• Title/Summary/Keyword: lignin peroxidase

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Studies on the Treatment of Pulp Bleaching Effluent with KS-62 Fungus (KS-62 균주에 의한 펄프 표백 폐액처리에 관한 연구)

  • 조준형;은주영
    • 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.

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Biodegradation of Polycyclic Aromatic Hydrocarbons by White Rot Fungi (백색부후균을 이용한 다환방향족 탄화수소(PAHs) 의 분해)

  • 류원률;서윤수;장용근;조무환
    • KSBB Journal
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    • v.15 no.3
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    • pp.262-267
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    • 2000
  • The white rot fungi Phanerochaete chrysosporium(IFO 31249) Trametes sp and Pleurotus sp. were studied for their ability to degrade Polycyclic Aromatic Hydrocarbons(PAHs) using anthracene and pyrene as model compounds. The disapperarance anthracene and pyrene of from cultures of wild type strains. P chrysosporium Trametes sp. and Pleurotus sp was observed However the activities of ligninolytic enzymes were not detected in P chrysosporium cultures during degradation while ligninolytic enzymes were detected in both culture of Trametes sp. and Pleurotus sp. Therefore our results showed that PAHs was degraded under ligninolytic as well as nonligninolytic conditions. The results also indicate that lignin peroxidase(LiP) mananese peroxidase(MnP) and laccase are not essential for the biodegradation of PAHs by white rot fungi.

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Kinetics of veratryl alcohol oxidation by lignin peroxidase and in-situ generated $H_2O_2$ in an electrochemical reactor

  • Lee, Gi-Beom;Gu, Man-Bok;Mun, Seung-Hyeon
    • 한국생물공학회:학술대회논문집
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    • 2000.11a
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    • pp.524-527
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    • 2000
  • An electroenzymatic system to oxidize veratryl alcohol of on electrodes with in-situ generated hydrogen peroxide was studied. We investigated hydrogen peroxide generation, current efficiency, and veratryl alcohol oxidation in the electrode system at various conditions. The reaction rates of veratryl alcohol oxidation were compared in an electrochemical, an electroenzymatic, and an usual biochemical systems to prove the concept of electroenzymatic oxidation.

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Decolorization of Three Acid Dyes by Enzymes from Fungal Strains

  • PARK , CHUL-HWAN;LEE, YU-RI;KIM, TAK-HYUN;LEE, BYUNG-HWAN;LEE, JIN-WON;KIM, SANG-YONG
    • Journal of Microbiology and Biotechnology
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    • v.14 no.6
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    • pp.1190-1195
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    • 2004
  • In recent years, there has been an intensive research on decolorization of dye and textile wastewater by various fungal strains. In this study, the decolorization ability of three commercial dyes, acid yellow 99, acid blue 350, and acid red 114, were investigated using 10 fungal strains. Among the fungal strains tested, Trametes versicolor KCTC 16781 completely decolorized all dyes in both solid and liquid experiments, and was also able to decolorize the mixture of those three dyes in liquid experiments. The secretion of the ligninolytic enzymes into the extracellular medium during decolorization by T versicolor KCTC 16781 was also studied. No lignin peroxidase activity was detected, and manganese peroxidase and laccase activities were investigated.

Production of Mn-peroxidase and Laccase from Lentinus edodes and Coriolus versicolor (표고 및 구름버섯으로부터 Mn-peroxidase와 Laccase의 생산(生産))

  • Bae, Hyeun-Jong;Han, Ok-Soo;Koh, Hong-Bum;Kim, Yoon-Soo
    • Journal of the Korean Wood Science and Technology
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    • v.21 no.3
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    • pp.87-93
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    • 1993
  • This study was undertaken to investigate the characteristics and the productivities of lignin olytic enzymes: laccase (Lac) and Mn-dependent peroxidase (MnP) from Coriolus versicolor and Lentinus edodes respectively. Enzymes were isolated from cultural filterates and purified according to the standard methods. These enzymes showed one band in SDS-PAGE and their molecular weights were found 62,000 and 45,000 dalton respectively. Polyclonal antibodies against Lac and MnP were raised against mouse. In the ELISA (enzyme-linked immunosorbent assay), Lac and MnP-antiserum produced a strong positive reaction with Lac and MnP antigen($A_{405}$=2.50 and 3.53 respectively). The sera to negative (S/N) ratio was determined by the dividing the mean absorbance of antibodies by the corresponding diluted samples from normal mouse serum. The sera produced showed 2 times more positive reaction in S/N ratio than negative sera.

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Roc10, a Rice HD-Zip transcription factor gene, modulates lignin biosynthesis for drought tolerance

  • Bang, Seung Woon;Lee, Dong-Keun;Jung, Harin;Chung, Pil Joong;Kim, Youn Shic;Choi, Yang Do;Suh, Joo-Won;Kim, Ju-Kon
    • Proceedings of the Korean Society of Crop Science Conference
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    • 2017.06a
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    • pp.159-159
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    • 2017
  • Drought, a common environmental constraint, induces a range of physiological, biochemical and molecular changes in plants, and can cause severe reductions in crop yield. Consequently, understanding the molecular mechanisms of drought tolerance is an important step towards crop biotechnology. Here, we report that the rice (Oryza sativa) homeodomain-leucine zipper class IV transcription factor gene, ${\underline{R}ice}$ ${\underline{o}utermost}$ ${\underline{c}ell-specific}$ gene 10 (Roc10), enhances drought tolerance and grain yield by increasing lignin accumulation in ground tissues. Overexpression of Roc10 in rice significantly increased drought tolerance at the vegetative stages of growth and promoted both more effective photosynthesis and a reduction in water loss rate, compared with non-transgenic controls or RNAi transgenic plants. Importantly, Roc10 overexpressing plants had a higher drought tolerance at the reproductive stage of growth and a higher grain yield compared with the controls under field-drought conditions. Roc10 is mainly expressed in outer cell layers including the epidermis and the vasculature of the shoots, which coincides with areas of cell wall lignification. Roc10 overexpression elevated the expression levels of lignin biosynthetic genes in shoots, with a concomitant increase in the accumulation of lignin, while the overexpression and RNAi lines showed opposite patterns of lignin accumulation. We identified downstream target genes of Roc10 by performing RNA-seq and chromatin immunoprecipitation (ChIP)-seq analyses of shoot tissues. Roc10 was found to directly bind to the promoter of PEROXIDASEN/PEROXIDASE38, a key gene in lignin biosynthesis. Together, our findings suggest that Roc10 confers drought stress tolerance by promoting lignin biosynthesis in ground tissues.

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Degradation Characteristics of Ligninsulfonate by Laccase and Mn-peroxidase (Laccase와 Mn-peroxidase에 의한 Ligninsulfonate의 분해 특성)

  • Bae, Hyeun-Jong;Kim, Yoon-Soo;Mun, Sung-Phil
    • Journal of the Korean Wood Science and Technology
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    • v.23 no.4
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    • pp.27-32
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    • 1995
  • To understand whether ligninolytic enzyme catalyze polymerization or depolymerization of the high molecular weight (HMW) lignin, the action of laccase and Mn-peroxidase (MnP) towards commercial ligninsulfonates (LS) was examined in various conditions of pH and cosubstrates. Polymerization occurred when LS was incubated with laccase at pH 6.0. In contrast, the high molecular weight portions were significant1y reduced at pH 4.5, especially when glucose was added. When LS was treated with MnP at pH 4.5, compounds of low molecular weight were produced. In particular, when cellobiose was added to Mn-P reaction mixture, the breakdown of LS was observed. In conclusion, degradation of LS by laccase and MnP occurred primarily at pH 4.5 where-as polymerization of LS was dominant at pH 6.0. Color index, however, was not greatly changed in the degradation mixtures of LS.

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Biodegradation of Endocrine Disrupting Chemicals by Genetic Transformants of Phlebia tremellosa Using Manganese Peroxidase Gene from Trametes versicolor (구름버섯 망간 과산화효소를 도입한 아교버섯 형질전환체에 의한 내분비장애 물질의 생분해)

  • Kum, Hyun-Woo;Kim, Myung-Kil;Choi, Hyoung-T.
    • Korean Journal of Microbiology
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    • v.45 no.1
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    • pp.82-85
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    • 2009
  • Endocrine disrupting chemicals (EDCs) disturb animal hormonal system even at very low concentrations, and finally give harmful effects to human through the food web. A white rot fungus Phlebia tremellosa isolated in Korea, was reported to have good degrading activity against the endocrine disrupting phthalates. However, this fungus has very low manganese peroxidase (MnP) activity under various culture conditions while laccase and lignin peroxidase activities were high. We have isolated an MnP cDNA from Trametes versicolor which was involved in the degradation of EDCs, and constructed an MnP expression vector to use in the genetic transformation of P. tremellosa in order to get higher MnP producing strains. Many transformants had integrated expression vector in their chromosomal DNAs, and showed increased MnP activity. One of two transformants showed increased degradation of 4 EDCs (70${\sim}$88%) than the wild type (30${\sim}$45% degradation rates), and showed twice better removal of estrogenic activities generated by the EDCs than the wild type.

Enzymatic Bleaching of Kraft-pulp with Horseradish Peroxidase and Radical Mediator (Horseradish Peroxidase와 라디칼 전달체를 이용한 Kraft 펄프의 표백)

  • 류근갑;권오열
    • KSBB Journal
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    • v.16 no.2
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    • pp.179-182
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    • 2001
  • The use of 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)(ABTS) as a radical mediator enhanced the bleaching efficiency of kraft pulp by horseradish peroxidase(HRP) and $H_2O_2$. High concentrations of up to 20 mM $H_2O_2$. were used. The bleaching of the kraft pulp increased as the amount of HRP and ABTS concentration were inceased up to 0.3 mg/90 mL and 2 mM, respectively. The bleaching of the kraft pulp was closely related with the HRPs activity and its adsorption onto the pulp. The activity of HRP and bleaching of kraft pulp were maximum at pH 7 and were reduced either in a acidic or alkaline solutions. The adsorption of HRP onto pulp was low in solutions of pH 6-8 and high in an acidic(pH5) and an alkaline solutions(pH 9). The adsorption of the enzyme was greater for alkali-lignin than for crystalline cellulose, the two major components of pulp.

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Decolorization of Synthetic Dyes and Ligninolytic Enzymes Production by White Rot Fungi (백색부후균에 의한 합성염료의 탈색과 리그닌분해 효소의 생산)

  • Gu, Bon-Joon;Kim, Min-Sik;Kim, Yin-Man;Kim, Seon-Woong;Choi, Won-Hyeok;Lee, Mi-Hwa;Cho, Hae-Jin;Lee, Tae-Soo
    • The Korean Journal of Mycology
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    • v.40 no.2
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    • pp.98-103
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    • 2012
  • This study has been conducted to screen the decolorization of 4 aromatic synthetic dyes and production of ligninolytic enzymes by 4 white rot fungi such as Bjerkanderia adusta, Cerrena unicolor, Pleurotus pulmonarius and Abortiporus biennis. It was found that B. adusta, C. unicolor, and P. pulmonarius have the ability to efficiently decolorize congo red and moderately decolorized amaranth and orange G in solid and liquid culture media. However, the decolorization rate of 4 synthetic dyes by A. biennis was relatively low. The decolorization of congo red, amaranth, orange G were related to the growth rate of the fungal mycelia in the solid medium. But, the all fungi tested did not efficiently decolorize methylene blue in the liquid culture media. To investigate the production of ligninolytic enzymes in media containing aromatic compounds, fungi were cultured in 1% naphthalene supplemented potato dextrose broth medium. All fungi tested had the capability to produce laccase, lignin peroxidase and manganese peroxidase, and B. adusta was the best ligninolytic enzymes producing white rot fungus among other fungi tested.