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Volumn 31, Issue 5, 2002, Pages 627-633

Ligninolytic enzymes of the fungus Irpex lacteus (Polyporus tulipiferae): Isolation and characterization of lignin peroxidase

Author keywords

Heme peroxidase; Lignin peroxidase; Ligninolytic enzymes; White rot fungi

Indexed keywords

AMINO ACIDS; CATALYSIS; ENZYMES; HYDROGEN PEROXIDE; LIGNIN; MANGANESE; REACTION KINETICS;

EID: 0037015412     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(02)00171-0     Document Type: Article
Times cited : (30)

References (47)
  • 1
    • 0027180067 scopus 로고
    • Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Gold M.H., Alic M. Molecular biology of the lignin-degrading basidiomycete Phanerochaete chrysosporium. Microbiol. Rev. 57:1993;605-622.
    • (1993) Microbiol. Rev. , vol.57 , pp. 605-622
    • Gold, M.H.1    Alic, M.2
  • 2
    • 0027216563 scopus 로고
    • An overview of the recent advances on the physiology and molecular biology of lignin peroxidases of Phanerochaete chrysosporium
    • Reddy C.A. An overview of the recent advances on the physiology and molecular biology of lignin peroxidases of Phanerochaete chrysosporium. J. Biotechnol. 30:1993;91-107.
    • (1993) J. Biotechnol. , vol.30 , pp. 91-107
    • Reddy, C.A.1
  • 3
    • 0028347666 scopus 로고
    • Lignin-modifying enzymes from selected white-rot fungi: Production and role in lignin degradation
    • Hatakka A. Lignin-modifying enzymes from selected white-rot fungi: production and role in lignin degradation. FEMS Microbiol. Rev. 13:1994;125-135.
    • (1994) FEMS Microbiol. Rev. , vol.13 , pp. 125-135
    • Hatakka, A.1
  • 5
    • 0025878967 scopus 로고
    • Ligninolytic properties of different white-rot fungi
    • Nerud F., Zouchova Z., Misurcova Z. Ligninolytic properties of different white-rot fungi. Biotechnol. Lett. 13:1991;657-660.
    • (1991) Biotechnol. Lett. , vol.13 , pp. 657-660
    • Nerud, F.1    Zouchova, Z.2    Misurcova, Z.3
  • 6
    • 0028803412 scopus 로고
    • Lignin peroxidases, manganese peroxidases, and other ligninolytic enzymes produced by Phlebia radiata during solid-state fermentation of wheat straw
    • Vares T., Kalsi M., Hatakka A. Lignin peroxidases, manganese peroxidases, and other ligninolytic enzymes produced by Phlebia radiata during solid-state fermentation of wheat straw. Appl. Environ. Microbiol. 61:1995;3315-3520.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3315-3520
    • Vares, T.1    Kalsi, M.2    Hatakka, A.3
  • 7
    • 0029167037 scopus 로고
    • Screening of 68 species of basidiomycetes for enzymes involved in lignin degradation
    • Pelaez F., Martinez M.J., Martinez A.T. Screening of 68 species of basidiomycetes for enzymes involved in lignin degradation. Mycol. Res. 99:1995;37-42.
    • (1995) Mycol. Res. , vol.99 , pp. 37-42
    • Pelaez, F.1    Martinez, M.J.2    Martinez, A.T.3
  • 8
    • 69749084914 scopus 로고
    • Lignin peroxidase of Phanerochaete chrysosporium
    • Tien M., Kirk K.T. Lignin peroxidase of Phanerochaete chrysosporium. Methods Enzymol. 161:1988;238-249.
    • (1988) Methods Enzymol. , vol.161 , pp. 238-249
    • Tien, M.1    Kirk, K.T.2
  • 9
    • 0032488874 scopus 로고    scopus 로고
    • Purification and characterization of two lignin peroxidase isozymes produced by Bjerkandera sp. strain Bos55
    • ten Have R., Hartmans S., Teunissen P.J., Field J.A. Purification and characterization of two lignin peroxidase isozymes produced by Bjerkandera sp. strain Bos55. FEBS Lett. 422:1998;391-394.
    • (1998) FEBS Lett. , vol.422 , pp. 391-394
    • Ten Have, R.1    Hartmans, S.2    Teunissen, P.J.3    Field, J.A.4
  • 10
  • 11
    • 0025382585 scopus 로고
    • Aryl-alcohol oxidase and lignin peroxidase from the white-rot fungus Bjerkandera adusta
    • Muheim A., Leisola M.S.A., Schoemaker E. Aryl-alcohol oxidase and lignin peroxidase from the white-rot fungus Bjerkandera adusta. J. Biotechnol. 13:1990;159-167.
    • (1990) J. Biotechnol. , vol.13 , pp. 159-167
    • Muheim, A.1    Leisola, M.S.A.2    Schoemaker, E.3
  • 12
    • 0025034204 scopus 로고
    • Formation and action of lignin-modifying enzymes in cultures of Phlebia radiata supplemented with veratric acid
    • Lundell T., Leonowicz A., Rogalski J., Hatakka T. Formation and action of lignin-modifying enzymes in cultures of Phlebia radiata supplemented with veratric acid. Appl. Environ. Microbiol. 56:1990;2623-2629.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 2623-2629
    • Lundell, T.1    Leonowicz, A.2    Rogalski, J.3    Hatakka, T.4
  • 13
    • 0024288734 scopus 로고
    • Ligninolytic enzymes of the white-rot fungus Phlebia radiata
    • Niku Paavola M.L., Karhunen E., Salola P., Raunio V. Ligninolytic enzymes of the white-rot fungus Phlebia radiata. Biochem. J. 254:1988;877-884.
    • (1988) Biochem. J. , vol.254 , pp. 877-884
    • Niku Paavola, M.L.1    Karhunen, E.2    Salola, P.3    Raunio, V.4
  • 14
    • 0001091831 scopus 로고
    • Production of laccase, lignin peroxidase and manganese-dependent peroxidase by various strains of Trametes versicolor depending on culture conditions
    • Rogalski J., Lundell T., Leonowicz A., Hatakka A. Production of laccase, lignin peroxidase and manganese-dependent peroxidase by various strains of Trametes versicolor depending on culture conditions. Acta Microbiol. Pol. 40:1991;221-234.
    • (1991) Acta Microbiol. Pol. , vol.40 , pp. 221-234
    • Rogalski, J.1    Lundell, T.2    Leonowicz, A.3    Hatakka, A.4
  • 15
    • 0032959539 scopus 로고    scopus 로고
    • Lignin-modifying enzymes of Flavodon flavus, a basidiomycete isolated from a coastal marine environment
    • Raghukumar C., D'Souza T.M., Thorn R.G., Reddy C.A. Lignin-modifying enzymes of Flavodon flavus, a basidiomycete isolated from a coastal marine environment. Appl. Environ. Microbiol. 65:1999;2103-2111.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2103-2111
    • Raghukumar, C.1    D'Souza, T.M.2    Thorn, R.G.3    Reddy, C.A.4
  • 16
    • 0028888065 scopus 로고
    • Potential for bioremediation of xenobiotic compounds by the white-rot fungus Phanerochaete chrysosporium
    • Paszczynski A., Crawford R.L. Potential for bioremediation of xenobiotic compounds by the white-rot fungus Phanerochaete chrysosporium. Biotechnol. Prog. 11:1995;368-379.
    • (1995) Biotechnol. Prog. , vol.11 , pp. 368-379
    • Paszczynski, A.1    Crawford, R.L.2
  • 17
    • 0031194116 scopus 로고    scopus 로고
    • Binding of pentachlorophenol to humic substances in soil by the action of white rot fungi
    • Ruttimann-Johnson C., Lamar R.T. Binding of pentachlorophenol to humic substances in soil by the action of white rot fungi. Soil Biol. Biochem. 29:1997;1143-1148.
    • (1997) Soil Biol. Biochem. , vol.29 , pp. 1143-1148
    • Ruttimann-Johnson, C.1    Lamar, R.T.2
  • 20
    • 0033928776 scopus 로고    scopus 로고
    • Biodegradation of pyrene by the white rot fungus, Irpex lacteus
    • Hwang S.S., Song H.G. Biodegradation of pyrene by the white rot fungus, Irpex lacteus. J. Microbiol. Biotechnol. 10:2000;344-348.
    • (2000) J. Microbiol. Biotechnol. , vol.10 , pp. 344-348
    • Hwang, S.S.1    Song, H.G.2
  • 21
    • 0033292860 scopus 로고    scopus 로고
    • Hydroxyl radical generation and phenol oxidase activity in wood degradation by the white-rot basidiomycete Irpex lacteus
    • Tanaka H., Itakura S., Enoki A. Hydroxyl radical generation and phenol oxidase activity in wood degradation by the white-rot basidiomycete Irpex lacteus. Mater. Org. 33:1999;91-105.
    • (1999) Mater. Org. , vol.33 , pp. 91-105
    • Tanaka, H.1    Itakura, S.2    Enoki, A.3
  • 22
    • 0034976251 scopus 로고    scopus 로고
    • Ligninolytic enzyme production in selected sub-tropical white rot fungi under different culture conditions
    • Tekere M., Zvauya R., Read J.S. Ligninolytic enzyme production in selected sub-tropical white rot fungi under different culture conditions. J. Basic Microbiol. 41:2001;115-129.
    • (2001) J. Basic Microbiol. , vol.41 , pp. 115-129
    • Tekere, M.1    Zvauya, R.2    Read, J.S.3
  • 23
    • 0027197211 scopus 로고
    • Overproduction of lignin peroxidase by Phanerochaete chrysosporium (BKM-F-1767) under nonlimiting nutrient conditions
    • Dosoretz C.G., Rothschild N., Hadar Y. Overproduction of lignin peroxidase by Phanerochaete chrysosporium (BKM-F-1767) under nonlimiting nutrient conditions. Appl. Environ. Microbiol. 59:1993;1919-1926.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1919-1926
    • Dosoretz, C.G.1    Rothschild, N.2    Hadar, Y.3
  • 24
    • 0033083121 scopus 로고    scopus 로고
    • Manganese deficiency can replace high oxygen levels needed for lignin peroxidase formation by Phanerochaete chrysosporium
    • Rothschild N., Levkowitz A., Hadar Y., Dosoretz C.G. Manganese deficiency can replace high oxygen levels needed for lignin peroxidase formation by Phanerochaete chrysosporium. Appl. Environ. Microbiol. 65:1999;483-488.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 483-488
    • Rothschild, N.1    Levkowitz, A.2    Hadar, Y.3    Dosoretz, C.G.4
  • 25
    • 0025099761 scopus 로고
    • Mn(II) regulation of lignin peroxidases and manganese-dependent peroxidases from lignin-degrading white rot fungi
    • Bonnarme P., Jeffries T.W. Mn(II) regulation of lignin peroxidases and manganese-dependent peroxidases from lignin-degrading white rot fungi. Appl. Environ. Microbiol. 56:1990;210-217.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 210-217
    • Bonnarme, P.1    Jeffries, T.W.2
  • 26
    • 0025362787 scopus 로고
    • Manganese regulates expression of manganese peroxidase by Phanerochaete chrysosporium
    • Brown J., Glenn J.K., Gold M.H. Manganese regulates expression of manganese peroxidase by Phanerochaete chrysosporium. J. Bacteriol. 172:1990;3125-3130.
    • (1990) J. Bacteriol. , vol.172 , pp. 3125-3130
    • Brown, J.1    Glenn, J.K.2    Gold, M.H.3
  • 27
    • 0021519023 scopus 로고
    • 2-requiring diarylpropane oxygenase from the white rot basidiomycete, Phanerochaete chrysosporium
    • 2-requiring diarylpropane oxygenase from the white rot basidiomycete, Phanerochaete chrysosporium. Arch. Biochem. Biophys. 234:1984;353-362.
    • (1984) Arch. Biochem. Biophys. , vol.234 , pp. 353-362
    • Gold, M.H.1    Kuwahara, M.2    Chiu, A.A.3    Glenn, J.K.4
  • 28
    • 0026763819 scopus 로고
    • Determination of the respiration kinetics for mycelial pellets of Phanerochaete chrysosporium
    • Michel F.C. Jr., Grulke E.A., Reddy C.A. Determination of the respiration kinetics for mycelial pellets of Phanerochaete chrysosporium. Appl. Environ. Microbiol. 58:1992;1740-1745.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1740-1745
    • Michel F.C., Jr.1    Grulke, E.A.2    Reddy, C.A.3
  • 29
    • 0030942922 scopus 로고    scopus 로고
    • Production of multiple laccase isoforms by Phanerochaete chrysosporium grown under nutrient sufficiency
    • Dittmer J.K., Patel N.J., Dhawale S.W., Dhawale S.S. Production of multiple laccase isoforms by Phanerochaete chrysosporium grown under nutrient sufficiency. FEMS Microbiol. Lett. 149:1997;65-70.
    • (1997) FEMS Microbiol. Lett. , vol.149 , pp. 65-70
    • Dittmer, J.K.1    Patel, N.J.2    Dhawale, S.W.3    Dhawale, S.S.4
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1972;680-685.
    • (1972) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0026559256 scopus 로고
    • Manganese-inhibited peroxidase from the white-rot fungus Bjerkandera sp. Bos55
    • de Jong E., Field J.A., de Bont J.A.M. Manganese-inhibited peroxidase from the white-rot fungus Bjerkandera sp. Bos55. FEBS Lett. 299:1992;107-110.
    • (1992) FEBS Lett. , vol.299 , pp. 107-110
    • De Jong, E.1    Field, J.A.2    De Bont, J.A.M.3
  • 33
    • 0025002841 scopus 로고
    • Lignin peroxidase compound III. Mechanism of formation and decomposition
    • Wariishi H., Gold M.H. Lignin peroxidase compound III. Mechanism of formation and decomposition. J. Biol. Chem. 265:1990;2070-2077.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2070-2077
    • Wariishi, H.1    Gold, M.H.2
  • 34
    • 0024676158 scopus 로고
    • Physical and enzymatic properties of lignin peroxidase isoenzymes from Phanerochaete chrysosporium
    • Farrell R.L., Murtagh K.E., Tien M., Mozuch M.D., Kirk K.T. Physical and enzymatic properties of lignin peroxidase isoenzymes from Phanerochaete chrysosporium. Enzyme Microb. Technol. 11:1989;322-328.
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 322-328
    • Farrell, R.L.1    Murtagh, K.E.2    Tien, M.3    Mozuch, M.D.4    Kirk, K.T.5
  • 35
    • 0025120223 scopus 로고
    • Lignin peroxidase from Phanerochaete chrysosporium. Molecular and kinetic characterization of isozymes
    • Glumoff T., Harvey P.J., Molinari S., Goble M., Frank G., Palmer J.M.et al. Lignin peroxidase from Phanerochaete chrysosporium. Molecular and kinetic characterization of isozymes. Eur. J. Biochem. 187:1990;515-520.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 515-520
    • Glumoff, T.1    Harvey, P.J.2    Molinari, S.3    Goble, M.4    Frank, G.5    Palmer, J.M.6
  • 36
    • 0031038203 scopus 로고    scopus 로고
    • Lignin peroxidase isozymes from Phanerochaete chrysosporium can be enzymatically dephosphorylated
    • Rothschild N., Hadar Y., Dosoretz C.G. Lignin peroxidase isozymes from Phanerochaete chrysosporium can be enzymatically dephosphorylated. Appl. Environ. Microbiol. 63:1997;857-861.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 857-861
    • Rothschild, N.1    Hadar, Y.2    Dosoretz, C.G.3
  • 37
    • 0034644544 scopus 로고    scopus 로고
    • Southern blot screening for lignin peroxidase and aryl-alcohol oxidase genes in 30 fungal species
    • Varela E., Martinez A.T., Martinez M.J. Southern blot screening for lignin peroxidase and aryl-alcohol oxidase genes in 30 fungal species. J. Biotechnol. 83:2000;245-251.
    • (2000) J. Biotechnol. , vol.83 , pp. 245-251
    • Varela, E.1    Martinez, A.T.2    Martinez, M.J.3
  • 38
    • 0029010146 scopus 로고
    • Ligninolytic system formation by Phanerochaete chrysosporium in air
    • Rothschild N., Hadar Y., Dosoretz C.G. Ligninolytic system formation by Phanerochaete chrysosporium in air. Appl. Environ. Microbiol. 61:1995;1833-1838.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1833-1838
    • Rothschild, N.1    Hadar, Y.2    Dosoretz, C.G.3
  • 39
    • 0028269476 scopus 로고
    • Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium
    • Reddy C.A., D'Souza T.M. Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium. FEMS Microbiol. Rev. 13:1994;137-152.
    • (1994) FEMS Microbiol. Rev. , vol.13 , pp. 137-152
    • Reddy, C.A.1    D'Souza, T.M.2
  • 41
    • 0027218398 scopus 로고
    • Isozymes of lignin peroxidase and manganese(II) peroxidase from the white-rot basidiomycete Trametes versicolor. II. Partial sequences, peptide maps, and amino acid and carbohydrate compositions
    • Johansson T., Welinder K.G., Nyman P.O. Isozymes of lignin peroxidase and manganese(II) peroxidase from the white-rot basidiomycete Trametes versicolor. II. Partial sequences, peptide maps, and amino acid and carbohydrate compositions. Arch. Biochem. Biophys. 300:1993;57-62.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 57-62
    • Johansson, T.1    Welinder, K.G.2    Nyman, P.O.3
  • 42
    • 0343924592 scopus 로고    scopus 로고
    • Recent advances on the molecular genetics of ligninolytic fungi
    • Cullen D. Recent advances on the molecular genetics of ligninolytic fungi. J. Biotechnol. 53:1997;273-289.
    • (1997) J. Biotechnol. , vol.53 , pp. 273-289
    • Cullen, D.1
  • 43
    • 0037117789 scopus 로고    scopus 로고
    • Molecular biology and structure-function of lignin-degrading heme peroxidases
    • Martinez A.T. Molecular biology and structure-function of lignin-degrading heme peroxidases. Enzyme Microb. Technol. 30:2002;425-444.
    • (2002) Enzyme Microb. Technol. , vol.30 , pp. 425-444
    • Martinez, A.T.1
  • 44
    • 0034307940 scopus 로고    scopus 로고
    • The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases
    • Camarero S., Ruiz-Duenas F.J., Sarkar S., Martinez M.J., Martinez A.T. The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases. FEMS Microbiol. Lett. 191:2000;37-43.
    • (2000) FEMS Microbiol. Lett. , vol.191 , pp. 37-43
    • Camarero, S.1    Ruiz-Duenas, F.J.2    Sarkar, S.3    Martinez, M.J.4    Martinez, A.T.5
  • 45
    • 0033537844 scopus 로고    scopus 로고
    • Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites
    • Camarero S., Sarkar S., Ruiz-Duenas F.J., Martinez M.J. Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites. J. Biol. Chem. 274:1999;10324-10330.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10324-10330
    • Camarero, S.1    Sarkar, S.2    Ruiz-Duenas, F.J.3    Martinez, M.J.4
  • 46
    • 0032546787 scopus 로고    scopus 로고
    • Characterization of a novel manganese peroxidase-lignin peroxidase hybrid isozyme produced by Bjerkandera species strain Bos55 in the absence of manganese
    • Mester T., de Jong E., Field J.A. Characterization of a novel manganese peroxidase-lignin peroxidase hybrid isozyme produced by Bjerkandera species strain Bos55 in the absence of manganese. J. Biol. Chem. 273:1998;15412-15417.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15412-15417
    • Mester, T.1    De Jong, E.2    Field, J.A.3
  • 47
    • 0027968068 scopus 로고
    • CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


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