Team, Korea Basic Science Institute, Daejeon 305-806, Republic of Korea, 3College of Oriental Medicine, Daejeon University, Daejeon 300-716, Republic of Korea |
| Bibliography | Journal of Microbiology, 43(6),503-509, 2005, |
| DOI | |
| Key Words | decolorization, Irpex lacteus, manganese peroxidase, white-rot fungi |
| Abstract | The production of manganese peroxidase (MnP) by Irpex lacteus, purified to electrophoretic homogeneity by acetone precipitation, HiPrep Q and HiPrep Sephacryl S-200 chromatography, was shown to correlate with the decolorization of textile industry wastewater. The MnP was purified 11.0-fold, with an overall yield of 24.3%. The molecular mass of the native enzyme, as determined by gel filtration chromatography, was about 53 kDa. The enzyme was shown to have a molecular mass of 53.2 and 38.3 kDa on SDS-PAGE and MALDI-TOF mass spectrometry, respectively, and an isoelectric point of about 3.7. The enzyme was optimally active at pH 6.0 and between 30 and 40oC. The enzyme efficiently catalyzed the decolorization of various artificial dyes and oxidized Mn (II) to Mn (III) in the presence of H2O2. The absorption spectrum of the enzyme exhibited maxima at 407, 500, and 640 nm. The amino acid sequence of the three tryptic peptides was analyzed by ESI Q-TOF MS/MS spectrometry, and showed low similarity to those of the extracellular peroxidases of other white-rot basidiomycetes. |
| Download PDF | 503-509.pdf |