• Journal of Microbiology
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• v.45 no.3
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• pp.213-218
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• 2007

Trametes versicolor has a lignin degrading enzyme system, which is also involved in the degradation of diverse recalcitrant compounds. Manganese-dependent peroxidase (MnP) is one of the lignin degrading enzymes in T. versicolor. In this study, a cDNA clone of a putative MnP-coding gene was cloned and transferred into an expression vector (pBARGPE1) carrying a phosphinothricin resistance gene (bar) as a selectable marker to yield the expression vector, pBARTvMnP2. Transformants were generated through genetic transformation using pBARTvMnP2. The genomic integration of the MnP clone was confirmed by PCR with bar-specific primers. One transformant showed higher enzyme activity than the recipient strain did, and was genetically stable even after 10 consecutive transfers on non-selective medium.

• Proceedings of the Korean Biophysical Society Conference
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• 1999.06a
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• pp.44-44
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• 1999

Yeast cytochrome c peroxidase (CcP) was cloned and overexpressed in E. coli, and purified by a Ni$^{2＋}$-affinity column. HoloCcP was obtained by reconstituting apoCcP with Mn$^{3+}$-protoporphyrin IX (MnPP). Electron paramagnetic resonance (EPR) spectra of spin-labeled holoCcP showed a slightly more immobilized signal than spin-labeled apoCcP.(omitted)

• Korean Journal of Microbiology
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• v.36 no.3
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• pp.228-235
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• 2000

Until now, it was diIliculi to overproduce lignin peroxidase(LiP) fiom Pl~anemchaete ch~ysosporium since the lack of optimized growth conditions. In this paper, we optimized the LIP production conditions and monitored LIP isozyines of fl chqsospoi.ium PSBL-1. The optimized condition includes sponge matrix support, no addition of $MnSO_4$, excess addition of niixogen source(48 inM diarmnonium), and addition of stabilizer(2 mM verakyl alcohol). Finally we obtained Lip activity of 1,800 unitsll. HI isozyne was overproduced when inyceliuin was cultivated in media containing $Mn^{2+}$ (2.73 inM) and excess nitrogen(48 11d4 diannnonium). Three azo dyes(acid yellow 9, congo ued, orange IT; each concenimtion of50 $\mu$M) we1-e rapidly decolorized within 2 inins by 0.4 un~t or Lip.

• Journal of Microbiology
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• v.42 no.1
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• pp.37-41
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• 2004

The textile industry wastewater has been decolorized efficiently by the white rot fungus, Irpex lacteus, without adding any chemicals. The degree of the decolorization of the dye effluent by shaking or stationary cultures is 59 and 93%, respectively, on the 8th day. The higher level of manganese-dependent peroxidase (MnP) and non-specific peroxidase (NsP) was detected in stationary cultures than in the cultures shaken. Laccase activities were equivalent in both cultures and its level was not affected significantly by the culture duration. Neither lignin peroxidase (LiP) nor Remazol Brilliant Blue R oxidase (RBBR ox) was detected in both cultures. The absorbance of the dye effluent was significantly decreased by the stationary culture filtrate of 7 days in the absence of Mn (II) and veratryl alcohol. In the stationary culture filtrate, three or more additional peroxidase bands were detected by the zymogram analysis.

• Journal of Microbiology and Biotechnology
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• v.16 no.2
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• pp.226-231
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• 2006

Several white-rot fungi are able to produce extracellular lignin-degrading enzymes such as manganese peroxidase (MnP), lignin peroxidase (LiP), and laccase. In order to enhance the production of laccase and MnP using Trametes versicolor KCTC 16781 in suspension culture, the effects of major medium ingredients, such as carbon and nitrogen sources, on the production of the enzymes were investigated. The decolorization mechanism in terms of biodegradation and biosorption was also investigated. Among the carbon sources used, glucose showed the highest potential for the production of laccase and MnP. Ammonium tartrate was a good nitrogen source for the enzyme production. No significant difference in the laccase production was observed, when glucose concentration was varied between 5 g/l and 30 g/l. As the concentration of nitrogen source increased, a lower MnP activity was observed. The optimal C/N ratio was 25 for the production of laccase and MnP. When the concentrations of glucose and ammonium tartrate were simultaneously increased, the laccase and MnP activities increased dramatically. The maximum laccase and MnP activities were 33.7 U/ml at 72 h and 475 U/ml at 96 h, respectively, in the optimal condition. In this condition, over 90% decolorization efficiency was observed.

• Bulletin of the Korean Chemical Society
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• v.31 no.11
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• pp.3173-3179
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• 2010

New complex $[Mn(II)H_{1.5}L]_2[Mn(II)H_3L]_2(ClO_4)_5{\cdot}3H_2O$ (1), where $H_3L$ is tris {2-(4-imidazolyl)methyliminoethyl} amine (imtren), has been prepared by reacting manganese(II) perchlorate hexahydrate with the imtren ligand in methanol. X-ray crystallographic study revealed that the imtren ligand hexadentately binds to Mn(II) ion through the three Schiff-base imine N atoms and three imidazole N atoms with a distorted octahedral geometry, and the apical tertiary amine N atom of the ligand pseudo-coordinates to Mn(II), forming overall a pseudo-seven coordination environment. The hydrogen-bonds between imidazole and imidazolate of $[Mn(II)H_{1.5}L]^{0.5+}$ complex ions are extended to build a 2D puckered network with trigonal voids. $[Mn(II)H_3L]^{2+}$ complex ions constitutes another extended 2D puckered layer without hydrogen bonds. Two layers are wedged each other to constitute overall stack of the crystal. Peroxidase activity of complex 1 was examined by observing the oxidation of 2,2'-azinobis(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) with hydrogen peroxide in the presence of complex 1. Generation of $ABTS^{+{\cdot}}$ was observed by UV-vis and EPR spectroscopies, indicating that the complex 1, a fully-coordinated mononuclear Mn(II) complex with nitrogen-only ligand, has a heme-independent peroxidase activity.

• Proceedings of the Korea Society of Poultry Science Conference
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• 2005.11a
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• pp.78-79
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• 2005

Effects of dietary lactose or killed Salmonella on the performance, immune response and anti-oxidant system was studied in chicks innoculated with Salmonella typhimurium. In 27 days of age broiler, dietary lactose decreased performance, while dietary lactose and killed Salmonella elevated plasma peroxidase activity and IL-1 level in supernatant of PBMC stimulated with LPS. When broiler chicks innoculated with Salmonella, performance, activities of erythrocyte MnSOD and plasma peroxidase were enhanced after 7 days of the innoculation. Dietary lactose and killed Salmonella increased activity of erythrocyte MnSOD, plasma peroxidase, proliferation of PBMC stimulated with LPS and IL-1 level in the supernatant after 15 days of the innoculation. The result indicated that dietary lactose and killed Salmonella have modulated innate immune response and antioxidant system in broiler chicks innoculated with Salmonella typhimurium.

• Proceedings of the Korea Society of Poultry Science Conference
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• 2006.11a
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• pp.60-61
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• 2006

Effect of dietary salmonella lysate in broiler chicks inoculated with Salmonella typhimurium on the antioxidant system(freshness) of broiler meats during 4$^{\circ}$C refrigeration was investigated. In Pectoral and leg muscle, regardless experimental diets, as the refrigeration day passed, CuZnSOD activity decreased gradually, while at 7d MnSOD activity and peroxide level raised and then lowered at 14d. MnSOD and peroxidase activity, however, had differed according to experimental diets. The results indicated that antioxidant system of broiler meats will be changed according to experimental diets(nutrients). As the CuZnSOD, MnSOD and peroxidase activity are responsible for proteolysis of muscle protein, it was concluded that change of antioxidant system during 4$^{\circ}$C storage explain the biological activity(freshness) of broiler meats.

• Journal of Microbiology
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• v.43 no.6
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• pp.503-509
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• 2005

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 $40^{\circ}C$. The enzyme efficiently catalyzed the decolorization of various artificial dyes and oxidized Mn (II) to Mn (III) in the presence of $H_2O_2$. 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.

• Journal of Microbiology and Biotechnology
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• v.32 no.2
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• pp.248-255
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• 2022

Phlebia sp. MG-60 is the salt-tolerant, white-rot fungus which was isolated from a mangrove forest. This fungus expresses three kinds of manganese peroxidase (MGMnP) isozymes, MGMnP1, MGMnP2 and MGMnP3 in low nitrogen medium (LNM) or LNM containing NaCl. To date, there have been no reports on the biochemical salt-tolerance of these MnP isozymes due to the difficulty of purification. In present study, we established forced expression transformants of these three types of MnP isozymes. In addition, the fact that this fungus hardly produces native MnP in a high-nitrogen medium (HNM) was used to perform isozyme-selective expression and simple purification in HNM. The resulting MGMnPs showed high tolerance for NaCl compared with the MnP of Phanerochaete chrysosporium. It was worth noting that high concentration of NaCl (over 200 mM to 1200 mM) can enhance the activity of MGMnP1. Additionally, MGMnP1 showed relatively high thermo tolerance compared with other isozymes. MGMnPs may have evolved to adapt to chloride-rich environments, mangrove forest.