• Journal of Microbiology and Biotechnology
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• v.27 no.1
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• pp.179-188
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• 2017

White-rot basidiomycetes are the organisms that decompose lignin most efficiently, and Trametes villosa is a promising species for ligninolytic enzyme production. There are several publications on T. villosa applications for lignin degradation regarding the expression and secretion of laccase and manganese peroxidase (MnP) but no reports on the identification and characterization of lignin peroxidase (LiP), a relevant enzyme for the efficient breakdown of lignin. The object of this study was to identify and partially characterize, for the first time, gDNA, mRNA, and the corresponding lignin peroxidase (TvLiP) protein from T. villosa strain CCMB561 from the Brazilian semiarid region. The presence of ligninolytic enzymes produced by this strain grown in inducer media was qualitatively and quantitatively analyzed by spectrophotometry, qPCR, and dye fading using Remazol Brilliant Blue R. The spectrophotometric analysis showed that LiP activity was higher than that of MnP. The greatest LiP expression as measured by qPCR occurred on the $7^{th}$ day, and the ABSA medium (agar, sugarcane bagasse, and ammonium sulfate) was the best that favored LiP expression. The amplification of the TvLiP gene median region covering approximately 50% of the T. versicolor LPGIV gene (87% identity); the presence of Trp199, Leu115, Asp193, Trp199, and Ala203 in the translated amplicon of the T. villosa mRNA; and the close phylogenetic relationship between TvLiP and T. versicolor LiP all indicate that the target enzyme is a lignin peroxidase. Therefore, T. villosa CCMB561 has great potential for use as a LiP, MnP, and Lac producer for industrial applications.

• Journal of Mushroom
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• v.11 no.2
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• pp.87-91
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• 2013

When No. 42 strain of Pleurotus ostreatus was cultivated at five different media, MnP and Lac but no LiP activity was detected throughout the culture period in the media. The production of MnP and Lac by No. 42 strain of Pleurotus ostreatus were correlated with wheat bran composition in the medium. In the liquid culture, maximum production of MnP and Lac were observed in the medium contained glucose-peptone- yeast-wheat bran(GPYW). However, in solid medium, maximum production of MnP was observed in wood meal-wheat bran(WMW) medium, but that of Lac was observed in wheat bran(W) medium.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.32 no.1
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• pp.86-93
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• 2000

High Colored kraft bleaching effluent is one of the main constrains in pulp and paper industry due to its dissloved lignin derivatives. The degradation of lignin in pulp and paper mill effluent is mainly caused by white-rot fungi. This paper showed that the treatment with KS-62 fungus significantly reduced the color and chemical oxygen demand in the effluent. The amounts of Mn ions in the wastewater would play roles in the induction and activity of MnP (Managanese peroxidase). Extracellular MnP was isolated from the fungus KS-62. The treatment with the MnP had the most effective decolorizatiion in the wastewater treatment using nutrients mediu.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.29 no.2
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• pp.83-90
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• 1997

An unbleached hardwood kraft pulp was bleached in vitro with partially purified manganese peroxidase (MnP) from the fungus Phanerochaete sordida YK-624 without the addition of MnSO$_4$ in the presence of oxalate, malonate or gluconate known as manganese chelator, When the pulp was treated without the addition of MnSO$_4$, the pulp brightness increased by about 10 points in the presence of 2 mM oxalate, but the brightness did not significantly increase in the presence of 50 mM malonate. Residual MnP activity decreased faster during the bleaching with MnP without MnSO$_4$ in the presence of malonate than in the presence of oxalate. Oxalate reduced MnO$_2$ which already existed in the pulp or was produced from $Mn^{2+}$ by oxidation with MnP and thus supplied $Mn^{2+}$ to the MnP system. Thus, bleaching of hardwood kraft pulp with MnP, using manganese originally existing in the pulp, became possible in the presence of oxalate, a good manganese chelator and reducing reagent. Properties of partially purified MnPs from liquid cultures of white rot fungi, Ganoderma sp. YK-505, Phanerochaete sordida YK-624 and Phanerochaete chrysosporium were compared. MnP from Ganoderma sp. YK-505 was superior to MnPs from P. sordida YK-624 and P. chrysosporium in stabilities against high temperature and high concentration of $H_2O$$_2$. The MnP from Ganoderma sp. YK-505 differed in pH-activity profile from other MnPs. These data suggest that MnP from Ganoderma sp. YK-505 has different structure from those of other fungi. Bleaching of hardwood kraft pulp using the MnP from ganoderma sp. YK-505 is now in progress.

• Mycobiology
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• v.47 no.2
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• pp.217-229
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• 2019

Two manganese peroxidases (MnPs), MnP1 and MnP2, and a laccase, Lac1, were purified from Trametes polyzona KU-RNW027. Both MnPs showed high stability in organic solvents which triggered their activities. Metal ions activated both MnPs at certain concentrations. The two MnPs and Lac1, played important roles in dye degradation and pharmaceutical products deactivation in a redox mediator-free system. They completely degraded Remazol brilliant blue (25 mg/L) in 10-30 min and showed high degradation activities to Remazol navy blue and Remazol brilliant yellow, while Lac1 could remove 75% of Remazol red. These three purified enzymes effectively deactivated tetracycline, doxycycline, amoxicillin, and ciprofloxacin. Optimal reaction conditions were $50^{\circ}C$ and pH 4.5. The two MnPs were activated by organic solvents and metal ions, indicating the efficacy of using T. polyzona KU-RNW027 for bioremediation of aromatic compounds in environments polluted with organic solvents and metal ions with no need for redox mediator supplements.

• Journal of the Korean Wood Science and Technology
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• v.25 no.2
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• pp.1-20
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• 1997

목재를 분해시키는 담자균류들은 목재 및 목질복합체에 쉽사리 침투하여 복잡한 리그노셀룰로오스 복합체를 분해시킨다. 이러한 분해에는 많은 효소시스템들이 복합적으로 작용하면서 상호 협동하는 것으로 보고되고 있다. 지금까지 일려진 효소들은 통상 3개의 그룹으로 나눌 수 있는데 그 하나는 목재성분을 직접적으로 공격하는 효소균들, 예를 들면 cellulase complex, laccase(LAC), lignin peroxidase(LIP), horse-radish peroxidase(HRP), manganese-independent peroxidase(MIP) 및 protocatechuate 3,4-dioxygenase(PCD) 등이 있고, 두번째 그룹으로서 manganese-dependent peroxidase(MnP), aryl alcohol oxidase(AAO) 및 glyoxal oxidase(GLO) 등인데, 이들 효소들은 목질을 직접적으로 공격하지 않고 제1그룹의 효소들과 협동하여 작용하는 것으로 알려지고 있다. 제3그룹의 효소들은 glucose oxidase(GOD) 및 cellobiose : quinone oxidoreductase(CBQ)로서 feedback type의 효소들로서 목재고분자의 분해시 대사의 고리를 결합시켜 주는 매우 중요한 기능을 하는 효소군들이다. 그러나 이 이외에도 다른 분해기구가 밝혀지고 있으며 기타 효소들에 의한 리그노셀룰로오스의 분해반응기구의 해명에는 상당한 시간이 걸릴 것으로 사료된다.

• Journal of the Korean Wood Science and Technology
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• v.39 no.6
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• pp.469-480
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• 2011

In this study, to determine the ligninase activity related to the PCBs degradation of Ceriporia sp. ZLY-2010, the protein contents and manganese peroxidase (MnP) and laccase activities during cultivation on shallow stationary culture (SSC) medium were observed. 4 PCB congeners were selected depending on the number of chlorine substituted on biphenyl. Furthermore, to examine the effects of cytochrome P450 monooxygenase, the inhibition of cytochrome P450 monooxygenase was evaluated by measuring the biodegradation rate when inhibitor such as 1-aminobenzotriazole was added. The extracellular protein contents were affected by PCB congeners in culture media. The total protein in the culture medium showed the biggest differences between the samples containing 2,2',4,4',5,5'-hexachlorobiphenyl and the control. On the other hand, MnP and laccase activity showed dominant increases within samples containing 4,4'-dichlorobiphenyl and 2,3',4',5-tetrachlorobiphenyl. Cytochrome P450 monooxygenase was inhibited by adding inhibitor, 1-aminobenzotriazole in low concentration. Only 2.73% of 2,3',4',5-tetrachlorobiphenyl was degraed on day 1, and biodegradation of 2,2',4,4',5,5'-hexachlorobiphenyl was inhibited as well, showing about 20% of biodegradation rate.

• Journal of Mushroom
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• v.21 no.4
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• pp.209-214
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• 2023

In this study, Pleurotus ostreatus No.42 was cultured in glucose-peptone-yeast-wheat bran medium using a previously reported novel rotary draft tube bioreactor. Versatile peroxidase (VP), a lignin-degrading enzyme, was isolated from a pellet-type mycelium culture grown in the medium for seven days. The VP was purified by sequentially applying ultra-filtration, DEAE-Sepharose CL-6B column, and Mono Q column. SDS-PAGE analysis revealed the molecular weight of VP to be 36.4 KDa with an isoelectric point of 3.65. The amino acid sequence was confirmed as VTCATGQTT. The purified VP was observed to possess the property of not only oxidizing Mn ions but also decomposing veratryl alcohol, a non-phenolic compound. The catalytic ability of VP is a subject for future research.

• Applied Biological Chemistry
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• v.48 no.1
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• pp.53-59
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• 2005

The effect of various stressors such as reductant ascorbic acid, signalling molecules (salicylic acid and methyl jasmonic acid), heavy metals $(NiCl_2,\;and\;MnSO_4)$ and NaCl on the glutathione peroxidase (GPX) activities and isoenzyme expression patterns were investigated in rice seedling roots. Total GPX activity increased according to the increase of ascorbic acid concentration. Prominent enhancement of GPX1 isozyme due to ascorbic acid contributed to the increase of total GPX activity. GPX showed different reactivity toward salicylic acid and methyl jasmonic acid. GPX activity increased at 0.1 mM salicylic acid, and then decreased thereafter. However, GPX increased gradually in a methyl jasmonic acid concentration-dependent manner, and 3 fold increase of GPX activity was found at 1 mM methyl jasmonic acid. Moreover, GPX1 isozyme increased according to the increase of salicylic acid, while GPX1 isozyme decreased according to the increase of methyl jasmonic acid. When metal ions were treated, GPX activity increased considerably according to the increase of $NiCl_2$ concentration, however, GPX activity increased about 2 fold at 0.5 mM $CuSO_4$ and then decreased. Enhancement of GPX1 isozyme contributed to the increase of total GPX activities in $NiCl_2-treated$ and $MnSO_4-treated$ rice seedlings. Total GPX activity increased 1.7 fold in response to 300 mM NaCl. Especially GPX2 isozyme showed gradual increase according to the increase of NaCl concentration.

• Proceedings of the Korea Society of Poultry Science Conference
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• 2005.11a
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• pp.76-77
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• 2005

Effects of dietary killed salmonella and vancomycin on the performance and immune response was investigated in broiler chicks inoculated with Salmonella typhimurium. During 3 week(27 d) of age, experimental diet did not affect daily gain, feed intake and feed efficiency. Dietary killed salmonella and vancomycin decreased MnSOD activity. At 7day after Salmonella typhimurium inoculation, dietary killed salmonella and vancomycin increased, daily gain and feed efficiency of broiler chicks. At 7 and 15 day after salmonella inoculation, dietary killed salmonella and vancomycin decreased erythrocyte peroxidase activity, but elevated proliferation of PBMC stimulated with LPS and supernatant IL-1 level secreted by the PBMC. The results suggested that dietary killed salmonella and vancomycin improved the performance of broiler chicks due to modulate antioxidant system and innate immune response of broiler chicks innoculated with Salmonella typhimurium.