메뉴 건너뛰기




Volumn 11, Issue , 2013, Pages 115-141

Organopollutant degradation by wood decay basidiomycetes

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIODEGRADATION; BIOREMEDIATION; DECAY (ORGANIC); ENZYME ACTIVITY; FUNGI; GENE ENCODING; GENE EXPRESSION; LIGNIN; METABOLISM; POLYSULFONES;

EID: 85030111584     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-642-36821-9_5     Document Type: Chapter
Times cited : (5)

References (298)
  • 1
    • 11244354522 scopus 로고    scopus 로고
    • Fungal degradation of wood: Initial proteomic analysis of extracellular proteins of Phanerochaete chrysosporium grown on oak substrate
    • Abbas A, Koc H et al.(2004) Fungal degradation of wood: initial proteomic analysis of extracellular proteins of Phanerochaete chrysosporium grown on oak substrate. Curr Genet.47:49-56
    • (2004) Curr Genet , vol.47 , pp. 49-56
    • Abbas, A.1    Koc, H.2
  • 2
    • 0027477044 scopus 로고
    • Isolation and transformation of uracil auxotrophs of the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Akileswaran L, Alic M et al.(1993) Isolation and transformation of uracil auxotrophs of the lignin-degrading basidiomycete Phanerochaete chrysosporium. Curr Genet.23:351-356
    • (1993) Curr Genet , vol.23 , pp. 351-356
    • Akileswaran, L.1    Alic, M.2
  • 3
    • 77957153282 scopus 로고
    • Mating system and DNA transformation of the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Alic MM(1990) Mating system and DNA transformation of the lignin-degrading basidiomycete Phanerochaete chrysosporium. Diss Abstr Int B.51(8):3681
    • (1990) Diss Abstr Int B , vol.51 , Issue.8 , pp. 3681
    • Alic, M.M.1
  • 4
    • 0013597411 scopus 로고
    • Genetics and molecular biology of the lignin-degrading Basidiomycete Phanerochaete chrysosporium
    • Bennett J, Lasure L (eds), Academic, New York
    • Alic M, Gold M.(1991) Genetics and molecular biology of the lignin-degrading Basidiomycete Phanerochaete chrysosporium. In: Bennett J, Lasure L (eds) More gene manipulations in fungi. Academic, New York, pp 319-341
    • (1991) More gene manipulations in fungi , pp. 319-341
    • Alic, M.1    Gold, M.2
  • 5
    • 0000783282 scopus 로고
    • Transformation by complementation of an adenine auxotroph of the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Alic M, Kornegay JR et al.(1989) Transformation by complementation of an adenine auxotroph of the lignin-degrading basidiomycete Phanerochaete chrysosporium. Appl Environ Microbiol.55:406-411
    • (1989) Appl Environ Microbiol , vol.55 , pp. 406-411
    • Alic, M.1    Kornegay, J.R.2
  • 6
    • 0025355394 scopus 로고
    • Transformation of Phanerochaete chrysosporium and Neurospora crassa with adenine biosynthetic genes from Schizophyllum commune
    • Alic M, Clark EK et al.(1990) Transformation of Phanerochaete chrysosporium and Neurospora crassa with adenine biosynthetic genes from Schizophyllum commune. Curr Genet.17:305-311
    • (1990) Curr Genet , vol.17 , pp. 305-311
    • Alic, M.1    Clark, E.K.2
  • 7
    • 0025727176 scopus 로고
    • Homologous transformation of the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Alic M, Mayfield MB et al.(1991) Homologous transformation of the lignin-degrading basidiomycete Phanerochaete chrysosporium. Curr Genet.19:491-494
    • (1991) Curr Genet , vol.19 , pp. 491-494
    • Alic, M.1    Mayfield, M.B.2
  • 8
    • 0027732837 scopus 로고
    • Gene replacement in the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Alic M, Akileswaran L et al.(1993) Gene replacement in the lignin-degrading basidiomycete Phanerochaete chrysosporium. Gene.136:307-311
    • (1993) Gene , vol.136 , pp. 307-311
    • Alic, M.1    Akileswaran, L.2
  • 9
    • 0031036975 scopus 로고    scopus 로고
    • Characterization of the gene encoding manganese peroxidase isozyme 3 from Phanerochaete chrysosporium
    • Alic M, Akileswaran L et al.(1997) Characterization of the gene encoding manganese peroxidase isozyme 3 from Phanerochaete chrysosporium. Biochim Biophys Acta.1338(1):1-7
    • (1997) Biochim Biophys Acta , vol.1338 , Issue.1 , pp. 1-7
    • Alic, M.1    Akileswaran, L.2
  • 10
    • 57649156230 scopus 로고    scopus 로고
    • Expression of genes encoding laccase and manganese-dependent peroxidase in the fungus Ceriporiopsis subvermispora is mediated by an ACE1-like copper-fist transcription factor
    • Alvarez JM, Canessa P et al.(2009) Expression of genes encoding laccase and manganese-dependent peroxidase in the fungus Ceriporiopsis subvermispora is mediated by an ACE1-like copper-fist transcription factor. Fungal Genet Biol.46(1):104-111
    • (2009) Fungal Genet Biol , vol.46 , Issue.1 , pp. 104-111
    • Alvarez, J.M.1    Canessa, P.2
  • 11
    • 0031768726 scopus 로고    scopus 로고
    • Oxidative biodegradation of phosphorothiolates by fungal laccase
    • Amitai G, Adani R et al.(1998) Oxidative biodegradation of phosphorothiolates by fungal laccase. FEBS Lett.438(3):195-200
    • (1998) FEBS Lett , vol.438 , Issue.3 , pp. 195-200
    • Amitai, G.1    Adani, R.2
  • 12
    • 0342327383 scopus 로고    scopus 로고
    • Sugar oxidoreductases and veratryl alcohol oxidase as related to lignin degradation
    • Ander P, Marzullo L.(1997) Sugar oxidoreductases and veratryl alcohol oxidase as related to lignin degradation. J Biotechnol.53(2-3):115-131
    • (1997) J Biotechnol , vol.53 , Issue.2-3 , pp. 115-131
    • Ander, P.1    Marzullo, L.2
  • 13
    • 0031006631 scopus 로고    scopus 로고
    • Pyranose 2- oxidase from Phanerochaete chrysosporium-further biochemical characterisation
    • Artolozaga MJ, Kubatova E et al.(1997) Pyranose 2- oxidase from Phanerochaete chrysosporium-further biochemical characterisation. Appl Microbiol Biotechnol.47(5):508-514
    • (1997) Appl Microbiol Biotechnol , vol.47 , Issue.5 , pp. 508-514
    • Artolozaga, M.J.1    Kubatova, E.2
  • 14
    • 0001758653 scopus 로고
    • Purification and characterization of an aryl-alcohol oxidase from the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Asada Y, Watanabe A et al.(1995) Purification and characterization of an aryl-alcohol oxidase from the lignin-degrading basidiomycete Phanerochaete chrysosporium. Biosci Biotech Biochem.59:1339-1341
    • (1995) Biosci Biotech Biochem , vol.59 , pp. 1339-1341
    • Asada, Y.1    Watanabe, A.2
  • 15
    • 0027942301 scopus 로고
    • Oxidative degradation of non-phenolic lignin during lipid peroxidation by fungal manganese peroxidase
    • Bao W, Fukushima Y et al.(1994) Oxidative degradation of non-phenolic lignin during lipid peroxidation by fungal manganese peroxidase. FEBS Lett.354:297-300
    • (1994) FEBS Lett , vol.354 , pp. 297-300
    • Bao, W.1    Fukushima, Y.2
  • 16
    • 0034915954 scopus 로고    scopus 로고
    • Genetic transformation of Trametes versicolor to phleomycin resistance with the dominant selectable marker shble
    • Bartholomew K, Dos Santos G et al.(2001) Genetic transformation of Trametes versicolor to phleomycin resistance with the dominant selectable marker shble. Appl Microbiol Biotechnol.56(1-2):201-204
    • (2001) Appl Microbiol Biotechnol , vol.56 , Issue.1-2 , pp. 201-204
    • Bartholomew, K.1    Dos Santos, G.2
  • 17
    • 0242573404 scopus 로고    scopus 로고
    • Reactive oxygen species and induction of lignin peroxidase in Phanerochaete chrysosporium
    • Belinky PA, Flikshtein N et al.(2003) Reactive oxygen species and induction of lignin peroxidase in Phanerochaete chrysosporium. Appl Environ Microbiol.69(11):6500-6506
    • (2003) Appl Environ Microbiol , vol.69 , Issue.11 , pp. 6500-6506
    • Belinky, P.A.1    Flikshtein, N.2
  • 18
    • 63149135884 scopus 로고    scopus 로고
    • Pharmaceuticals and endocrine disrupting compounds in U. S. drinking water
    • Benotti MJ, Trenholm RA et al.(2009) Pharmaceuticals and endocrine disrupting compounds in U. S. drinking water. Environ Sci Technol.43(3):597-603
    • (2009) Environ Sci Technol , vol.43 , Issue.3 , pp. 597-603
    • Benotti, M.J.1    Trenholm, R.A.2
  • 19
    • 84455173789 scopus 로고    scopus 로고
    • Heterologous expression of Pycnoporus cinnabarinus cellobiose dehydrogenase in Pichia pastoris and involvement in saccharification processes
    • Bey M, Berrin JG et al.(2011) Heterologous expression of Pycnoporus cinnabarinus cellobiose dehydrogenase in Pichia pastoris and involvement in saccharification processes. Microb Cell Fact.10:113
    • (2011) Microb Cell Fact , vol.10 , pp. 113
    • Bey, M.1    Berrin, J.G.2
  • 20
    • 0030022238 scopus 로고    scopus 로고
    • Mineralization of polycyclic aromatic hydrocarbons by the white rot fungus Pleurotus ostreatus
    • Bezalel L, Hadar Y et al.(1996 a) Mineralization of polycyclic aromatic hydrocarbons by the white rot fungus Pleurotus ostreatus. Appl Environ Microbiol.62(1):292-295
    • (1996) Appl Environ Microbiol , vol.62 , Issue.1 , pp. 292-295
    • Bezalel, L.1    Hadar, Y.2
  • 21
    • 0030011872 scopus 로고    scopus 로고
    • Metabolism of phenanthrene by the white rot fungus Pleurotus ostreatus
    • Bezalel L, Hadar Y et al.(1996 b) Metabolism of phenanthrene by the white rot fungus Pleurotus ostreatus. Appl Environ Microbiol.62(7):2547-2553
    • (1996) Appl Environ Microbiol , vol.62 , Issue.7 , pp. 2547-2553
    • Bezalel, L.1    Hadar, Y.2
  • 22
    • 0030861449 scopus 로고    scopus 로고
    • Enzymatic mechanisms involved in phenanthrene degradation by the white rot fungus Pleurotus ostreatus
    • Bezalel L, Hadar Y et al.(1997) Enzymatic mechanisms involved in phenanthrene degradation by the white rot fungus Pleurotus ostreatus. Appl Environ Microbiol.63(7):2495-2501
    • (1997) Appl Environ Microbiol , vol.63 , Issue.7 , pp. 2495-2501
    • Bezalel, L.1    Hadar, Y.2
  • 23
    • 0031689831 scopus 로고    scopus 로고
    • A reporter system for analysis of regulatable promoter functions in the basidiomycete fungus Phanerochaete chrysosporium
    • Birch PR, Sims PF et al.(1998) A reporter system for analysis of regulatable promoter functions in the basidiomycete fungus Phanerochaete chrysosporium. J Appl Microbiol.85(3):417-424
    • (1998) J Appl Microbiol , vol.85 , Issue.3 , pp. 417-424
    • Birch, P.R.1    Sims, P.F.2
  • 24
    • 0026381303 scopus 로고
    • Delignification by wood-decay fungi
    • Blanchette R.(1991) Delignification by wood-decay fungi. Ann Rev Phytopath.29:381-398
    • (1991) Ann Rev Phytopath , vol.29 , pp. 381-398
    • Blanchette, R.1
  • 25
    • 0029901336 scopus 로고    scopus 로고
    • Fluorene oxidation in vivo by Phanerochaete chrysosporium and in vitro during manganese peroxidase-dependent lipid peroxidation
    • Bogan B, Lamar R et al.(1996 a) Fluorene oxidation in vivo by Phanerochaete chrysosporium and in vitro during manganese peroxidase-dependent lipid peroxidation.Appl Environ Microbiol.62:1788-1792
    • (1996) Appl Environ Microbiol , vol.62 , pp. 1788-1792
    • Bogan, B.1    Lamar, R.2
  • 26
    • 0029737394 scopus 로고    scopus 로고
    • Expression of lip genes during growth in soil and oxidation of anthracene by Phanerochaete chrysosporium
    • Bogan BW, Schoenike B et al.(1996 b) Expression of lip genes during growth in soil and oxidation of anthracene by Phanerochaete chrysosporium. Appl Environ Microbiol.62(10):3697-3703
    • (1996) Appl Environ Microbiol , vol.62 , Issue.10 , pp. 3697-3703
    • Bogan, B.W.1    Schoenike, B.2
  • 27
    • 0029902274 scopus 로고    scopus 로고
    • Manganese peroxidase mRNA and enzyme activity levels during bioremediation of polycyclic aromatic hydrocarbon-contaminated soil with Phanerochaete chrysosporium
    • Bogan B, Schoenike B et al.(1996 c) Manganese peroxidase mRNA and enzyme activity levels during bioremediation of polycyclic aromatic hydrocarbon-contaminated soil with Phanerochaete chrysosporium.Appl Environ Microbiol.62:2381-2386
    • (1996) Appl Environ Microbiol , vol.62 , pp. 2381-2386
    • Bogan, B.1    Schoenike, B.2
  • 28
    • 0025099761 scopus 로고
    • Mn(II) regulation of lignin peroxidases and manganese-dependent peroxidase from lignin-degrading white-rot fungi
    • Bonnarme P, Jeffries T.(1990) Mn(II) regulation of lignin peroxidases and manganese-dependent peroxidase from lignin-degrading white-rot fungi. Appl Environ Microbiol.56:210-217
    • (1990) Appl Environ Microbiol , vol.56 , pp. 210-217
    • Bonnarme, P.1    Jeffries, T.2
  • 29
    • 0030734780 scopus 로고    scopus 로고
    • Reactivities of various mediators and laccases with kraft pulp and lignin model compounds
    • Bourbonnais R, Paice MG et al.(1997) Reactivities of various mediators and laccases with kraft pulp and lignin model compounds. Appl Environ Microbiol.63:4627-4632
    • (1997) Appl Environ Microbiol , vol.63 , pp. 4627-4632
    • Bourbonnais, R.1    Paice, M.G.2
  • 30
    • 3042846929 scopus 로고    scopus 로고
    • Electrochemical analysis of the interactions of laccase mediators with lignin model compounds
    • Bourbonnais R, Leech D et al.(1998) Electrochemical analysis of the interactions of laccase mediators with lignin model compounds. Biochim Biophys Acta.1379(3):381-390
    • (1998) Biochim Biophys Acta , vol.1379 , Issue.3 , pp. 381-390
    • Bourbonnais, R.1    Leech, D.2
  • 31
    • 0025362787 scopus 로고
    • Manganese regulates expression of manganese peroxidase by Phanerochaete chrysosporium
    • Brown JA, Glenn JK et al.(1990) Manganese regulates expression of manganese peroxidase by Phanerochaete chrysosporium. J Bacteriol.172(6):3125-3130
    • (1990) J Bacteriol , vol.172 , Issue.6 , pp. 3125-3130
    • Brown, J.A.1    Glenn, J.K.2
  • 32
    • 0025861493 scopus 로고
    • Manganese peroxidase gene transcription in Phanerochaete chrysosporium: Activation by manganese
    • Brown J, Alic M et al.(1991) Manganese peroxidase gene transcription in Phanerochaete chrysosporium: activation by manganese. J Bacteriol.173:4101-4106
    • (1991) J Bacteriol , vol.173 , pp. 4101-4106
    • Brown, J.1    Alic, M.2
  • 33
    • 0027521768 scopus 로고
    • Heat shock induction of manganese peroxidase gene transcription in Phanerochaete chrysosporium
    • Brown J, Li D et al.(1993) Heat shock induction of manganese peroxidase gene transcription in Phanerochaete chrysosporium. Appl Environ Microbiol.59:4295-4299
    • (1993) Appl Environ Microbiol , vol.59 , pp. 4295-4299
    • Brown, J.1    Li, D.2
  • 34
    • 0024575412 scopus 로고
    • Biodegradation of polycyclic hydrocarbons by Phanerochaete chrysosporium
    • Bumpus JA.(1989) Biodegradation of polycyclic hydrocarbons by Phanerochaete chrysosporium. Appl Environ Microbiol.55(1):154-158
    • (1989) Appl Environ Microbiol , vol.55 , Issue.1 , pp. 154-158
    • Bumpus, J.A.1
  • 35
    • 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 et al.(1999) 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(15):10324-10330
    • (1999) J Biol Chem , vol.274 , Issue.15 , pp. 10324-10330
    • Camarero, S.1    Sarkar, S.2
  • 36
    • 17444419429 scopus 로고    scopus 로고
    • Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes
    • Camarero S, Ibarra D et al.(2005) Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes. Appl Environ Microbiol.71(4):1775-1784
    • (2005) Appl Environ Microbiol , vol.71 , Issue.4 , pp. 1775-1784
    • Camarero, S.1    Ibarra, D.2
  • 37
    • 0029994409 scopus 로고    scopus 로고
    • Initial oxidative and subsequent conjugative metabolites produced during the metabolism of phenanthrene by fungi
    • Casillas RP, Crow SA Jr et al.(1996) Initial oxidative and subsequent conjugative metabolites produced during the metabolism of phenanthrene by fungi. J Ind Microbiol.16(4):205-215
    • (1996) J Ind Microbiol , vol.16 , Issue.4 , pp. 205-215
    • Casillas, R.P.1    Crow Jr, S.A.2
  • 38
    • 84864098084 scopus 로고    scopus 로고
    • Transcriptional and enzymatic profiling of Pleurotus ostreatus laccase genes in submerged and solid-state fermentation cultures
    • Castanera R, Perez G et al.(2012) Transcriptional and enzymatic profiling of Pleurotus ostreatus laccase genes in submerged and solid-state fermentation cultures. Appl Environ Microbiol.78(11):4037-4045
    • (2012) Appl Environ Microbiol , vol.78 , Issue.11 , pp. 4037-4045
    • Castanera, R.1    Perez, G.2
  • 39
    • 77955561065 scopus 로고    scopus 로고
    • Cytochrome P450 monooxygenases involved in anthracene metabolism by the white-rot basidiomycete Phanerochaete chrysosporium
    • Chigu NL, Hirosue S et al.(2010) Cytochrome P450 monooxygenases involved in anthracene metabolism by the white-rot basidiomycete Phanerochaete chrysosporium. Appl Microbiol Biotechnol.87(5):1907-1916
    • (2010) Appl Microbiol Biotechnol , vol.87 , Issue.5 , pp. 1907-1916
    • Chigu, N.L.1    Hirosue, S.2
  • 40
    • 0035214846 scopus 로고    scopus 로고
    • Transcript and activity levels of different Pleurotus ostreatus peroxidases are differentially affected by Mn2+
    • Cohen R, Hadar Y et al.(2001) Transcript and activity levels of different Pleurotus ostreatus peroxidases are differentially affected by Mn2+. Environ Microbiol.3(5):312-322
    • (2001) Environ Microbiol , vol.3 , Issue.5 , pp. 312-322
    • Cohen, R.1    Hadar, Y.2
  • 41
    • 1842854104 scopus 로고    scopus 로고
    • Mn2+ alters peroxidase profiles and lignin degradation by the white-rot fungus Pleurotus ostreatus under different nutritional and growth conditions
    • Cohen R, Persky L et al.(2002 a) Mn2+ alters peroxidase profiles and lignin degradation by the white-rot fungus Pleurotus ostreatus under different nutritional and growth conditions. Appl Biochem Biotechnol.102-103(1-6):415-429
    • (2002) Appl Biochem Biotechnol , vol.102-103 , Issue.1-6 , pp. 415-429
    • Cohen, R.1    Persky, L.2
  • 42
    • 0036015795 scopus 로고    scopus 로고
    • Lignocellulose affects Mn2+ regulation of peroxidase transcript levels in solid-state cultures of Pleurotus ostreatus
    • Cohen R, Yarden O et al.(2002 b) Lignocellulose affects Mn2+ regulation of peroxidase transcript levels in solid-state cultures of Pleurotus ostreatus. Appl Environ Microbiol.68(6):3156-3158
    • (2002) Appl Environ Microbiol , vol.68 , Issue.6 , pp. 3156-3158
    • Cohen, R.1    Yarden, O.2
  • 43
    • 0027369584 scopus 로고
    • Characterization and structural analysis of the laccase I gene from the newly isolated ligninolytic basidiomycete PM1 (CECT 2971)
    • Coll P, Tabernero C et al.(1993) Characterization and structural analysis of the laccase I gene from the newly isolated ligninolytic basidiomycete PM1 (CECT 2971). Appl EnvironMicrobiol.59:4129-4135
    • (1993) Appl EnvironMicrobiol , vol.59 , pp. 4129-4135
    • Coll, P.1    Tabernero, C.2
  • 44
    • 0032984977 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA encoding a novel extracellular peroxidase from Trametes versicolor
    • Collins PJ, O’Brien MM et al.(1999) Cloning and characterization of a cDNA encoding a novel extracellular peroxidase from Trametes versicolor. Appl Environ Microbiol.65(3):1343-1347
    • (1999) Appl Environ Microbiol , vol.65 , Issue.3 , pp. 1343-1347
    • Collins, P.J.1    O’Brien, M.M.2
  • 45
    • 0033931925 scopus 로고    scopus 로고
    • Studies on the production of fungal peroxidases in Aspergillus niger
    • Conesa A, van den Hondel CA et al.(2000) Studies on the production of fungal peroxidases in Aspergillus niger. Appl Environ Microbiol.66(7):3016-3023
    • (2000) Appl Environ Microbiol , vol.66 , Issue.7 , pp. 3016-3023
    • Conesa, A.1    Van Den Hondel, C.A.2
  • 46
    • 84856508014 scopus 로고    scopus 로고
    • Heterologous expression of manganese peroxidase in Aspergillus niger and its effect on phenanthrene removal from soil
    • Cortes-Espinosa DV, Absalon AE et al.(2011) Heterologous expression of manganese peroxidase in Aspergillus niger and its effect on phenanthrene removal from soil. J Mol Microbiol Biotechnol.21(3-4):120-129
    • (2011) J Mol Microbiol Biotechnol , vol.21 , Issue.3-4 , pp. 120-129
    • Cortes-Espinosa, D.V.1    Absalon, A.E.2
  • 48
    • 33845916930 scopus 로고    scopus 로고
    • Molecular genetics of lignin-degrading fungi and their application in organopollutant degradation
    • Kempken F (ed), Springer, Berlin
    • Cullen D.(2002) Molecular genetics of lignin-degrading fungi and their application in organopollutant degradation. In: Kempken F (ed) The Mycota, vol XI. Springer, Berlin, pp 71-90
    • (2002) The Mycota, vol XI , pp. 71-90
    • Cullen, D.1
  • 49
    • 20444447321 scopus 로고    scopus 로고
    • Enzymology and molecular biology of lignin degradation
    • Brambl R, Marzulf GA (eds), Springer, Berlin
    • Cullen D, Kersten PJ.(2004) Enzymology and molecular biology of lignin degradation. In: Brambl R, Marzulf GA (eds) The Mycota III biochemistry and molecular biology. Springer, Berlin, pp 249-273
    • (2004) The Mycota III biochemistry and molecular biology , pp. 249-273
    • Cullen, D.1    Kersten, P.J.2
  • 50
    • 84855464743 scopus 로고    scopus 로고
    • Metatranscriptomics reveals the diversity of genes expressed by eukaryotes in forest soils
    • Damon C, Lehembre F et al.(2012) Metatranscriptomics reveals the diversity of genes expressed by eukaryotes in forest soils. PLoS One.7(1):e28967
    • (2012) PLoS One , vol.7 , Issue.1
    • Damon, C.1    Lehembre, F.2
  • 51
    • 0028340896 scopus 로고
    • Pyranose oxidase, a major source of H2O2 during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida
    • Daniel G, Volc J et al.(1994) Pyranose oxidase, a major source of H2O2 during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida. Appl Environ Microbiol.60:2524-2532
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2524-2532
    • Daniel, G.1    Volc, J.2
  • 52
    • 35148832513 scopus 로고    scopus 로고
    • Characteristics of Gloeophyllum trabeum alcohol oxidase, an extracellular source of H2O2 in brown rot decay of wood
    • Daniel G, Volc J et al.(2007) Characteristics of Gloeophyllum trabeum alcohol oxidase, an extracellular source of H2O2 in brown rot decay of wood. Appl Environ Microbiol.73(19):6241-6253
    • (2007) Appl Environ Microbiol , vol.73 , Issue.19 , pp. 6241-6253
    • Daniel, G.1    Volc, J.2
  • 53
    • 0025869075 scopus 로고
    • Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay
    • Datta A, Bettermann A et al.(1991) Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay. Appl Environ Microbiol.57:1453-1460
    • (1991) Appl Environ Microbiol , vol.57 , pp. 1453-1460
    • Datta, A.1    Bettermann, A.2
  • 54
    • 77955241103 scopus 로고    scopus 로고
    • Inactivation of ku80 in the mushroom-forming fungus Schizophyllum commune increases the relative incidence of homologous recombination
    • De Jong JF, Ohm RA et al.(2010) Inactivation of ku80 in the mushroom-forming fungus Schizophyllum commune increases the relative incidence of homologous recombination. FEMS Microbiol Lett.310(1):91-95
    • (2010) FEMS Microbiol Lett , vol.310 , Issue.1 , pp. 91-95
    • De Jong, J.F.1    Ohm, R.A.2
  • 55
    • 8144219533 scopus 로고    scopus 로고
    • Pyranose 2- oxidase from Phanerochaete chrysosporium: Isolation from solid substrate, protein purification, and characterization of gene structure and regulation
    • De Koker TH, Mozuch MD et al.(2004) Pyranose 2- oxidase from Phanerochaete chrysosporium: isolation from solid substrate, protein purification, and characterization of gene structure and regulation. Appl Environ Microbiol.70:5794-5800
    • (2004) Appl Environ Microbiol , vol.70 , pp. 5794-5800
    • De Koker, T.H.1    Mozuch, M.D.2
  • 56
    • 84865739463 scopus 로고    scopus 로고
    • Comparative metatranscriptomics reveals widespread community responses during phenanthrene degradation in soil
    • de Menezes A, Clipson N et al.(2012) Comparative metatranscriptomics reveals widespread community responses during phenanthrene degradation in soil. Environ Microbiol.14(9):2577-2588
    • (2012) Environ Microbiol , vol.14 , Issue.9 , pp. 2577-2588
    • de Menezes, A.1    Clipson, N.2
  • 57
    • 69849114831 scopus 로고    scopus 로고
    • Gene cloning and heterologous expression of pyranose 2-oxidase from the brown-rot fungus, Gloeophyllum trabeum
    • Dietrich D, Crooks C.(2009) Gene cloning and heterologous expression of pyranose 2-oxidase from the brown-rot fungus, Gloeophyllum trabeum. Biotechnol Lett.31(8):1223-1228
    • (2009) Biotechnol Lett , vol.31 , Issue.8 , pp. 1223-1228
    • Dietrich, D.1    Crooks, C.2
  • 58
    • 28344457845 scopus 로고    scopus 로고
    • Microarray-based global differential expression profiling of P450 monooxygenases and regulatory proteins for signal transduction pathways in the white rot fungus Phanerochaete chrysosporium
    • Doddapaneni H, Yadav JS.(2005) Microarray-based global differential expression profiling of P450 monooxygenases and regulatory proteins for signal transduction pathways in the white rot fungus Phanerochaete chrysosporium. Mol Genet Genomics.274:454-466
    • (2005) Mol Genet Genomics , vol.274 , pp. 454-466
    • Doddapaneni, H.1    Yadav, J.S.2
  • 59
    • 0029963241 scopus 로고    scopus 로고
    • Expression of lignin peroxidase H8 in Escherichia coli: Folding and activation of the recombinant enzyme with Ca2+ and haem
    • Doyle WA, Smith AT.(1996) Expression of lignin peroxidase H8 in Escherichia coli: folding and activation of the recombinant enzyme with Ca2+ and haem. Biochem J.315(Pt 1):15-19
    • (1996) Biochem J , vol.315 , pp. 15-19
    • Doyle, W.A.1    Smith, A.T.2
  • 60
    • 0032515940 scopus 로고    scopus 로고
    • Cloning and sequencing of a gene encoding cellobiose dehydrogenase from Trametes versicolor
    • Dumonceaux TJ, Bartholomew KA et al.(1998) Cloning and sequencing of a gene encoding cellobiose dehydrogenase from Trametes versicolor. Gene.210:211-219
    • (1998) Gene , vol.210 , pp. 211-219
    • Dumonceaux, T.J.1    Bartholomew, K.A.2
  • 61
    • 0035813522 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase is essential for wood invasion and nonessential for kraft pulp delignification by Trametes versicolor
    • Dumonceaux T, Bartholomew K et al.(2001) Cellobiose dehydrogenase is essential for wood invasion and nonessential for kraft pulp delignification by Trametes versicolor. EnzymeMicrob Technol.29:478-489
    • (2001) EnzymeMicrob Technol , vol.29 , pp. 478-489
    • Dumonceaux, T.1    Bartholomew, K.2
  • 62
    • 79961228770 scopus 로고    scopus 로고
    • The plant cell walldecomposing machinery underlies the functional diversity of forest fungi
    • Eastwood DC, Floudas D et al.(2011) The plant cell walldecomposing machinery underlies the functional diversity of forest fungi. Science.333(6043):762-765
    • (2011) Science , vol.333 , Issue.6043 , pp. 762-765
    • Eastwood, D.C.1    Floudas, D.2
  • 63
    • 0030570825 scopus 로고    scopus 로고
    • A fungalmetabolitemediates degradation of non-phenolic lignin structures and synthetic lignin by laccase
    • Eggert C, Temp U et al.(1996) A fungalmetabolitemediates degradation of non-phenolic lignin structures and synthetic lignin by laccase. FEBS Lett.391:144-148
    • (1996) FEBS Lett , vol.391 , pp. 144-148
    • Eggert, C.1    Temp, U.2
  • 64
    • 58149102783 scopus 로고    scopus 로고
    • Effect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts
    • Eibes GM, Lu-Chau TA et al.(2009) Effect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts. Bioprocess Biosyst Eng.32(1):129-134
    • (2009) Bioprocess Biosyst Eng , vol.32 , Issue.1 , pp. 129-134
    • Eibes, G.M.1    Lu-Chau, T.A.2
  • 65
    • 0032826602 scopus 로고    scopus 로고
    • Preparation and crossing of basidiospore-derived monokaryons-a useful tool for obtaining laccase and other ligninolytic enzyme higher- producing dikaryotic strains of Pleurotus ostreatus
    • Eichlerova I, Homolka L.(1999) Preparation and crossing of basidiospore-derived monokaryons-a useful tool for obtaining laccase and other ligninolytic enzyme higher- producing dikaryotic strains of Pleurotus ostreatus. Antonie Van Leeuwenhoek.75(4):321-327
    • (1999) Antonie Van Leeuwenhoek , vol.75 , Issue.4 , pp. 321-327
    • Eichlerova, I.1    Homolka, L.2
  • 66
    • 0345910192 scopus 로고    scopus 로고
    • Variability of ligninolytic enzyme activities in basidiospore isolates of the fungus Pleurotus ostreatus in comparison with that of protoplast-derived isolates
    • Eichlerova-Volakova I, Homolka L.(1997) Variability of ligninolytic enzyme activities in basidiospore isolates of the fungus Pleurotus ostreatus in comparison with that of protoplast-derived isolates. Folia Microbiol.42(6):583-588
    • (1997) Folia Microbiol , vol.42 , Issue.6 , pp. 583-588
    • Eichlerova-Volakova, I.1    Homolka, L.2
  • 68
    • 84859466995 scopus 로고    scopus 로고
    • Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis
    • Fernandez-Fueyo E, Ruiz-Duenas FJ et al.(2012) Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis. Proc Natl Acad Sci USA.109(14):5458-5463
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.14 , pp. 5458-5463
    • Fernandez-Fueyo, E.1    Ruiz-Duenas, F.J.2
  • 69
    • 84862977387 scopus 로고    scopus 로고
    • The Paleozoic origin of enzymatic lignin decomposition reconstructed from 31 fungal genomes
    • Floudas D, Binder M et al.(2012) The Paleozoic origin of enzymatic lignin decomposition reconstructed from 31 fungal genomes. Science.336(6089):1715-1719
    • (2012) Science , vol.336 , Issue.6089 , pp. 1715-1719
    • Floudas, D.1    Binder, M.2
  • 70
    • 36249025731 scopus 로고    scopus 로고
    • Fungal inoculum properties: Extracellular enzyme expression and pentachlorophenol removal by New Zealand trametes species in contaminated field soils
    • Ford CI, Walter M et al.(2007 a) Fungal inoculum properties:extracellular enzyme expression and pentachlorophenol removal by New Zealand trametes species in contaminated field soils. J Environ Qual.36(6):1749-1759
    • (2007) J Environ Qual , vol.36 , Issue.6 , pp. 1749-1759
    • Ford, C.I.1    Walter, M.2
  • 71
    • 36248949697 scopus 로고    scopus 로고
    • Fungal inoculum properties: Extracellular enzyme expression and pentachlorophenol removal in highly contaminated field soils
    • Ford CI, Walter M et al.(2007 b) Fungal inoculum properties:extracellular enzyme expression and pentachlorophenol removal in highly contaminated field soils. J Environ Qual.36(6):1599-1608
    • (2007) J Environ Qual , vol.36 , Issue.6 , pp. 1599-1608
    • Ford, C.I.1    Walter, M.2
  • 72
    • 0028897509 scopus 로고
    • Laccase component of the Ceriporiopsis subvermispora lignin-degrading system
    • Fukushima Y, Kirk TK.(1995) Laccase component of the Ceriporiopsis subvermispora lignin-degrading system. Appl Environ Microbiol.61:872-876
    • (1995) Appl Environ Microbiol , vol.61 , pp. 872-876
    • Fukushima, Y.1    Kirk, T.K.2
  • 73
    • 71049133607 scopus 로고    scopus 로고
    • Remediation of soils contaminated with polycyclic aromatic hydrocarbons (PAHs)
    • Gan S, Lau EV et al.(2009) Remediation of soils contaminated with polycyclic aromatic hydrocarbons (PAHs). J Hazard Mater.172(2-3):532-549
    • (2009) J Hazard Mater , vol.172 , Issue.2-3 , pp. 532-549
    • Gan, S.1    Lau, E.V.2
  • 74
    • 84055213590 scopus 로고    scopus 로고
    • Directed evolution of a temperature-, peroxide- and alkaline pH-tolerant versatile peroxidase
    • Garcia-Ruiz E, Gonzalez-Perez D et al.(2012) Directed evolution of a temperature-, peroxide- and alkaline pH-tolerant versatile peroxidase. Biochem J.441(1):487-498
    • (2012) Biochem J , vol.441 , Issue.1 , pp. 487-498
    • Garcia-Ruiz, E.1    Gonzalez-Perez, D.2
  • 75
    • 0028595597 scopus 로고
    • Establishment of genetic linkage by allele-specific polymerase chain reaction:Application to the lignin peroxidase gene family of Phanerochaete chrysosporium
    • Gaskell J, Stewart P et al.(1994) Establishment of genetic linkage by allele-specific polymerase chain reaction:application to the lignin peroxidase gene family of Phanerochaete chrysosporium. Biotechnology.12:1372-1375
    • (1994) Biotechnology , vol.12 , pp. 1372-1375
    • Gaskell, J.1    Stewart, P.2
  • 76
    • 77952526063 scopus 로고    scopus 로고
    • Quantitative evaluation of tracers for quantification of wastewater contamination of potable water sources
    • Gasser G, Rona M et al.(2010) Quantitative evaluation of tracers for quantification of wastewater contamination of potable water sources. Environ Sci Technol.44(10):3919-3925
    • (2010) Environ Sci Technol , vol.44 , Issue.10 , pp. 3919-3925
    • Gasser, G.1    Rona, M.2
  • 77
    • 0024652461 scopus 로고
    • Degradation of fluorene in soil by fungus Phanerochaete chrysosporium
    • George EJ, Neufield RD.(1989) Degradation of fluorene in soil by fungus Phanerochaete chrysosporium. Biotechnol Bioengineer.33:1306-1310
    • (1989) Biotechnol Bioengineer , vol.33 , pp. 1306-1310
    • George, E.J.1    Neufield, R.D.2
  • 78
    • 0028318272 scopus 로고
    • A histone promoter for expression of a phleomycin-resistance gene in Phanerochaete chrysosporium
    • Gessner M, Raeder U.(1994) A histone promoter for expression of a phleomycin-resistance gene in Phanerochaete chrysosporium. Gene.142:237-241
    • (1994) Gene , vol.142 , pp. 237-241
    • Gessner, M.1    Raeder, U.2
  • 79
    • 0030803571 scopus 로고    scopus 로고
    • Truncated-gene reporter system for studying the regulation of manganese peroxidase expression
    • Gettemy JM, Li D et al.(1997) Truncated-gene reporter system for studying the regulation of manganese peroxidase expression. Curr Genet.31(6):519-524
    • (1997) Curr Genet , vol.31 , Issue.6 , pp. 519-524
    • Gettemy, J.M.1    Li, D.2
  • 80
    • 0031890797 scopus 로고    scopus 로고
    • Reverse transcription-PCR analysis of the regulation of the manganese peroxidase gene family
    • Gettemy JM, Ma B et al.(1998) Reverse transcription-PCR analysis of the regulation of the manganese peroxidase gene family. Appl Environ Microbiol.64(2):569-574
    • (1998) Appl Environ Microbiol , vol.64 , Issue.2 , pp. 569-574
    • Gettemy, J.M.1    Ma, B.2
  • 81
    • 0033179031 scopus 로고    scopus 로고
    • Protein and gene structure of a blue laccase from Pleurotus ostreatus1
    • Giardina P, Palmieri G et al.(1999) Protein and gene structure of a blue laccase from Pleurotus ostreatus1. Biochem J.341(Pt 3):655-663
    • (1999) Biochem J , vol.341 , pp. 655-663
    • Giardina, P.1    Palmieri, G.2
  • 82
    • 75849159740 scopus 로고    scopus 로고
    • Laccases: A neverending story
    • Giardina P, Faraco V et al.(2010) Laccases: a neverending story. Cell Mol Life Sci.67(3):369-385
    • (2010) Cell Mol Life Sci , vol.67 , Issue.3 , pp. 369-385
    • Giardina, P.1    Faraco, V.2
  • 83
    • 0020568668 scopus 로고
    • Decolorization of several polymeric dyes by the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Glenn JK, Gold MH.(1983) Decolorization of several polymeric dyes by the lignin-degrading basidiomycete Phanerochaete chrysosporium. Appl Environ Microbiol.45(6):1741-1747
    • (1983) Appl Environ Microbiol , vol.45 , Issue.6 , pp. 1741-1747
    • Glenn, J.K.1    Gold, M.H.2
  • 84
    • 0021101692 scopus 로고
    • An extracellular H202-requiring enzyme preparation involved in lignin biodegradation by the white-rot basidiomycete Phanerochaete chrysosporium
    • Glenn JK, Morgan MA et al.(1983) An extracellular H202-requiring enzyme preparation involved in lignin biodegradation by the white-rot basidiomycete Phanerochaete chrysosporium. Biochem Biophys Res Comm.114:1077-1083
    • (1983) Biochem Biophys Res Comm , vol.114 , pp. 1077-1083
    • Glenn, J.K.1    Morgan, M.A.2
  • 85
    • 0022965641 scopus 로고
    • Mn(II) oxidation is the principal function of the extracellular Mnperoxidase from Phanerochaete chrysosporium
    • Glenn JK, Akileswaran L et al.(1986) Mn(II) oxidation is the principal function of the extracellular Mnperoxidase from Phanerochaete chrysosporium. Arch Biochem Biophys.251:688-696
    • (1986) Arch Biochem Biophys , vol.251 , pp. 688-696
    • Glenn, J.K.1    Akileswaran, L.2
  • 86
    • 0025119879 scopus 로고
    • Characterization of a gene encoding a manganese peroxidase from Phanerochaete chrysosporium
    • Godfrey BJ, Mayfield MB et al.(1990) Characterization of a gene encoding a manganese peroxidase from Phanerochaete chrysosporium. Gene.93(1):119-124
    • (1990) Gene , vol.93 , Issue.1 , pp. 119-124
    • Godfrey, B.J.1    Mayfield, M.B.2
  • 87
    • 0028268135 scopus 로고
    • A reporter gene construct for studying the regulation of manganese peroxidase gene expression
    • Godfrey B, Akileswaran L et al.(1994) A reporter gene construct for studying the regulation of manganese peroxidase gene expression. Appl Environ Microbiol.60:1353-2358
    • (1994) Appl Environ Microbiol , vol.60 , pp. 1353-2358
    • Godfrey, B.1    Akileswaran, L.2
  • 88
    • 80051761213 scopus 로고    scopus 로고
    • Transformation of the recalcitrant pharmaceutical compound carbamazepine by Pleurotus ostreatus: Role of cytochrome P450 monooxygenase and manganese peroxidase
    • Golan-Rozen N, Chefetz B et al.(2011) Transformation of the recalcitrant pharmaceutical compound carbamazepine by Pleurotus ostreatus: role of cytochrome P450 monooxygenase and manganese peroxidase. Environ Sci Technol.45(16):6800-6805
    • (2011) Environ Sci Technol , vol.45 , Issue.16 , pp. 6800-6805
    • Golan-Rozen, N.1    Chefetz, B.2
  • 89
    • 0021519023 scopus 로고
    • Purification and characterization of an extracellular H2O2-requiring diarylpropane oxygenase from the white rot basidiomycete, Phanerochaete chrysosporium
    • Gold MH, Kuwahara M et al.(1984) Purification and characterization of an extracellular H2O2-requiring diarylpropane oxygenase from the white rot basidiomycete, Phanerochaete chrysosporium. Archives Biochem Biophys.234:353-362
    • (1984) Archives Biochem Biophys , vol.234 , pp. 353-362
    • Gold, M.H.1    Kuwahara, M.2
  • 90
    • 79955828431 scopus 로고    scopus 로고
    • Potential of Trametes trogii culture fluids and its purified laccase for the decolorization of different types of recalcitrant dyes without the addition of redox mediators
    • Grassi E, Scodeller P et al.(2011) Potential of Trametes trogii culture fluids and its purified laccase for the decolorization of different types of recalcitrant dyes without the addition of redox mediators. Biodeterior Biodegradation.65:635-643
    • (2011) Biodeterior Biodegradation , vol.65 , pp. 635-643
    • Grassi, E.1    Scodeller, P.2
  • 91
    • 84862174834 scopus 로고    scopus 로고
    • The genome portal of the Department of Energy Joint Genome Institute
    • Database issue
    • Grigoriev IV, Nordberg H et al.(2012) The genome portal of the Department of Energy Joint Genome Institute. Nucleic Acids Res.40(Database issue):D26-D32
    • (2012) Nucleic Acids Res , vol.40 , pp. D26-D32
    • Grigoriev, I.V.1    Nordberg, H.2
  • 92
    • 54849406129 scopus 로고    scopus 로고
    • Purification of recombinant laccase from Trametes versicolor in Pichia methanolica and its use for the decolorization of anthraquinone dye
    • Guo M, Lu F et al.(2008) Purification of recombinant laccase from Trametes versicolor in Pichia methanolica and its use for the decolorization of anthraquinone dye. Biotechnol Lett.30(12):2091-2096
    • (2008) Biotechnol Lett , vol.30 , Issue.12 , pp. 2091-2096
    • Guo, M.1    Lu, F.2
  • 93
    • 80052745488 scopus 로고    scopus 로고
    • Regioselective oxygenation of fatty acids, fatty alcohols and other aliphatic compounds by a basidiomycete heme-thiolate peroxidase
    • Gutierrez A, Babot ED et al.(2011) Regioselective oxygenation of fatty acids, fatty alcohols and other aliphatic compounds by a basidiomycete heme-thiolate peroxidase. Arch Biochem Biophys.514(1-2):33-43
    • (2011) Arch Biochem Biophys , vol.514 , Issue.1-2 , pp. 33-43
    • Gutierrez, A.1    Babot, E.D.2
  • 94
    • 0034650750 scopus 로고    scopus 로고
    • A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase
    • Hallberg BM, Bergfors T et al.(2000) A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase. Structure Fold Des.8(1):79-88
    • (2000) Structure Fold Des , vol.8 , Issue.1 , pp. 79-88
    • Hallberg, B.M.1    Bergfors, T.2
  • 95
    • 0029132865 scopus 로고
    • Mechanisms for polycyclic aromatic hydrocarbon degradation by ligninolytic fungi
    • Hammel KE.(1995 a) Mechanisms for polycyclic aromatic hydrocarbon degradation by ligninolytic fungi. Environ Health Perspect.103(Suppl 5):41-43
    • (1995) Environ Health Perspect , vol.103
    • Hammel, K.E.1
  • 97
    • 43849099090 scopus 로고    scopus 로고
    • Role of fungal peroxidases in biological ligninolysis
    • Hammel KE, Cullen D.(2008) Role of fungal peroxidases in biological ligninolysis. Curr Opin Plant Biol.11(3):349-355
    • (2008) Curr Opin Plant Biol , vol.11 , Issue.3 , pp. 349-355
    • Hammel, K.E.1    Cullen, D.2
  • 98
    • 0023805713 scopus 로고
    • The oxidative 4- dechlorination of polychlorinated phenols is catalyzed by extracellular fungal lignin peroxidases
    • Hammel KE, Tardone PJ.(1988) The oxidative 4- dechlorination of polychlorinated phenols is catalyzed by extracellular fungal lignin peroxidases. Biochemistry.27:6563-6568
    • (1988) Biochemistry , vol.27 , pp. 6563-6568
    • Hammel, K.E.1    Tardone, P.J.2
  • 99
    • 0022968235 scopus 로고
    • Oxidation of polycyclic hydrocarbons and dibenzo[p]-dioxins by Phanerochaete chrysosporium ligninase
    • Hammel KE, Kalyanaraman B et al.(1986 a) Oxidation of polycyclic hydrocarbons and dibenzo[p]-dioxins by Phanerochaete chrysosporium ligninase.J Biol Chem.261:16948-16952
    • (1986) J Biol Chem , vol.261 , pp. 16948-16952
    • Hammel, K.E.1    Kalyanaraman, B.2
  • 100
    • 0142020040 scopus 로고
    • Substrate free radicals are intermediates in ligninase catalysis
    • Hammel KE, Kalyanaraman B et al.(1986 b) Substrate free radicals are intermediates in ligninase catalysis.Proc Natl Acad Sci USA.83:3808-3812
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3808-3812
    • Hammel, K.E.1    Kalyanaraman, B.2
  • 101
    • 0026747122 scopus 로고
    • Oxidative degradation of phenanthrene by the ligninolytic fungus Phanerochaete chrysosporium
    • Hammel KE, Gai WZ et al.(1992) Oxidative degradation of phenanthrene by the ligninolytic fungus Phanerochaete chrysosporium. Appl Environ Microbiol.58(6):1832-1838
    • (1992) Appl Environ Microbiol , vol.58 , Issue.6 , pp. 1832-1838
    • Hammel, K.E.1    Gai, W.Z.2
  • 102
    • 67649770254 scopus 로고    scopus 로고
    • Biodegradation aspects of polycyclic aromatic hydrocarbons (PAHs): A review
    • Haritash AK, Kaushik CP.(2009) Biodegradation aspects of polycyclic aromatic hydrocarbons (PAHs): a review. J Hazard Mater.169(1-3):1-15
    • (2009) J Hazard Mater , vol.169 , Issue.1-3 , pp. 1-15
    • Haritash, A.K.1    Kaushik, C.P.2
  • 103
    • 77950948151 scopus 로고    scopus 로고
    • Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: Structure and function of a large, enigmatic family
    • Harris PV, Welner D et al.(2010) Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: structure and function of a large, enigmatic family. Biochemistry.49(15):3305-3316
    • (2010) Biochemistry , vol.49 , Issue.15 , pp. 3305-3316
    • Harris, P.V.1    Welner, D.2
  • 104
    • 0021906999 scopus 로고
    • Single-electron transfer processes and the reaction mechanism of enzymic degradation of lignin
    • Harvey PJ, Schoemaker HE et al.(1985) Single-electron transfer processes and the reaction mechanism of enzymic degradation of lignin. FEBS Lett.183:13-16
    • (1985) FEBS Lett , vol.183 , pp. 13-16
    • Harvey, P.J.1    Schoemaker, H.E.2
  • 105
    • 77954532592 scopus 로고    scopus 로고
    • Elimination of carbamazepine by repeated treatment with laccase in the presence of 1-hydroxybenzotriazole
    • Hata T, Shintate H et al.(2010) Elimination of carbamazepine by repeated treatment with laccase in the presence of 1-hydroxybenzotriazole. J Hazard Mater.181(1-3):1175-1178
    • (2010) J Hazard Mater , vol.181 , Issue.1-3 , pp. 1175-1178
    • Hata, T.1    Shintate, H.2
  • 106
    • 0037052865 scopus 로고    scopus 로고
    • Occurrence, fate, and removal of pharmaceutical residues in the aquatic environment:A review of recent research data
    • Heberer T.(2002) Occurrence, fate, and removal of pharmaceutical residues in the aquatic environment:a review of recent research data. Toxicol Lett.131(1-2):5-17
    • (2002) Toxicol Lett , vol.131 , Issue.1-2 , pp. 5-17
    • Heberer, T.1
  • 107
    • 0032145444 scopus 로고    scopus 로고
    • Purification and characterization of peroxidases from the dyedecolorizing fungus Bjerkandera adusta
    • Heinfling A, Martinez MJ et al.(1998 a) Purification and characterization of peroxidases from the dyedecolorizing fungus Bjerkandera adusta. FEMS Microbiol Lett.165(1):43-50
    • (1998) FEMS Microbiol Lett , vol.165 , Issue.1 , pp. 43-50
    • Heinfling, A.1    Martinez, M.J.2
  • 108
    • 0344734070 scopus 로고    scopus 로고
    • Transformation of industrial dyes by manganese peroxidases from Bjerkandera adusta and Pleurotus eryngii in a manganese-independent reaction
    • Heinfling A, Martinez MJ et al.(1998 b) Transformation of industrial dyes by manganese peroxidases from Bjerkandera adusta and Pleurotus eryngii in a manganese-independent reaction. Appl Environ Microbiol.64(8):2788-2793
    • (1998) Appl Environ Microbiol , vol.64 , Issue.8 , pp. 2788-2793
    • Heinfling, A.1    Martinez, M.J.2
  • 109
    • 0034629232 scopus 로고    scopus 로고
    • A critical review of cellobiose dehydrogenases
    • Henriksson G, Johansson G et al.(2000) A critical review of cellobiose dehydrogenases. J Biotechnol.78(2):93-113
    • (2000) J Biotechnol , vol.78 , Issue.2 , pp. 93-113
    • Henriksson, G.1    Johansson, G.2
  • 110
    • 84857914934 scopus 로고    scopus 로고
    • Fungal aryl-alcohol oxidase: A peroxide-producing flavoenzyme involved in lignin degradation
    • Hernandez-Ortega A, Ferreira P et al.(2012) Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation. Appl Microbiol Biotechnol.93(4):1395-1410
    • (2012) Appl Microbiol Biotechnol , vol.93 , Issue.4 , pp. 1395-1410
    • Hernandez-Ortega, A.1    Ferreira, P.2
  • 111
    • 0028169897 scopus 로고
    • Direct 1H NMR evidence for conversion of beta-D-cellobiose to cellobionolactone by cellobiose dehydrogenase from Phanerochaete chrysosporium
    • Higham CW, Gordon-Smith D et al.(1994) Direct 1H NMR evidence for conversion of beta-D-cellobiose to cellobionolactone by cellobiose dehydrogenase from Phanerochaete chrysosporium. FEBS Lett.351(1):128-132
    • (1994) FEBS Lett , vol.351 , Issue.1 , pp. 128-132
    • Higham, C.W.1    Gordon-Smith, D.2
  • 112
    • 0026331063 scopus 로고
    • Degradation of xenobiotics by white rot fungi
    • Higson FK.(1991) Degradation of xenobiotics by white rot fungi. Rev Environ ContamToxicol.122:111-152
    • (1991) Rev Environ ContamToxicol , vol.122 , pp. 111-152
    • Higson, F.K.1
  • 113
    • 0004159313 scopus 로고
    • Lignin biochemistry: Biosynthesis and biodegradation
    • Higuchi T.(1990) Lignin biochemistry: biosynthesis and biodegradation. Wood Sci Technol.24(1):23-63
    • (1990) Wood Sci Technol , vol.24 , Issue.1 , pp. 23-63
    • Higuchi, T.1
  • 114
    • 79953163565 scopus 로고    scopus 로고
    • Insight into functional diversity of cytochrome P450 in the white-rot basidiomycete Phanerochaete chrysosporium:Involvement of versatile monooxygenase
    • Hirosue S, Tazaki M et al.(2011) Insight into functional diversity of cytochrome P450 in the white-rot basidiomycete Phanerochaete chrysosporium:involvement of versatile monooxygenase. Biochem Biophys Res Commun.407(1):118-123
    • (2011) Biochem Biophys Res Commun , vol.407 , Issue.1 , pp. 118-123
    • Hirosue, S.1    Tazaki, M.2
  • 115
    • 77952886858 scopus 로고    scopus 로고
    • Changes in oxidative enzyme activity during interspecific mycelial interactions involving the white-rot fungus Trametes versicolor
    • Hiscox J, Baldrian P et al.(2010) Changes in oxidative enzyme activity during interspecific mycelial interactions involving the white-rot fungus Trametes versicolor. Fungal Genet Biol.47(6):562-571
    • (2010) Fungal Genet Biol , vol.47 , Issue.6 , pp. 562-571
    • Hiscox, J.1    Baldrian, P.2
  • 116
    • 33646268426 scopus 로고    scopus 로고
    • Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences
    • Hoegger PJ, Kilaru S et al.(2006) Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences. FEBS J.273(10):2308-2326
    • (2006) FEBS J , vol.273 , Issue.10 , pp. 2308-2326
    • Hoegger, P.J.1    Kilaru, S.2
  • 117
    • 77954296079 scopus 로고    scopus 로고
    • New and classic families of secreted fungal heme peroxidases
    • Hofrichter M, Ullrich R et al.(2010) New and classic families of secreted fungal heme peroxidases. Appl Microbiol Biotechnol.87(3):871-897
    • (2010) Appl Microbiol Biotechnol , vol.87 , Issue.3 , pp. 871-897
    • Hofrichter, M.1    Ullrich, R.2
  • 118
    • 0024288709 scopus 로고
    • Structure and regulation of a lignin peroxidase gene from Phanerochaete chrysosporium
    • Holzbaur E, Tien M.(1988) Structure and regulation of a lignin peroxidase gene from Phanerochaete chrysosporium. Biochem Biophys Res Commun.155:626-633
    • (1988) Biochem Biophys Res Commun , vol.155 , pp. 626-633
    • Holzbaur, E.1    Tien, M.2
  • 119
    • 0034036074 scopus 로고    scopus 로고
    • Carboxin resistance transformation of the homobasidiomycete fungus Pleurotus ostreatus
    • Honda Y, Matsuyama T et al.(2000) Carboxin resistance transformation of the homobasidiomycete fungus Pleurotus ostreatus. Curr Genet.37(3):209-212
    • (2000) Curr Genet , vol.37 , Issue.3 , pp. 209-212
    • Honda, Y.1    Matsuyama, T.2
  • 120
    • 79959976450 scopus 로고    scopus 로고
    • Effects of xylan and starch on secretome of the basidiomycete Phanerochaete chrysosporium grown on cellulose
    • Hori C, Igarashi K et al.(2011) Effects of xylan and starch on secretome of the basidiomycete Phanerochaete chrysosporium grown on cellulose. FEMS Microbiol Lett.321(1):14-23
    • (2011) FEMS Microbiol Lett , vol.321 , Issue.1 , pp. 14-23
    • Hori, C.1    Igarashi, K.2
  • 121
    • 84860462184 scopus 로고    scopus 로고
    • Biological degradation of anthroquinone and azo dyes by a novel laccase from Lentinus sp
    • Hsu CA, Wen TN et al.(2012) Biological degradation of anthroquinone and azo dyes by a novel laccase from Lentinus sp. Environ Sci Technol.46(9):5109-5117
    • (2012) Environ Sci Technol , vol.46 , Issue.9 , pp. 5109-5117
    • Hsu, C.A.1    Wen, T.N.2
  • 122
    • 0033823686 scopus 로고    scopus 로고
    • Transformation of triclosan by Trametes versicolor and Pycnoporus cinnabarinus
    • Hundt K, Martin D et al.(2000) Transformation of triclosan by Trametes versicolor and Pycnoporus cinnabarinus. Appl Environ Microbiol.66(9):4157-4160
    • (2000) Appl Environ Microbiol , vol.66 , Issue.9 , pp. 4157-4160
    • Hundt, K.1    Martin, D.2
  • 123
    • 0032855263 scopus 로고    scopus 로고
    • Bioconversion of recalcitrant 4-methyldibenzothiophene to waterextractable products using lignin-degrading basidiomycete Coriolus versicolor
    • Ichinose H, Wariishi H et al.(1999) Bioconversion of recalcitrant 4-methyldibenzothiophene to waterextractable products using lignin-degrading basidiomycete Coriolus versicolor. Biotechnol Prog.15(4):706-714
    • (1999) Biotechnol Prog , vol.15 , Issue.4 , pp. 706-714
    • Ichinose, H.1    Wariishi, H.2
  • 124
    • 0035009111 scopus 로고    scopus 로고
    • Efficient transformation of filamentous fungus Pleurotus ostreatus using single-strand carrier DNA
    • Irie T, Honda Y et al.(2001) Efficient transformation of filamentous fungus Pleurotus ostreatus using single-strand carrier DNA. Appl Microbiol Biotechnol.55(5):563-565
    • (2001) Appl Microbiol Biotechnol , vol.55 , Issue.5 , pp. 563-565
    • Irie, T.1    Honda, Y.2
  • 125
    • 0032169337 scopus 로고    scopus 로고
    • Expression of Phanerochaete chrysosporium genes encoding lignin peroxidases, manganese peroxidases, and glyoxal oxidase in wood
    • Janse BJH, Gaskell J et al.(1998) Expression of Phanerochaete chrysosporium genes encoding lignin peroxidases, manganese peroxidases, and glyoxal oxidase in wood. Appl Environ Microbiol.64(9):3536-3538
    • (1998) Appl Environ Microbiol , vol.64 , Issue.9 , pp. 3536-3538
    • Janse, B.J.H.1    Gaskell, J.2
  • 126
    • 0033971693 scopus 로고    scopus 로고
    • Natural mediators in the oxidation of polycyclic aromatic hydrocarbons by laccase mediator systems
    • Johannes C, Majcherczyk A.(2000) Natural mediators in the oxidation of polycyclic aromatic hydrocarbons by laccase mediator systems. Appl Environ Microbiol.66(2):524-528
    • (2000) Appl Environ Microbiol , vol.66 , Issue.2 , pp. 524-528
    • Johannes, C.1    Majcherczyk, A.2
  • 127
    • 0029959323 scopus 로고    scopus 로고
    • Degradation of anthracene by laccase of Trametes versicolor in the presence of different mediator compounds
    • Johannes C, Majcherczyk A et al.(1996) Degradation of anthracene by laccase of Trametes versicolor in the presence of different mediator compounds. Appl Microbiol Biotechnol.46(3):313-317
    • (1996) Appl Microbiol Biotechnol , vol.46 , Issue.3 , pp. 313-317
    • Johannes, C.1    Majcherczyk, A.2
  • 128
    • 0036211084 scopus 로고    scopus 로고
    • Differential regulation of mnp2, a new manganese peroxidaseencoding gene from the ligninolytic fungus Trametes versicolor PRL 572
    • Johansson T, Nyman PO et al.(2002) Differential regulation of mnp2, a new manganese peroxidaseencoding gene from the ligninolytic fungus Trametes versicolor PRL 572. Appl Environ Microbiol.68(4):2077-2080
    • (2002) Appl Environ Microbiol , vol.68 , Issue.4 , pp. 2077-2080
    • Johansson, T.1    Nyman, P.O.2
  • 129
    • 0026348456 scopus 로고
    • Heterologous expression and characterization of an active lignin peroxidase from Phanerochaete chrysosporium using recombinant baculovirus
    • Johnson TM, Li JK.(1991) Heterologous expression and characterization of an active lignin peroxidase from Phanerochaete chrysosporium using recombinant baculovirus. Arch Biochem Biophys.291:371-378
    • (1991) Arch Biochem Biophys , vol.291 , pp. 371-378
    • Johnson, T.M.1    Li, J.K.2
  • 130
    • 0026699574 scopus 로고
    • Production and characterization of recombinant lignin peroxidase isozyme H2 from Phanerochaete chrysosporium using recombinant baculovirus
    • Johnson T, Pease E et al.(1992) Production and characterization of recombinant lignin peroxidase isozyme H2 from Phanerochaete chrysosporium using recombinant baculovirus. Arch Biochem Biophys.296:660-666
    • (1992) Arch Biochem Biophys , vol.296 , pp. 660-666
    • Johnson, T.1    Pease, E.2
  • 131
    • 44649153681 scopus 로고    scopus 로고
    • Identification of fungal metabolites of anticonvulsant drug carbamazepine
    • Kang SI, Kang SY et al.(2008) Identification of fungal metabolites of anticonvulsant drug carbamazepine. Appl Microbiol Biotechnol.79(4):663-669
    • (2008) Appl Microbiol Biotechnol , vol.79 , Issue.4 , pp. 663-669
    • Kang, S.I.1    Kang, S.Y.2
  • 132
    • 0032755394 scopus 로고    scopus 로고
    • Peroxyl radicals are potential agents of lignin biodegradation
    • Kapich AN, Jensen KA et al.(1999) Peroxyl radicals are potential agents of lignin biodegradation. FEBS Lett.461(1-2):115-119
    • (1999) FEBS Lett , vol.461 , Issue.1-2 , pp. 115-119
    • Kapich, A.N.1    Jensen, K.A.2
  • 133
    • 0032570013 scopus 로고    scopus 로고
    • Structure and expression of a laccase gene from the ligninolytic basidiomycete Ceriporiopsis subvermispora
    • Karahanian E, Corsini G et al.(1998) Structure and expression of a laccase gene from the ligninolytic basidiomycete Ceriporiopsis subvermispora. Biochim Biophys Acta.1443(1-2):65-74
    • (1998) Biochim Biophys Acta , vol.1443 , Issue.1-2 , pp. 65-74
    • Karahanian, E.1    Corsini, G.2
  • 134
    • 56949096940 scopus 로고    scopus 로고
    • Fungal dye decolourization:Recent advances and future potential
    • Kaushik P, Malik A.(2009) Fungal dye decolourization:recent advances and future potential. Environ Int.35(1):127-141
    • (2009) Environ Int , vol.35 , Issue.1 , pp. 127-141
    • Kaushik, P.1    Malik, A.2
  • 135
    • 0023989854 scopus 로고
    • Degradation mechanisms of phenolic b-1 lignin substructure and model compounds by laccase of Coriolus versicolor
    • Kawai S, Umezawa T et al.(1988) Degradation mechanisms of phenolic b-1 lignin substructure and model compounds by laccase of Coriolus versicolor. Arch Biochem Biophys.262:99-110
    • (1988) Arch Biochem Biophys , vol.262 , pp. 99-110
    • Kawai, S.1    Umezawa, T.2
  • 136
    • 0022531431 scopus 로고
    • Purification and characterization of glucose oxidase from ligninolytic cultures of Phanerochaete chrysosporium
    • Kelley RL, Reddy CA.(1986) Purification and characterization of glucose oxidase from ligninolytic cultures of Phanerochaete chrysosporium. J Bacteriol.166(1):269-274
    • (1986) J Bacteriol , vol.166 , Issue.1 , pp. 269-274
    • Kelley, R.L.1    Reddy, C.A.2
  • 137
    • 0024231384 scopus 로고
    • Glucose oxidase of Phanerochaete chrysosporium
    • Kelley RL, Reddy CA.(1988) Glucose oxidase of Phanerochaete chrysosporium. Methods Enzymol.161:307-316
    • (1988) Methods Enzymol , vol.161 , pp. 307-316
    • Kelley, R.L.1    Reddy, C.A.2
  • 138
    • 0025246775 scopus 로고
    • Glyoxal oxidase of Phanerochaete chrysosporium: Its characterization and activation by lignin peroxidase
    • Kersten PJ.(1990) Glyoxal oxidase of Phanerochaete chrysosporium: its characterization and activation by lignin peroxidase. Proc Natl Acad Sci USA.87(8):2936-2940
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.8 , pp. 2936-2940
    • Kersten, P.J.1
  • 139
    • 0027242188 scopus 로고
    • Cloning and characterization of a cDNA encoding glyoxal oxidase, a peroxide-producing enzyme from the lignindegrading basidiomycete Phanerochaete chrysosporium
    • Kersten P, Cullen D.(1993) Cloning and characterization of a cDNA encoding glyoxal oxidase, a peroxide-producing enzyme from the lignindegrading basidiomycete Phanerochaete chrysosporium. Proc Natl Acad Sci USA.90:7411-7413
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7411-7413
    • Kersten, P.1    Cullen, D.2
  • 140
    • 0023264566 scopus 로고
    • Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium
    • Kersten PJ, Kirk TK.(1987) Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium. J Bacteriol.169:2195-2201
    • (1987) J Bacteriol , vol.169 , pp. 2195-2201
    • Kersten, P.J.1    Kirk, T.K.2
  • 141
    • 0021910164 scopus 로고
    • The ligninase of Phanerochaete chrysosporium generates cation radicals from methoxybenzenes
    • Kersten PJ, Tien M et al.(1985) The ligninase of Phanerochaete chrysosporium generates cation radicals from methoxybenzenes. J Biol Chem.260:2609-2612
    • (1985) J Biol Chem , vol.260 , pp. 2609-2612
    • Kersten, P.J.1    Tien, M.2
  • 142
    • 0028803376 scopus 로고
    • Phanerochaete chrysosporium glyoxal oxidase is encoded by two allelic variants: Structure, genomic organization and heterologous expression of glx1 and glx2
    • Kersten PJ, Witek C et al.(1995) Phanerochaete chrysosporium glyoxal oxidase is encoded by two allelic variants: structure, genomic organization and heterologous expression of glx1 and glx2. J Bacteriol.177:6106-6110
    • (1995) J Bacteriol , vol.177 , pp. 6106-6110
    • Kersten, P.J.1    Witek, C.2
  • 143
    • 0037046296 scopus 로고    scopus 로고
    • Transformation of the medicinal basidiomycete Trametes versicolor to hygromycin B resistance by restriction enzyme mediated integration
    • Kim K, Leem Y et al.(2002) Transformation of the medicinal basidiomycete Trametes versicolor to hygromycin B resistance by restriction enzyme mediated integration. FEMS Microbiol Lett.209(2):273-276
    • (2002) FEMS Microbiol Lett , vol.209 , Issue.2 , pp. 273-276
    • Kim, K.1    Leem, Y.2
  • 144
    • 0023478845 scopus 로고
    • Enzymatic “combustion”:The microbial degradation of lignin
    • Kirk TK, Farrell RL.(1987) Enzymatic “combustion”:the microbial degradation of lignin. Annu Rev Microbiol.41:465-505
    • (1987) Annu Rev Microbiol , vol.41 , pp. 465-505
    • Kirk, T.K.1    Farrell, R.L.2
  • 145
    • 0025168353 scopus 로고
    • Cloning, sequence analysis, and expression of ligninolytic phenoloxidase genes of the white-rot basidiomycete Coriolus hirsutus
    • Kojima Y, Tsukuda Y et al.(1990) Cloning, sequence analysis, and expression of ligninolytic phenoloxidase genes of the white-rot basidiomycete Coriolus hirsutus. J Biol Chem.256:15224-15230
    • (1990) J Biol Chem , vol.256 , pp. 15224-15230
    • Kojima, Y.1    Tsukuda, Y.2
  • 146
    • 0030024125 scopus 로고    scopus 로고
    • Metabolic pathways utilized by Phanerochaete chrysosporium for degradation of the cyclodiene pesticide endosulfan
    • Kullman SW, Matsumura F.(1996) Metabolic pathways utilized by Phanerochaete chrysosporium for degradation of the cyclodiene pesticide endosulfan. Appl Environ Microbiol.62:593-600
    • (1996) Appl Environ Microbiol , vol.62 , pp. 593-600
    • Kullman, S.W.1    Matsumura, F.2
  • 147
    • 0025191522 scopus 로고
    • In situ depletion of pentachlorophenol from contaminated soil by Phanerochaete spp
    • Lamar R, Dietrich D.(1990) In situ depletion of pentachlorophenol from contaminated soil by Phanerochaete spp. Appl Environ Microbiol.56:3093-3100
    • (1990) Appl Environ Microbiol , vol.56 , pp. 3093-3100
    • Lamar, R.1    Dietrich, D.2
  • 148
    • 0000093062 scopus 로고
    • Fate of pentachlorophenol (PCP) in sterile soils inoculated with the white-rot basidiomycete Phanerochaete chrysosporium; mineralization, volatilization and depletion of PCP
    • Lamar RT, Glaser JA et al.(1990 a) Fate of pentachlorophenol (PCP) in sterile soils inoculated with the white-rot basidiomycete Phanerochaete chrysosporium; mineralization, volatilization and depletion of PCP. Soil Biol Biochem.22(4):433-440
    • (1990) Soil Biol Biochem , vol.22 , Issue.4 , pp. 433-440
    • Lamar, R.T.1    Glaser, J.A.2
  • 149
    • 0025197554 scopus 로고
    • Sensitivity to and degradation of pentachlorophenol by Phanerochaete spp
    • Lamar RT, Larsen MJ et al.(1990 b) Sensitivity to and degradation of pentachlorophenol by Phanerochaete spp. Appl Environ Microbiol.56(11):3519-3526
    • (1990) Appl Environ Microbiol , vol.56 , Issue.11 , pp. 3519-3526
    • Lamar, R.T.1    Larsen, M.J.2
  • 150
    • 0028164644 scopus 로고
    • Treatment of a pentachlorophenol- and creosote-contaminated soil using the lignin-degrading fungus Phanerochaete chrysosporium:A field demonstration
    • Lamar RT, Davis MW et al.(1994) Treatment of a pentachlorophenol- and creosote-contaminated soil using the lignin-degrading fungus Phanerochaete chrysosporium:a field demonstration. Soil Biol Biochem.26:1603-1611
    • (1994) Soil Biol Biochem , vol.26 , pp. 1603-1611
    • Lamar, R.T.1    Davis, M.W.2
  • 151
    • 0029067996 scopus 로고
    • Quantitation of fungal mRNAs in complex substrates by reverse transcription PCR and its application to Phanerochaete chrysosporium-colonized soil
    • Lamar RT, Schoenike B et al.(1995) Quantitation of fungal mRNAs in complex substrates by reverse transcription PCR and its application to Phanerochaete chrysosporium-colonized soil. Appl Environ Microbiol.61:2122-2126
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2122-2126
    • Lamar, R.T.1    Schoenike, B.2
  • 152
    • 81755178934 scopus 로고    scopus 로고
    • Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61
    • Langston JA, Shaghasi T et al.(2011) Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61. Appl Environ Microbiol.77(19):7007-7015
    • (2011) Appl Environ Microbiol , vol.77 , Issue.19 , pp. 7007-7015
    • Langston, J.A.1    Shaghasi, T.2
  • 153
    • 0344603831 scopus 로고    scopus 로고
    • Molecular karyotype of the white rot fungus Pleurotus ostreatus
    • Larraya LM, Perez G et al.(1999) Molecular karyotype of the white rot fungus Pleurotus ostreatus. Appl Environ Microbiol.65(8):3413-3417
    • (1999) Appl Environ Microbiol , vol.65 , Issue.8 , pp. 3413-3417
    • Larraya, L.M.1    Perez, G.2
  • 154
    • 0034466657 scopus 로고    scopus 로고
    • Genetic linkage map of the edible basidiomycete Pleurotus ostreatus
    • Larraya LM, Perez G et al.(2000) Genetic linkage map of the edible basidiomycete Pleurotus ostreatus. Appl Environ Microbiol.66(12):5290-5300
    • (2000) Appl Environ Microbiol , vol.66 , Issue.12 , pp. 5290-5300
    • Larraya, L.M.1    Perez, G.2
  • 155
    • 0036193076 scopus 로고    scopus 로고
    • Quantitative trait loci controlling vegetative growth rate in the edible basidiomycete Pleurotus ostreatus
    • Larraya LM, Idareta E et al.(2002) Quantitative trait loci controlling vegetative growth rate in the edible basidiomycete Pleurotus ostreatus. Appl Environ Microbiol.68(3):1109-1114
    • (2002) Appl Environ Microbiol , vol.68 , Issue.3 , pp. 1109-1114
    • Larraya, L.M.1    Idareta, E.2
  • 156
    • 0035347318 scopus 로고    scopus 로고
    • Isoenzyme multiplicity and characterization of recombinant manganese peroxidases from Ceriporiopsis subvermispora and Phanerochaete chrysosporium
    • Larrondo LF, Lobos S et al.(2001) Isoenzyme multiplicity and characterization of recombinant manganese peroxidases from Ceriporiopsis subvermispora and Phanerochaete chrysosporium. Appl Environ Microbiol.67(5):2070-2075
    • (2001) Appl Environ Microbiol , vol.67 , Issue.5 , pp. 2070-2075
    • Larrondo, L.F.1    Lobos, S.2
  • 157
    • 0038530715 scopus 로고    scopus 로고
    • Heterologous expression of laccase cDNA from Ceriporiopsis subvermispora yields copper-activated apoprotein and complex isoform patterns
    • Larrondo LF, Avila M et al.(2003) Heterologous expression of laccase cDNA from Ceriporiopsis subvermispora yields copper-activated apoprotein and complex isoform patterns. Microbiology.149 (Pt 5):1177-1182
    • (2003) Microbiology , vol.149 , pp. 1177-1182
    • Larrondo, L.F.1    Avila, M.2
  • 158
    • 33845955361 scopus 로고    scopus 로고
    • Phanerochaete chrysosporium genomics
    • Arora DK, Berka R (eds), Elsevier, Amsterdam
    • Larrondo L, Vicuna R et al.(2005) Phanerochaete chrysosporium genomics. In: Arora DK, Berka R (eds) Applied mycology and biotechnology, vol 5. Elsevier, Amsterdam, pp 315-352
    • (2005) Applied mycology and biotechnology, vol 5 , pp. 315-352
    • Larrondo, L.1    Vicuna, R.2
  • 159
    • 63249101774 scopus 로고    scopus 로고
    • Presence and fate of carbamazepine, oxcarbazepine, and seven of their metabolites at wastewater treatment plants
    • Leclercq M, Mathieu O et al.(2009) Presence and fate of carbamazepine, oxcarbazepine, and seven of their metabolites at wastewater treatment plants. Arch Environ Contam Toxicol.56(3):408-415
    • (2009) Arch Environ Contam Toxicol , vol.56 , Issue.3 , pp. 408-415
    • Leclercq, M.1    Mathieu, O.2
  • 160
    • 0029889182 scopus 로고    scopus 로고
    • Development of fungal inocula for bioaugmentation of contaminated soils
    • Lestan D, Lamar RT.(1996) Development of fungal inocula for bioaugmentation of contaminated soils. Appl Environ Microbiol.62(6):2045-2052
    • (1996) Appl Environ Microbiol , vol.62 , Issue.6 , pp. 2045-2052
    • Lestan, D.1    Lamar, R.T.2
  • 161
    • 0029928876 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium
    • Li B, Nagalla SR et al.(1996) Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium. Appl Environ Microbiol.62(4):1329-1335
    • (1996) Appl Environ Microbiol , vol.62 , Issue.4 , pp. 1329-1335
    • Li, B.1    Nagalla, S.R.2
  • 162
    • 0034595083 scopus 로고    scopus 로고
    • Homologous expression of recombinant cellobiose dehydrogenase in Phanerochaete chrysosporium
    • Li B, Rotsaert FA et al.(2000) Homologous expression of recombinant cellobiose dehydrogenase in Phanerochaete chrysosporium. Biochem Biophys Res Commun.270(1):141-146
    • (2000) Biochem Biophys Res Commun , vol.270 , Issue.1 , pp. 141-146
    • Li, B.1    Rotsaert, F.A.2
  • 163
    • 34250866191 scopus 로고    scopus 로고
    • Screening method for ecotoxicological hazard assessment of 42 pharmaceuticals considering human metabolism and excretory routes
    • Lienert J, Gudel K et al.(2007) Screening method for ecotoxicological hazard assessment of 42 pharmaceuticals considering human metabolism and excretory routes. Environ Sci Technol.41(12):4471-4478
    • (2007) Environ Sci Technol , vol.41 , Issue.12 , pp. 4471-4478
    • Lienert, J.1    Gudel, K.2
  • 164
    • 76849083614 scopus 로고    scopus 로고
    • DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and highredox potential dyes
    • Liers C, Bobeth C et al.(2010) DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and highredox potential dyes. Appl Microbiol Biotechnol.85(6):1869-1879
    • (2010) Appl Microbiol Biotechnol , vol.85 , Issue.6 , pp. 1869-1879
    • Liers, C.1    Bobeth, C.2
  • 165
    • 0028036741 scopus 로고
    • Isozymes of manganesedependent peroxidase and laccase produced by the lignin-degrading basidiomycete Ceriporiopsis subvermispora
    • Lobos S, Larrain J et al.(1994) Isozymes of manganesedependent peroxidase and laccase produced by the lignin-degrading basidiomycete Ceriporiopsis subvermispora. Microbiology.140:2691-2698
    • (1994) Microbiology , vol.140 , pp. 2691-2698
    • Lobos, S.1    Larrain, J.2
  • 166
    • 70349271264 scopus 로고    scopus 로고
    • Production and synthetic dyes decolourization capacity of a recombinant laccase from Pichia pastoris
    • Lu L, ZhaoMet al.(2009) Production and synthetic dyes decolourization capacity of a recombinant laccase from Pichia pastoris. J Appl Microbiol.107(4):1149-1156
    • (2009) J Appl Microbiol , vol.107 , Issue.4 , pp. 1149-1156
    • Lu, L.1    Zhaomet, A.2
  • 167
    • 79952575710 scopus 로고    scopus 로고
    • Bacteria-mediated PAH degradation in soil and sediment
    • Lu XY, Zhang T et al.(2011) Bacteria-mediated PAH degradation in soil and sediment. Appl Microbiol Biotechnol.89(5):1357-1371
    • (2011) Appl Microbiol Biotechnol , vol.89 , Issue.5 , pp. 1357-1371
    • Lu, X.Y.1    Zhang, T.2
  • 168
    • 77049096911 scopus 로고    scopus 로고
    • Lignin-modifying enzymes in filamentous basdiomycetes-ecological, functional and phylogenetic review
    • Lundell TK, Makela MR et al.(2010) Lignin-modifying enzymes in filamentous basdiomycetes-ecological, functional and phylogenetic review. J Basic Microbiol.50:4-20
    • (2010) J Basic Microbiol , vol.50 , pp. 4-20
    • Lundell, T.K.1    Makela, M.R.2
  • 169
    • 0035140816 scopus 로고    scopus 로고
    • The green fluorescent protein gene functions as a reporter of gene expression in Phanerochaete chrysosporium
    • Ma B, Mayfield MB et al.(2001) The green fluorescent protein gene functions as a reporter of gene expression in Phanerochaete chrysosporium. Appl Environ Microbiol.67(2):948-955
    • (2001) Appl Environ Microbiol , vol.67 , Issue.2 , pp. 948-955
    • Ma, B.1    Mayfield, M.B.2
  • 170
    • 0141631799 scopus 로고    scopus 로고
    • Homologous expression of Phanerochaete chrysosporium manganese peroxidase, using bialaphos resistance as a dominant selectable marker
    • Ma B, Mayfield MB et al.(2003) Homologous expression of Phanerochaete chrysosporium manganese peroxidase, using bialaphos resistance as a dominant selectable marker. Curr Genet.43(6):407-414
    • (2003) Curr Genet , vol.43 , Issue.6 , pp. 407-414
    • Ma, B.1    Mayfield, M.B.2
  • 171
    • 2942644860 scopus 로고    scopus 로고
    • Novel promoter sequence required for manganese regulation of manganese peroxidase isozyme 1 gene expression in Phanerochaete chrysosporium
    • Ma B, MayfieldMB et al.(2004) Novel promoter sequence required for manganese regulation of manganese peroxidase isozyme 1 gene expression in Phanerochaete chrysosporium. Eukaryot Cell.3(3):579-588
    • (2004) Eukaryot Cell , vol.3 , Issue.3 , pp. 579-588
    • Ma, B.1    Mayfield, M.B.2
  • 172
    • 84857078845 scopus 로고    scopus 로고
    • Time-dependent profiles of transcripts encoding lignocellulosemodifying enzymes of the white rot fungus Phanerochaete carnosa grown on multiple wood substrates
    • Macdonald J, Master ER.(2012) Time-dependent profiles of transcripts encoding lignocellulosemodifying enzymes of the white rot fungus Phanerochaete carnosa grown on multiple wood substrates. Appl Environ Microbiol.78(5):1596-1600
    • (2012) Appl Environ Microbiol , vol.78 , Issue.5 , pp. 1596-1600
    • Macdonald, J.1    Master, E.R.2
  • 173
    • 79958235330 scopus 로고    scopus 로고
    • Transcriptomic responses of the softwood-degrading white-rot fungus Phanerochaete carnosa during growth on coniferous and deciduous wood
    • Macdonald J, Doering M et al.(2011) Transcriptomic responses of the softwood-degrading white-rot fungus Phanerochaete carnosa during growth on coniferous and deciduous wood. Appl Environ Microbiol.77:3211-3218
    • (2011) Appl Environ Microbiol , vol.77 , pp. 3211-3218
    • Macdonald, J.1    Doering, M.2
  • 174
    • 84863395511 scopus 로고    scopus 로고
    • Expression and regulation of genes encoding lignocellulosedegrading activity in the genus Phanerochaete
    • MacDonald J, Suzuki H et al.(2012) Expression and regulation of genes encoding lignocellulosedegrading activity in the genus Phanerochaete. Appl Microbiol Biotechnol.94(2):339-351
    • (2012) Appl Microbiol Biotechnol , vol.94 , Issue.2 , pp. 339-351
    • MacDonald, J.1    Suzuki, H.2
  • 175
    • 82455171991 scopus 로고    scopus 로고
    • ItRAQ-based quantitative secretome analysis of Phanerochaete chrysosporium
    • Manavalan A, Adav SS et al.(2011) iTRAQ-based quantitative secretome analysis of Phanerochaete chrysosporium. J Proteomics.75(2):642-654
    • (2011) J Proteomics , vol.75 , Issue.2 , pp. 642-654
    • Manavalan, A.1    Adav, S.S.2
  • 176
    • 77953535569 scopus 로고    scopus 로고
    • Effect of manganese on the secretion of manganese-peroxidase by the basidiomycete Ceriporiopsis subvermispora
    • Mancilla RA, Canessa P et al.(2010) Effect of manganese on the secretion of manganese-peroxidase by the basidiomycete Ceriporiopsis subvermispora. Fungal Genet Biol.47(7):656-661
    • (2010) Fungal Genet Biol , vol.47 , Issue.7 , pp. 656-661
    • Mancilla, R.A.1    Canessa, P.2
  • 177
    • 58549115673 scopus 로고    scopus 로고
    • Ability of white-rot fungi to remove selected pharmaceuticals and identification of degradation products of ibuprofen by Trametes versicolor
    • Marco-Urrea E, Perez-Trujillo M et al.(2009) Ability of white-rot fungi to remove selected pharmaceuticals and identification of degradation products of ibuprofen by Trametes versicolor. Chemosphere.74(6):765-772
    • (2009) Chemosphere , vol.74 , Issue.6 , pp. 765-772
    • Marco-Urrea, E.1    Perez-Trujillo, M.2
  • 178
    • 75849156553 scopus 로고    scopus 로고
    • Oxidation of atenolol, propranolol, carbamazepine and clofibric acid by a biological Fenton-like system mediated by the white-rot fungus Trametes versicolor
    • Marco-Urrea E, Radjenovic J et al.(2010) Oxidation of atenolol, propranolol, carbamazepine and clofibric acid by a biological Fenton-like system mediated by the white-rot fungus Trametes versicolor. Water Res.44(2):521-532
    • (2010) Water Res , vol.44 , Issue.2 , pp. 521-532
    • Marco-Urrea, E.1    Radjenovic, J.2
  • 179
    • 2542601548 scopus 로고    scopus 로고
    • Genome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78
    • Martinez D, Larrondo LF et al.(2004) Genome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78. Nat Biotechnol.22:695-700
    • (2004) Nat Biotechnol , vol.22 , pp. 695-700
    • Martinez, D.1    Larrondo, L.F.2
  • 180
    • 60549116487 scopus 로고    scopus 로고
    • Genome, transcriptome, and secretome analysis of wood decay fungus Postia placenta supports unique mechanisms of lignocellulose conversion
    • Martinez D, Challacombe J et al.(2009) Genome, transcriptome, and secretome analysis of wood decay fungus Postia placenta supports unique mechanisms of lignocellulose conversion. Proc Natl Acad Sci USA.106(6):1954-1959
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.6 , pp. 1954-1959
    • Martinez, D.1    Challacombe, J.2
  • 181
    • 0033590216 scopus 로고    scopus 로고
    • Purification and characterization of a benzo[a]pyrene hydroxylase from Pleurotus pulmonarius
    • Masapahy S, Lamb DC et al.(1999) Purification and characterization of a benzo[a]pyrene hydroxylase from Pleurotus pulmonarius. Biochem Biophys Res Commun.266(2):326-329
    • (1999) Biochem Biophys Res Commun , vol.266 , Issue.2 , pp. 326-329
    • Masapahy, S.1    Lamb, D.C.2
  • 182
    • 77956971213 scopus 로고    scopus 로고
    • Laboratory evolution of high-redox potential laccases
    • Mate D, Garcia-Burgos C et al.(2010) Laboratory evolution of high-redox potential laccases. Chem Biol.17(9):1030-1041
    • (2010) Chem Biol , vol.17 , Issue.9 , pp. 1030-1041
    • Mate, D.1    Garcia-Burgos, C.2
  • 183
    • 50949089410 scopus 로고    scopus 로고
    • Gene silencing by RNA Interference in the white rot fungus Phanerochaete chrysosporium
    • Matityahu A, Hadar Y et al.(2008) Gene silencing by RNA Interference in the white rot fungus Phanerochaete chrysosporium. Appl Environ Microbiol.74(17):5359-5365
    • (2008) Appl Environ Microbiol , vol.74 , Issue.17 , pp. 5359-5365
    • Matityahu, A.1    Hadar, Y.2
  • 184
    • 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, Field JA.(1998) Characterization of a novel manganese peroxidase-lignin peroxidase hybrid isozyme produced by Bjerkandera species strain BOS55 in the absence of manganese. J Biol Chem.273:15412-15417
    • (1998) J Biol Chem , vol.273 , pp. 15412-15417
    • Mester, T.1    Field, J.A.2
  • 185
    • 26044433775 scopus 로고    scopus 로고
    • Carbamazepine and its metabolites in wastewater and in biosolids in a municipal wastewater treatment plant
    • Miao XS, Yang JJ et al.(2005) Carbamazepine and its metabolites in wastewater and in biosolids in a municipal wastewater treatment plant. Environ Sci Technol.39(19):7469-7475
    • (2005) Environ Sci Technol , vol.39 , Issue.19 , pp. 7469-7475
    • Miao, X.S.1    Yang, J.J.2
  • 186
    • 76449112993 scopus 로고    scopus 로고
    • Random mutants of a Pleurotus ostreatus laccase as new biocatalysts for industrial effluents bioremediation
    • Miele A, Giardina P et al.(2010) Random mutants of a Pleurotus ostreatus laccase as new biocatalysts for industrial effluents bioremediation. J Appl Microbiol.108(3):998-1006
    • (2010) J Appl Microbiol , vol.108 , Issue.3 , pp. 998-1006
    • Miele, A.1    Giardina, P.2
  • 187
    • 70349466798 scopus 로고    scopus 로고
    • Escherichia coli expression and in vitro activation of a unique ligninolytic peroxidase that has a catalytic tyrosine residue
    • Miki Y, Morales M et al.(2009) Escherichia coli expression and in vitro activation of a unique ligninolytic peroxidase that has a catalytic tyrosine residue. Protein Expr Purif.68(2):208-214
    • (2009) Protein Expr Purif , vol.68 , Issue.2 , pp. 208-214
    • Miki, Y.1    Morales, M.2
  • 188
    • 0024223233 scopus 로고
    • Biodegradation of pentachlorophenol by the white rot fungus Phanerochaete chrysosporium
    • Mileski GJ, Bumpus JA et al.(1988) Biodegradation of pentachlorophenol by the white rot fungus Phanerochaete chrysosporium. Appl Environ Microbiol.54(12):2885-2889
    • (1988) Appl Environ Microbiol , vol.54 , Issue.12 , pp. 2885-2889
    • Mileski, G.J.1    Bumpus, J.A.2
  • 189
    • 0028238729 scopus 로고
    • Lipid peroxidation by the manganese peroxidase of Phanerochaete chrysosporium is the basis for phenanthrene oxidation by the intact fungus
    • Moen M, Hammel K.(1994) Lipid peroxidation by the manganese peroxidase of Phanerochaete chrysosporium is the basis for phenanthrene oxidation by the intact fungus. Appl Environ Microbiol.60:1956-1961
    • (1994) Appl Environ Microbiol , vol.60 , pp. 1956-1961
    • Moen, M.1    Hammel, K.2
  • 190
    • 68749113804 scopus 로고    scopus 로고
    • Increased PCP removal by Amylomyces rouxii transformants with heterologous Phanerochaete chrysosporium peroxidases supplementing their natural degradative pathway
    • Montiel-Gonzalez AM, Fernandez FJ et al.(2009) Increased PCP removal by Amylomyces rouxii transformants with heterologous Phanerochaete chrysosporium peroxidases supplementing their natural degradative pathway. Appl Microbiol Biotechnol.84(2):335-340
    • (2009) Appl Microbiol Biotechnol , vol.84 , Issue.2 , pp. 335-340
    • Montiel-Gonzalez, A.M.1    Fernandez, F.J.2
  • 191
    • 0033010480 scopus 로고    scopus 로고
    • Cloning and analysis of Pycnoporus cinnabarinus cellobiose dehydrogenase
    • Moukha SM, Dumonceaux TJ et al.(1999) Cloning and analysis of Pycnoporus cinnabarinus cellobiose dehydrogenase. Gene.234(1):23-33
    • (1999) Gene , vol.234 , Issue.1 , pp. 23-33
    • Moukha, S.M.1    Dumonceaux, T.J.2
  • 192
    • 0025382585 scopus 로고
    • Aryl-alcohol-oxidase and lignin-peroxidase from the white-rot fungus Bjerkandera adusta comparison with Phanerochaete chrysosporium lignin-peroxidase for reactivity with veratryl alcohol, homoveratric acid and alpha-benzyl veratryl alcohol
    • Muheim A, Leisola MSA et al.(1990) Aryl-alcohol-oxidase and lignin-peroxidase from the white-rot fungus Bjerkandera adusta comparison with Phanerochaete chrysosporium lignin-peroxidase for reactivity with veratryl alcohol, homoveratric acid and alpha-benzyl veratryl alcohol. J Biotechnol.13(2-3):159-167
    • (1990) J Biotechnol , vol.13 , Issue.2-3 , pp. 159-167
    • Muheim, A.1    Leisola, M.S.A.2
  • 193
    • 80052261097 scopus 로고    scopus 로고
    • Efficient gene targeting in DeltaCc.ku70 or DeltaCc.lig4 mutants of the agaricomycete Coprinopsis cinerea
    • Nakazawa T, Ando Y et al.(2011) Efficient gene targeting in DeltaCc.ku70 or DeltaCc.lig4 mutants of the agaricomycete Coprinopsis cinerea. Fungal Genet Biol.48(10):939-946
    • (2011) Fungal Genet Biol , vol.48 , Issue.10 , pp. 939-946
    • Nakazawa, T.1    Ando, Y.2
  • 194
    • 0032504601 scopus 로고    scopus 로고
    • Expression of the lignin peroxidase H2 gene from Phanerochaete chrysosporium in Escherichia coli
    • Nie G, Reading NS et al.(1998) Expression of the lignin peroxidase H2 gene from Phanerochaete chrysosporium in Escherichia coli. Biochem Biophys Res Commun.249(1):146-150
    • (1998) Biochem Biophys Res Commun , vol.249 , Issue.1 , pp. 146-150
    • Nie, G.1    Reading, N.S.2
  • 195
    • 0030606178 scopus 로고    scopus 로고
    • Cloning and expression of pyranose oxidase cDNA from Coriolus versicolor in E. coli
    • Nishimura I, Okada K et al.(1996) Cloning and expression of pyranose oxidase cDNA from Coriolus versicolor in E. coli. J Biotechnol.52:11-20
    • (1996) J Biotechnol , vol.52 , pp. 11-20
    • Nishimura, I.1    Okada, K.2
  • 196
    • 77956685978 scopus 로고    scopus 로고
    • Genome sequence of the model mushroom Schizophyllum commune
    • Ohm RA, de Jong JF et al.(2010) Genome sequence of the model mushroom Schizophyllum commune. Nat Biotechnol.28(9):957-963
    • (2010) Nat Biotechnol , vol.28 , Issue.9 , pp. 957-963
    • Ohm, R.A.1    de Jong, J.F.2
  • 197
    • 84860511529 scopus 로고    scopus 로고
    • Insight into trade-off between wood decay and parasitism from the genome of a fungal forest pathogen
    • Olson A, Aerts A et al.(2012) Insight into trade-off between wood decay and parasitism from the genome of a fungal forest pathogen. New Phytol.194(4):1001-1013
    • (2012) New Phytol , vol.194 , Issue.4 , pp. 1001-1013
    • Olson, A.1    Aerts, A.2
  • 198
    • 0027501491 scopus 로고
    • Ubiquity of lignin-degrading peroxidases among various wood-degrading fungi
    • Orth A, Royse D et al.(1993) Ubiquity of lignin-degrading peroxidases among various wood-degrading fungi. Appl Environ Microbiol.59:4017-4023
    • (1993) Appl Environ Microbiol , vol.59 , pp. 4017-4023
    • Orth, A.1    Royse, D.2
  • 199
    • 0028063078 scopus 로고
    • Characterization of a cDNA encoding a manganese peroxidase from Phanerochaete chrysosporium: Genomic organization of lignin and manganese peroxidase genes
    • Orth A, Rzhetskaya M et al.(1994) Characterization of a cDNA encoding a manganese peroxidase from Phanerochaete chrysosporium: genomic organization of lignin and manganese peroxidase genes. Gene.148:161-165
    • (1994) Gene , vol.148 , pp. 161-165
    • Orth, A.1    Rzhetskaya, M.2
  • 200
    • 0034052120 scopus 로고    scopus 로고
    • Copper induction of laccase isoenzymes in the ligninolytic fungus Pleurotus ostreatus
    • Palmieri G, Giardina P et al.(2000) Copper induction of laccase isoenzymes in the ligninolytic fungus Pleurotus ostreatus. Appl Environ Microbiol.66(3):920-924
    • (2000) Appl Environ Microbiol , vol.66 , Issue.3 , pp. 920-924
    • Palmieri, G.1    Giardina, P.2
  • 201
    • 0022490037 scopus 로고
    • Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium
    • Paszczynski A, Huynh V-B et al.(1986) Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium. Arch Biochem Biophys.244:750-765
    • (1986) Arch Biochem Biophys , vol.244 , pp. 750-765
    • Paszczynski, A.1    Huynh, V.-B.2
  • 202
    • 0026717196 scopus 로고
    • Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium
    • Pease E, Tien M.(1992) Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium. J Bacteriol.174:3532-3540
    • (1992) J Bacteriol , vol.174 , pp. 3532-3540
    • Pease, E.1    Tien, M.2
  • 203
    • 0024971123 scopus 로고
    • Manganesedependent peroxidase from Phanerochaete chrysosporium. Primary structure deduced from complementary DNA sequence
    • Pease EA, Andrawis A et al.(1989) Manganesedependent peroxidase from Phanerochaete chrysosporium. Primary structure deduced from complementary DNA sequence. J Biol Chem.264 (23):13531-13535
    • (1989) J Biol Chem , vol.264 , Issue.23 , pp. 13531-13535
    • Pease, E.A.1    Andrawis, A.2
  • 204
    • 53749102061 scopus 로고    scopus 로고
    • Microbial biodegradation of polyaromatic hydrocarbons
    • Peng RH, Xiong AS et al.(2008) Microbial biodegradation of polyaromatic hydrocarbons. FEMS Microbiol Rev.32(6):927-955
    • (2008) FEMS Microbiol Rev , vol.32 , Issue.6 , pp. 927-955
    • Peng, R.H.1    Xiong, A.S.2
  • 205
    • 0032524691 scopus 로고    scopus 로고
    • Purification and characterization of laccases from the white-rot basidiomycete Dichomitus squalens
    • Perie FH, Reddy GV et al.(1998) Purification and characterization of laccases from the white-rot basidiomycete Dichomitus squalens. Arch Biochem Biophys.353(2):349-355
    • (1998) Arch Biochem Biophys , vol.353 , Issue.2 , pp. 349-355
    • Perie, F.H.1    Reddy, G.V.2
  • 206
    • 0032863407 scopus 로고    scopus 로고
    • Polycyclic aromatic hydrocarbon metabolism by white rot fungi and oxidation by Coriolopsis gallica UAMH 8260 laccase
    • Pickard MA, Roman R et al.(1999) Polycyclic aromatic hydrocarbon metabolism by white rot fungi and oxidation by Coriolopsis gallica UAMH 8260 laccase. Appl Environ Microbiol.65(9):3805-3809
    • (1999) Appl Environ Microbiol , vol.65 , Issue.9 , pp. 3805-3809
    • Pickard, M.A.1    Roman, R.2
  • 207
    • 67349210370 scopus 로고    scopus 로고
    • Pyranose 2-oxidase from Phanerochaete chrysosporium-expression in E. coli and biochemical characterization
    • Pisanelli I, Kujawa M et al.(2009) Pyranose 2-oxidase from Phanerochaete chrysosporium-expression in E. coli and biochemical characterization. J Biotechnol.142(2):97-106
    • (2009) J Biotechnol , vol.142 , Issue.2 , pp. 97-106
    • Pisanelli, I.1    Kujawa, M.2
  • 208
    • 80955144212 scopus 로고    scopus 로고
    • Fungal laccases:Versatile tools for lignocellulose transformation
    • Piscitelli A, Del Vecchio C et al.(2011 a) Fungal laccases:versatile tools for lignocellulose transformation. C R Biol.334(11):789-794
    • (2011) C R Biol , vol.334 , Issue.11 , pp. 789-794
    • Piscitelli, A.1    Del Vecchio, C.2
  • 209
    • 79955603460 scopus 로고    scopus 로고
    • Induction and transcriptional regulation of laccases in fungi
    • Piscitelli A, Giardina P et al.(2011 b) Induction and transcriptional regulation of laccases in fungi. Curr Genomics.12(2):104-112
    • (2011) Curr Genomics , vol.12 , Issue.2 , pp. 104-112
    • Piscitelli, A.1    Giardina, P.2
  • 210
    • 0034784719 scopus 로고    scopus 로고
    • Feasibility of bioremediation by white-rot fungi
    • Pointing SB.(2001) Feasibility of bioremediation by white-rot fungi. Appl Microbiol Biotechnol.57(1-2):20-33
    • (2001) Appl Microbiol Biotechnol , vol.57 , Issue.1-2 , pp. 20-33
    • Pointing, S.B.1
  • 211
    • 0024978214 scopus 로고
    • Characterization of a cDNA encoding a manganese peroxidase, from the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Pribnow D, Mayfield MB et al.(1989) Characterization of a cDNA encoding a manganese peroxidase, from the lignin-degrading basidiomycete Phanerochaete chrysosporium. J Biol Chem.264(9):5036-5040
    • (1989) J Biol Chem , vol.264 , Issue.9 , pp. 5036-5040
    • Pribnow, D.1    Mayfield, M.B.2
  • 212
    • 80053088478 scopus 로고    scopus 로고
    • Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components
    • Quinlan RJ, Sweeney MD et al.(2011) Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components. Proc Natl Acad Sci USA.108(37):15079-15084
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.37 , pp. 15079-15084
    • Quinlan, R.J.1    Sweeney, M.D.2
  • 213
    • 0029085553 scopus 로고
    • Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium
    • Raices M, Paifer E et al.(1995) Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium. FEBS Lett.369(2-3):233-238
    • (1995) FEBS Lett , vol.369 , Issue.2-3 , pp. 233-238
    • Raices, M.1    Paifer, E.2
  • 214
    • 0026585821 scopus 로고
    • The nature of extrachromosomal maintenance of transforming plasmids in the filamentous basidiomycete Phanerochaete chrysosporium
    • Randall TA, Reddy CA.(1992) The nature of extrachromosomal maintenance of transforming plasmids in the filamentous basidiomycete Phanerochaete chrysosporium. Curr Genet.21:255-260
    • (1992) Curr Genet , vol.21 , pp. 255-260
    • Randall, T.A.1    Reddy, C.A.2
  • 215
    • 0024396112 scopus 로고
    • Use of a shuttle vector for the transformation of the white-rot basidiomycete, Phanerochaete chrysosporium
    • Randall T, Rao TR et al.(1989) Use of a shuttle vector for the transformation of the white-rot basidiomycete, Phanerochaete chrysosporium. Biochem Biophys Res Commun.161:720-725
    • (1989) Biochem Biophys Res Commun , vol.161 , pp. 720-725
    • Randall, T.1    Rao, T.R.2
  • 216
    • 0026083954 scopus 로고
    • A novel extrachromosomally maintained transformation vector for the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Randall T, Reddy CA et al.(1991) A novel extrachromosomally maintained transformation vector for the lignin-degrading basidiomycete Phanerochaete chrysosporium. J Bacteriol.173(2):776-782
    • (1991) J Bacteriol , vol.173 , Issue.2 , pp. 776-782
    • Randall, T.1    Reddy, C.A.2
  • 217
    • 50849138842 scopus 로고    scopus 로고
    • Secretome analysis of Phanerochaete chrysosporium strain CIRMBRFM41 grown on softwood
    • Ravalason H, Jan G et al.(2008) Secretome analysis of Phanerochaete chrysosporium strain CIRMBRFM41 grown on softwood. Appl Microbiol Biotechnol.80(4):719-733
    • (2008) Appl Microbiol Biotechnol , vol.80 , Issue.4 , pp. 719-733
    • Ravalason, H.1    Jan, G.2
  • 218
    • 0033591046 scopus 로고    scopus 로고
    • A two-component tetrachlorohydroquinone reductive dehalogenase system from the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Reddy GV, Gold MH.(1999) A two-component tetrachlorohydroquinone reductive dehalogenase system from the lignin-degrading basidiomycete Phanerochaete chrysosporium. Biochem Biophys Res Commun.257(3):901-905
    • (1999) Biochem Biophys Res Commun , vol.257 , Issue.3 , pp. 901-905
    • Reddy, G.V.1    Gold, M.H.2
  • 219
    • 0033974553 scopus 로고    scopus 로고
    • Degradation of pentachlorophenol by Phanerochaete chrysosporium: Intermediates and reactions involved
    • Reddy GV, Gold MH.(2000) Degradation of pentachlorophenol by Phanerochaete chrysosporium: intermediates and reactions involved. Microbiology.146(Pt 2):405-413
    • (2000) Microbiology , vol.146 , pp. 405-413
    • Reddy, G.V.1    Gold, M.H.2
  • 220
    • 0031691308 scopus 로고    scopus 로고
    • Degradation of 2,4,6-trichlorophenol by Phanerochaete chrysosporium:Involvement of reductive dechlorination
    • Reddy GV, Gelpke MD et al.(1998) Degradation of 2,4,6-trichlorophenol by Phanerochaete chrysosporium:involvement of reductive dechlorination. J Bacteriol.180(19):5159-5164
    • (1998) J Bacteriol , vol.180 , Issue.19 , pp. 5159-5164
    • Reddy, G.V.1    Gelpke, M.D.2
  • 221
    • 0027292239 scopus 로고
    • Methods to investigate the expression of lignin peroxidase genes by the white-rot fungus Phanerochaete chrysosporium
    • Reiser J, Walther I et al.(1993) Methods to investigate the expression of lignin peroxidase genes by the white-rot fungus Phanerochaete chrysosporium. Appl Environ Microbiol.59:2897-2903
    • (1993) Appl Environ Microbiol , vol.59 , pp. 2897-2903
    • Reiser, J.1    Walther, I.2
  • 222
    • 77951225698 scopus 로고    scopus 로고
    • Degradation of naproxen and carbamazepine in spiked sludge by slurry and solid-phase Trametes versicolor systems
    • Rodriguez-Rodriguez CE, Marco-Urrea E et al.(2010) Degradation of naproxen and carbamazepine in spiked sludge by slurry and solid-phase Trametes versicolor systems. Bioresour Technol.101(7):2259-2266
    • (2010) Bioresour Technol , vol.101 , Issue.7 , pp. 2259-2266
    • Rodriguez-Rodriguez, C.E.1    Marco-Urrea, E.2
  • 223
    • 0345035421 scopus 로고    scopus 로고
    • Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates
    • Ruiz-Duenas FJ, Martinez MJ et al.(1999) Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates. Appl Environ Microbiol.65(10):4705-4707
    • (1999) Appl Environ Microbiol , vol.65 , Issue.10 , pp. 4705-4707
    • Ruiz-Duenas, F.J.1    Martinez, M.J.2
  • 224
    • 38949176067 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the catalytic tryptophan environment in Pleurotus eryngii versatile peroxidase
    • Ruiz-Duenas FJ, Morales M et al.(2008) Site-directed mutagenesis of the catalytic tryptophan environment in Pleurotus eryngii versatile peroxidase. Biochemistry.47(6):1685-1695
    • (2008) Biochemistry , vol.47 , Issue.6 , pp. 1685-1695
    • Ruiz-Duenas, F.J.1    Morales, M.2
  • 225
    • 67649786142 scopus 로고    scopus 로고
    • Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases
    • Ruiz-Duenas FJ, Morales M et al.(2009) Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases. J Exp Bot.60(2):441-452
    • (2009) J Exp Bot , vol.60 , Issue.2 , pp. 441-452
    • Ruiz-Duenas, F.J.1    Morales, M.2
  • 226
    • 80955142808 scopus 로고    scopus 로고
    • Pleurotus ostreatus heme peroxidases: An in silico analysis from the genome sequence to the enzyme molecular structure
    • Ruiz-Duenas FJ, Fernandez E et al.(2011) Pleurotus ostreatus heme peroxidases: an in silico analysis from the genome sequence to the enzyme molecular structure. C R Biol.334(11):795-805
    • (2011) C R Biol , vol.334 , Issue.11 , pp. 795-805
    • Ruiz-Duenas, F.J.1    Fernandez, E.2
  • 227
    • 0029776475 scopus 로고    scopus 로고
    • Polymerization of pentachlorophenol and ferulic acid by fungal extracellular lignin-degrading enzymes
    • Ruttimann-Johnson C, Lamar RT.(1996) Polymerization of pentachlorophenol and ferulic acid by fungal extracellular lignin-degrading enzymes. Appl Environ Microbiol.62(10):3890-3893
    • (1996) Appl Environ Microbiol , vol.62 , Issue.10 , pp. 3890-3893
    • Ruttimann-Johnson, C.1    Lamar, R.T.2
  • 228
    • 36048970828 scopus 로고    scopus 로고
    • Functionality improvement of fungal lignin peroxidase by DNA shuffling for 2,4-dichlorophenol degradability and H2O2 stability
    • Ryu K, Hwang SY et al.(2008 a) Functionality improvement of fungal lignin peroxidase by DNA shuffling for 2,4-dichlorophenol degradability and H2O2 stability. J Biotechnol.133(1):110-115
    • (2008) J Biotechnol , vol.133 , Issue.1 , pp. 110-115
    • Ryu, K.1    Hwang, S.Y.2
  • 229
    • 45449084391 scopus 로고    scopus 로고
    • Expression in yeast of secreted lignin peroxidase with improved 2,4- dichlorophenol degradability by DNA shuffling
    • Ryu K, Kang JH et al.(2008 b) Expression in yeast of secreted lignin peroxidase with improved 2,4- dichlorophenol degradability by DNA shuffling. J Biotechnol.135(3):241-246
    • (2008) J Biotechnol , vol.135 , Issue.3 , pp. 241-246
    • Ryu, K.1    Kang, J.H.2
  • 230
    • 77957701203 scopus 로고    scopus 로고
    • Transcriptional effect of a calmodulin inhibitor, W-7, on the ligninolytic enzyme genes in Phanerochaete chrysosporium
    • Sakamoto T, Kitaura H et al.(2010) Transcriptional effect of a calmodulin inhibitor, W-7, on the ligninolytic enzyme genes in Phanerochaete chrysosporium. Curr Genet.56(5):401-410
    • (2010) Curr Genet , vol.56 , Issue.5 , pp. 401-410
    • Sakamoto, T.1    Kitaura, H.2
  • 231
    • 77953580652 scopus 로고    scopus 로고
    • Pleurotus ostreatus manganese-dependent peroxidase silencing impairs decolourization of Orange II
    • Salame TM, Yarden O et al.(2010) Pleurotus ostreatus manganese-dependent peroxidase silencing impairs decolourization of Orange II. Microb Biotechnol.3(1):93-106
    • (2010) Microb Biotechnol , vol.3 , Issue.1 , pp. 93-106
    • Salame, T.M.1    Yarden, O.2
  • 232
    • 79251597602 scopus 로고    scopus 로고
    • RNAi as a potential tool for biotechnological applications in fungi
    • Salame TM, Ziv C et al.(2011) RNAi as a potential tool for biotechnological applications in fungi. Appl Microbiol Biotechnol.89(3):501-512
    • (2011) Appl Microbiol Biotechnol , vol.89 , Issue.3 , pp. 501-512
    • Salame, T.M.1    Ziv, C.2
  • 233
    • 84866145027 scopus 로고    scopus 로고
    • Predominance of a Versatile-Peroxidase-Encoding Gene, mnp4, as Demonstrated by Gene Replacement via a Gene Targeting System for Pleurotus ostreatus
    • Salame TM, Knop D et al.(2012) Predominance of a Versatile-Peroxidase-Encoding Gene, mnp4, as Demonstrated by Gene Replacement via a Gene Targeting System for Pleurotus ostreatus. Appl Environ Microbiol.78(15):5341-5352
    • (2012) Appl Environ Microbiol , vol.78 , Issue.15 , pp. 5341-5352
    • Salame, T.M.1    Knop, D.2
  • 234
    • 0029014670 scopus 로고
    • Properties of laccase isoenzymes produced by the basidiomycete Ceriporiopsis subvermispora
    • Salas C, Lobos S et al.(1995) Properties of laccase isoenzymes produced by the basidiomycete Ceriporiopsis subvermispora. Biotechnol Appl Biochem.21:323-333
    • (1995) Biotechnol Appl Biochem , vol.21 , pp. 323-333
    • Salas, C.1    Lobos, S.2
  • 235
    • 0025738953 scopus 로고
    • Isolation and structural analysis of the laccase gene from the lignin-degrading fungus Phlebia radiata
    • Saloheimo M, Niku-Paavola M et al.(1991) Isolation and structural analysis of the laccase gene from the lignin-degrading fungus Phlebia radiata. J Gen Microbiol.137:1537-1544
    • (1991) J Gen Microbiol , vol.137 , pp. 1537-1544
    • Saloheimo, M.1    Niku-Paavola, M.2
  • 236
    • 0026022706 scopus 로고
    • Purification and characterization of a veratryl alcohol oxidase enzyme from the lignin degrading basidiomycete Pleurotus ostreatus
    • Sannia G, Limongi P et al.(1991) Purification and characterization of a veratryl alcohol oxidase enzyme from the lignin degrading basidiomycete Pleurotus ostreatus. Biochim Biophys Acta.1073:114-119
    • (1991) Biochim Biophys Acta , vol.1073 , pp. 114-119
    • Sannia, G.1    Limongi, P.2
  • 237
    • 67349249841 scopus 로고    scopus 로고
    • The first genome-level transcriptome of the wood-degrading fungus Phanerochaete chrysosporium grown on red oak
    • Sato S, Feltus FA et al.(2009) The first genome-level transcriptome of the wood-degrading fungus Phanerochaete chrysosporium grown on red oak. Curr Genet.55(3):273-286
    • (2009) Curr Genet , vol.55 , Issue.3 , pp. 273-286
    • Sato, S.1    Feltus, F.A.2
  • 238
    • 0031924036 scopus 로고    scopus 로고
    • Conversion of aminonitrotoluenes by fungal manganese peroxidase
    • Scheibner K, Hofrichter M.(1998) Conversion of aminonitrotoluenes by fungal manganese peroxidase. J Basic Microbiol.38(1):51-59
    • (1998) J Basic Microbiol , vol.38 , Issue.1 , pp. 51-59
    • Scheibner, K.1    Hofrichter, M.2
  • 239
    • 27144480805 scopus 로고    scopus 로고
    • Metabolic regulation at the tricarboxylic acid and glyoxylate cycles of the lignin-degrading basidiomycete Phanerochaete chrysosporium against exogenous addition of vanillin
    • Shimizu M, Yuda N et al.(2005) Metabolic regulation at the tricarboxylic acid and glyoxylate cycles of the lignin-degrading basidiomycete Phanerochaete chrysosporium against exogenous addition of vanillin. Proteomics.5(15):3919-3931
    • (2005) Proteomics , vol.5 , Issue.15 , pp. 3919-3931
    • Shimizu, M.1    Yuda, N.2
  • 240
    • 0021992631 scopus 로고
    • On the mechanism of enzymatic lignin breakdown
    • Shoemaker HE, Harvey PJ et al.(1985) On the mechanism of enzymatic lignin breakdown. FEBS Lett.183:7-12
    • (1985) FEBS Lett , vol.183 , pp. 7-12
    • Shoemaker, H.E.1    Harvey, P.J.2
  • 241
    • 79953684578 scopus 로고    scopus 로고
    • Removal of synthetic textile dyes from wastewaters: A critical review on present treatment technologies
    • Singh K, Arora S.(2011) Removal of synthetic textile dyes from wastewaters: a critical review on present treatment technologies. Crit Rev Environ Sci Technol.41:807-878
    • (2011) Crit Rev Environ Sci Technol , vol.41 , pp. 807-878
    • Singh, K.1    Arora, S.2
  • 242
    • 0031977068 scopus 로고    scopus 로고
    • Tandem organization and highly disparate expression of the two laccase genes lcc1 and lcc2 in the cultivated mushroom Agaricus bisporus
    • Smith M, Shnyreva A et al.(1998) Tandem organization and highly disparate expression of the two laccase genes lcc1 and lcc2 in the cultivated mushroom Agaricus bisporus. Microbiology.144(Pt 4):1063-1069
    • (1998) Microbiology , vol.144 , pp. 1063-1069
    • Smith, M.1    Shnyreva, A.2
  • 243
    • 0032914591 scopus 로고    scopus 로고
    • Homologous expression of recombinant lignin peroxidase in Phanerochaete chrysosporium
    • Sollewijn Gelpke MD, Mayfield-Gambill M et al.(1999) Homologous expression of recombinant lignin peroxidase in Phanerochaete chrysosporium. Appl Environ Microbiol.65(4):1670-1674
    • (1999) Appl Environ Microbiol , vol.65 , Issue.4 , pp. 1670-1674
    • Sollewijn Gelpke, M.D.1    Mayfield-Gambill, M.2
  • 244
    • 0037066106 scopus 로고    scopus 로고
    • Lignin peroxidase oxidation of veratryl alcohol: Effects of the mutants H82A, Q222A, W171A, and F267L
    • Sollewijn Gelpke MD, Lee J et al.(2002) Lignin peroxidase oxidation of veratryl alcohol: effects of the mutants H82A, Q222A, W171A, and F267L. Biochemistry.41(10):3498-3506
    • (2002) Biochemistry , vol.41 , Issue.10 , pp. 3498-3506
    • Sollewijn Gelpke, M.D.1    Lee, J.2
  • 245
    • 0033003023 scopus 로고    scopus 로고
    • Organization and differential regulation of a cluster of lignin peroxidase genes of Phanerochaete chrysosporium
    • Stewart P, Cullen D.(1999) Organization and differential regulation of a cluster of lignin peroxidase genes of Phanerochaete chrysosporium. J Bacteriol.181:3427-3432
    • (1999) J Bacteriol , vol.181 , pp. 3427-3432
    • Stewart, P.1    Cullen, D.2
  • 246
    • 0026764236 scopus 로고
    • The lignin peroxidase gene family of Phanerochaete chrysosporium: Complex regulation by carbon and nitrogen limitation, and the identification of a second dimorphic chromosome
    • Stewart P, Kersten P et al.(1992) The lignin peroxidase gene family of Phanerochaete chrysosporium: complex regulation by carbon and nitrogen limitation, and the identification of a second dimorphic chromosome. J Bacteriol.174:5036-5042
    • (1992) J Bacteriol , vol.174 , pp. 5036-5042
    • Stewart, P.1    Kersten, P.2
  • 247
    • 0029961704 scopus 로고    scopus 로고
    • Efficient expression of a Phanerochaete chrysosporium manganese peroxidase gene in Aspergillus oryzae
    • Stewart P, Whitwam RE et al.(1996) Efficient expression of a Phanerochaete chrysosporium manganese peroxidase gene in Aspergillus oryzae. Appl Environ Microbiol.62(3):860-864
    • (1996) Appl Environ Microbiol , vol.62 , Issue.3 , pp. 860-864
    • Stewart, P.1    Whitwam, R.E.2
  • 248
    • 0034921274 scopus 로고    scopus 로고
    • Basic and applied aspects in the microbial degradation of azo dyes
    • Stolz A.(2001) Basic and applied aspects in the microbial degradation of azo dyes. Appl Microbiol Biotechnol.56(1-2):69-80
    • (2001) Appl Microbiol Biotechnol , vol.56 , Issue.1-2 , pp. 69-80
    • Stolz, A.1
  • 249
    • 0842308462 scopus 로고    scopus 로고
    • Molecular approach for analysis of model fungal genes encoding ligninolytic peroxidases in wood-decaying soil systems
    • Stuardo M, Vasquez M et al.(2004) Molecular approach for analysis of model fungal genes encoding ligninolytic peroxidases in wood-decaying soil systems. Lett Appl Microbiol.38(1):43-49
    • (2004) Lett Appl Microbiol , vol.38 , Issue.1 , pp. 43-49
    • Stuardo, M.1    Vasquez, M.2
  • 250
    • 79955750085 scopus 로고    scopus 로고
    • Hydrogen peroxide elimination from C4a-hydroperoxyflavin in a flavoprotein oxidase occurs through a single proton transfer from flavin N5 to a peroxide leaving group
    • Sucharitakul J, Wongnate T et al.(2011) Hydrogen peroxide elimination from C4a-hydroperoxyflavin in a flavoprotein oxidase occurs through a single proton transfer from flavin N5 to a peroxide leaving group. J Biol Chem.286(19):16900-16909
    • (2011) J Biol Chem , vol.286 , Issue.19 , pp. 16900-16909
    • Sucharitakul, J.1    Wongnate, T.2
  • 251
    • 0034127006 scopus 로고    scopus 로고
    • Efficient heterologous expression in Aspergillus oryzae of a unique dyedecolorizing peroxidase, DyP, of Geotrichum candidum
    • Sugano Y, Nakano R et al.(2000) Efficient heterologous expression in Aspergillus oryzae of a unique dyedecolorizing peroxidase, DyP, of Geotrichum candidum. Appl Environ Microbiol.66(4):1754-1758
    • (2000) Appl Environ Microbiol , vol.66 , Issue.4 , pp. 1754-1758
    • Sugano, Y.1    Nakano, R.2
  • 252
    • 0037018885 scopus 로고    scopus 로고
    • Transformation of the edible mushroom Pleurotus ostreatus by particle bombardment
    • Sunagawa M, Magae Y.(2002) Transformation of the edible mushroom Pleurotus ostreatus by particle bombardment. FEMS Microbiol Lett.211(2):143-146
    • (2002) FEMS Microbiol Lett , vol.211 , Issue.2 , pp. 143-146
    • Sunagawa, M.1    Magae, Y.2
  • 253
    • 84867027657 scopus 로고    scopus 로고
    • P450 monooxygenases (P450ome) of the model white rot fungus Phanerochaete chrysosporium
    • Syed K, Yadav JS.(2012) P450 monooxygenases (P450ome) of the model white rot fungus Phanerochaete chrysosporium. Crit Rev Microbiol.38(4):339-363
    • (2012) Crit Rev Microbiol , vol.38 , Issue.4 , pp. 339-363
    • Syed, K.1    Yadav, J.S.2
  • 254
    • 77956265419 scopus 로고    scopus 로고
    • Genome-to-function characterization of novel fungal P450 monooxygenases oxidizing polycyclic aromatic hydrocarbons (PAHs)
    • Syed K, Doddapaneni H et al.(2010) Genome-to-function characterization of novel fungal P450 monooxygenases oxidizing polycyclic aromatic hydrocarbons (PAHs). Biochem Biophys Res Commun.399(4):492-497
    • (2010) Biochem Biophys Res Commun , vol.399 , Issue.4 , pp. 492-497
    • Syed, K.1    Doddapaneni, H.2
  • 255
    • 79954436898 scopus 로고    scopus 로고
    • Cytochrome b(5) reductase-cytochrome b(5) as an active P450 redox enzyme system in Phanerochaete chrysosporium:Atypical properties and in vivo evidence of electron transfer capability to CYP63A2
    • Syed K, Kattamuri C et al.(2011 a) Cytochrome b(5) reductase-cytochrome b(5) as an active P450 redox enzyme system in Phanerochaete chrysosporium:atypical properties and in vivo evidence of electron transfer capability to CYP63A2. Arch Biochem Biophys.509(1):26-32
    • (2011) Arch Biochem Biophys , vol.509 , Issue.1 , pp. 26-32
    • Syed, K.1    Kattamuri, C.2
  • 256
    • 82555175839 scopus 로고    scopus 로고
    • A fungal P450 (CYP5136A3) capable of oxidizing polycyclic aromatic hydrocarbons and endocrine disrupting alkylphenols: Role of Trp(129) and Leu(324)
    • Syed K, Porollo A et al.(2011 b) A fungal P450 (CYP5136A3) capable of oxidizing polycyclic aromatic hydrocarbons and endocrine disrupting alkylphenols: role of Trp(129) and Leu(324). PLoS One.6(12):e28286
    • (2011) PLoS One , vol.6 , Issue.12
    • Syed, K.1    Porollo, A.2
  • 257
    • 77956915511 scopus 로고    scopus 로고
    • H-bonding and positive charge at the N5/O4 locus are critical for covalent flavin attachment in Trametes pyranose 2-oxidase
    • Tan TC, Pitsawong W et al.(2010) H-bonding and positive charge at the N5/O4 locus are critical for covalent flavin attachment in Trametes pyranose 2-oxidase. J Mol Biol.402(3):578-594
    • (2010) J Mol Biol , vol.402 , Issue.3 , pp. 578-594
    • Tan, T.C.1    Pitsawong, W.2
  • 258
    • 79957747146 scopus 로고    scopus 로고
    • Regioselective control of beta-d-glucose oxidation by pyranose 2-oxidase is intimately coupled to conformational degeneracy
    • Tan TC, Haltrich D et al.(2011) Regioselective control of beta-d-glucose oxidation by pyranose 2-oxidase is intimately coupled to conformational degeneracy. J Mol Biol.409(4):588-600
    • (2011) J Mol Biol , vol.409 , Issue.4 , pp. 588-600
    • Tan, T.C.1    Haltrich, D.2
  • 259
    • 0032768558 scopus 로고    scopus 로고
    • Cloning and characterization of a second laccase gene from the lignindegrading basidiomycete Pycnoporus cinnabarinus
    • Temp U, Zierold U et al.(1999) Cloning and characterization of a second laccase gene from the lignindegrading basidiomycete Pycnoporus cinnabarinus. Gene.236(1):169-177
    • (1999) Gene , vol.236 , Issue.1 , pp. 169-177
    • Temp, U.1    Zierold, U.2
  • 260
    • 0032535618 scopus 로고    scopus 로고
    • 2-Chloro-1,4- dimethoxybenzene cation radical: Formation and role in the lignin peroxidase oxidation of anisyl alcohol
    • Teunissen PJ, Sheng D et al.(1998) 2-Chloro-1,4- dimethoxybenzene cation radical: formation and role in the lignin peroxidase oxidation of anisyl alcohol. Arch Biochem Biophys.360(2):233-238
    • (1998) Arch Biochem Biophys , vol.360 , Issue.2 , pp. 233-238
    • Teunissen, P.J.1    Sheng, D.2
  • 261
    • 37049181820 scopus 로고
    • Lignin-degrading enzyme from the Hymenomycete Phanerochaete chrysosporium Burds
    • Tien M, Kirk TK.(1983) Lignin-degrading enzyme from the Hymenomycete Phanerochaete chrysosporium Burds. Science (Washington, DC).221:661-663
    • (1983) Science (Washington, DC) , vol.221 , pp. 661-663
    • Tien, M.1    Kirk, T.K.2
  • 262
    • 0000230699 scopus 로고
    • Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase
    • Tien M, Kirk TK.(1984) Lignin-degrading enzyme from Phanerochaete chrysosporium: purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase. Proc Natl Acad Sci USA.81:2280-2284
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 2280-2284
    • Tien, M.1    Kirk, T.K.2
  • 263
    • 33750322286 scopus 로고    scopus 로고
    • Exclusive overproduction of recombinant versatile peroxidase MnP2 by genetically modified white rot fungus, Pleurotus ostreatus
    • Tsukihara T, Honda Y et al.(2006) Exclusive overproduction of recombinant versatile peroxidase MnP2 by genetically modified white rot fungus, Pleurotus ostreatus. J Biotechnol.126(4):431-439
    • (2006) J Biotechnol , vol.126 , Issue.4 , pp. 431-439
    • Tsukihara, T.1    Honda, Y.2
  • 264
    • 43049143502 scopus 로고    scopus 로고
    • Mechanism for oxidation of high-molecular-weight substrates by a fungal versatile peroxidase, MnP2
    • Tsukihara T, Honda Y et al.(2008) Mechanism for oxidation of high-molecular-weight substrates by a fungal versatile peroxidase, MnP2. Appl Environ Microbiol.74(9):2873-2881
    • (2008) Appl Environ Microbiol , vol.74 , Issue.9 , pp. 2873-2881
    • Tsukihara, T.1    Honda, Y.2
  • 265
    • 0026643601 scopus 로고
    • Oxidation of phenolic b-aryl ether lignin model compounds by mangansese peroxidase from Phanerochaete chrysosporium:Oxidative cleavage of an a-carbonyl model compound
    • Tuor U, Wariishii H et al.(1992) Oxidation of phenolic b-aryl ether lignin model compounds by mangansese peroxidase from Phanerochaete chrysosporium:oxidative cleavage of an a-carbonyl model compound. Biochemistry.31:4986-4995
    • (1992) Biochemistry , vol.31 , pp. 4986-4995
    • Tuor, U.1    Wariishii, H.2
  • 266
    • 27544451251 scopus 로고    scopus 로고
    • The haloperoxidase of the agaric fungus Agrocybe aegerita hydroxylates toluene and naphthalene
    • Ullrich R, HofrichterM(2005) The haloperoxidase of the agaric fungus Agrocybe aegerita hydroxylates toluene and naphthalene. FEBS Lett.579(27):6247-6250
    • (2005) FEBS Lett , vol.579 , Issue.27 , pp. 6247-6250
    • Ullrich, R.1    Hofrichter, M.2
  • 267
    • 0026053383 scopus 로고
    • Degradation of 2,4- dichlorophenol by the lignin-degrading fungus Phanerochaete chrysosporium
    • Valli K, Gold MH.(1991) Degradation of 2,4- dichlorophenol by the lignin-degrading fungus Phanerochaete chrysosporium. J Bacteriol.173(1):345-352
    • (1991) J Bacteriol , vol.173 , Issue.1 , pp. 345-352
    • Valli, K.1    Gold, M.H.2
  • 268
    • 0026599562 scopus 로고
    • Degradation of 2,4- dinitrotoluene by the lignin-degrading fungus Phanerochaete chrysosporium
    • Valli K, Brock J et al.(1992 a) Degradation of 2,4- dinitrotoluene by the lignin-degrading fungus Phanerochaete chrysosporium.Appl Environ Microbiol.58:221-228
    • (1992) Appl Environ Microbiol , vol.58 , pp. 221-228
    • Valli, K.1    Brock, J.2
  • 269
    • 0026517256 scopus 로고
    • Degradation of 2,7- dichlorodibenzo-p-dioxin by the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Valli K, Wariichi H et al.(1992 b) Degradation of 2,7- dichlorodibenzo-p-dioxin by the lignin-degrading basidiomycete Phanerochaete chrysosporium.J Bacteriol.174:2131-2137
    • (1992) J Bacteriol , vol.174 , pp. 2131-2137
    • Valli, K.1    Wariichi, H.2
  • 270
    • 0031805826 scopus 로고    scopus 로고
    • Phanerochaete chrysosporium cellobiohydrolase and cellobiose dehydrogenase transcripts in wood
    • Vallim MA, Janse BJ et al.(1998) Phanerochaete chrysosporium cellobiohydrolase and cellobiose dehydrogenase transcripts in wood. Appl Environ Microbiol.64(5):1924-1928
    • (1998) Appl Environ Microbiol , vol.64 , Issue.5 , pp. 1924-1928
    • Vallim, M.A.1    Janse, B.J.2
  • 271
    • 0033117627 scopus 로고    scopus 로고
    • Transformation and mineralization of 2,4,6-trinitrotoluene (TNT) by manganese peroxidase from the white-rot basidiomycete Phlebia radiata
    • Van Aken B, Hofrichter M et al.(1999) Transformation and mineralization of 2,4,6-trinitrotoluene (TNT) by manganese peroxidase from the white-rot basidiomycete Phlebia radiata. Biodegradation.10(2):83-91
    • (1999) Biodegradation , vol.10 , Issue.2 , pp. 83-91
    • Van Aken, B.1    Hofrichter, M.2
  • 272
    • 20444468865 scopus 로고    scopus 로고
    • The Phanerochaete chrysosporium secretome: Database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium
    • Vanden Wymelenberg A, Sabat G et al.(2005) The Phanerochaete chrysosporium secretome: database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium. J Biotechnol.118(1):17-34
    • (2005) J Biotechnol , vol.118 , Issue.1 , pp. 17-34
    • Vanden Wymelenberg, A.1    Sabat, G.2
  • 273
    • 33646123079 scopus 로고    scopus 로고
    • Computational analysis of the Phanerochaete chrysosporium v2.0 genome database and mass spectrometry identification of peptides in ligninolytic cultures reveals complex mixtures of secreted proteins
    • Vanden Wymelenberg A, Minges P et al.(2006 a) Computational analysis of the Phanerochaete chrysosporium v2.0 genome database and mass spectrometry identification of peptides in ligninolytic cultures reveals complex mixtures of secreted proteins.Fungal Genet Biol.43:343-356
    • (2006) Fungal Genet Biol , vol.43 , pp. 343-356
    • Vanden Wymelenberg, A.1    Minges, P.2
  • 274
    • 33746040871 scopus 로고    scopus 로고
    • Structure, organization, and transcriptional regulation of a family of copper radical oxidase genes in the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Vanden Wymelenberg A, Sabat G et al.(2006 b) Structure, organization, and transcriptional regulation of a family of copper radical oxidase genes in the lignin-degrading basidiomycete Phanerochaete chrysosporium.Appl Environ Microbiol.72:4871-4877
    • (2006) Appl Environ Microbiol , vol.72 , pp. 4871-4877
    • Vanden Wymelenberg, A.1    Sabat, G.2
  • 275
    • 67149111640 scopus 로고    scopus 로고
    • Transcriptome and secretome analysis of Phanerochaete chrysosporium reveal complex patterns of gene expression
    • Vanden Wymelenberg A, Gaskell J et al.(2009) Transcriptome and secretome analysis of Phanerochaete chrysosporium reveal complex patterns of gene expression. Appl Environ Microbiol.75:4058-4068
    • (2009) Appl Environ Microbiol , vol.75 , pp. 4058-4068
    • Vanden Wymelenberg, A.1    Gaskell, J.2
  • 276
    • 77953074402 scopus 로고    scopus 로고
    • Comparative transcriptome and secretome analysis of wood decay fungi Postia placenta and Phanerochaete chrysosporium
    • Vanden Wymelenberg A, Gaskell J et al.(2010) Comparative transcriptome and secretome analysis of wood decay fungi Postia placenta and Phanerochaete chrysosporium. Appl Environ Microbiol.76:3599-3610
    • (2010) Appl Environ Microbiol , vol.76 , pp. 3599-3610
    • Vanden Wymelenberg, A.1    Gaskell, J.2
  • 277
    • 79960107735 scopus 로고    scopus 로고
    • Significant alteration of gene expression in wood decay fungi Postia placenta and Phanerochaete chrysosporium by plant species
    • Vanden Wymelenberg A, Gaskell J et al.(2011) Significant alteration of gene expression in wood decay fungi Postia placenta and Phanerochaete chrysosporium by plant species. Appl Environ Microbiol.77(13):4499-4507
    • (2011) Appl Environ Microbiol , vol.77 , Issue.13 , pp. 4499-4507
    • Vanden Wymelenberg, A.1    Gaskell, J.2
  • 278
    • 0027958351 scopus 로고
    • Lignin peroxidase oxidation of aromatic compounds in systems containing organic solvents
    • Vazquez-Duhalt R, Westlake DWS et al.(1994) Lignin peroxidase oxidation of aromatic compounds in systems containing organic solvents. Appl Envrion Microbiol.60:459-466
    • (1994) Appl Envrion Microbiol , vol.60 , pp. 459-466
    • Vazquez-Duhalt, R.1    Westlake, D.W.S.2
  • 279
    • 0029871579 scopus 로고
    • The identification and characterization of four laccase genes from the plant pathogenic fungus Rhizoctonia solani
    • Wahleithmer JA, Xu F et al.(1995) The identification and characterization of four laccase genes from the plant pathogenic fungus Rhizoctonia solani. Curr Genet.29:395-403
    • (1995) Curr Genet , vol.29 , pp. 395-403
    • Wahleithmer, J.A.1    Xu, F.2
  • 280
    • 60249097290 scopus 로고    scopus 로고
    • Expression of lignin peroxidase H2 from Phanerochaete chrysosporium by multicopy recombinant Pichia strain
    • Wang W, Wen X.(2009) Expression of lignin peroxidase H2 from Phanerochaete chrysosporium by multicopy recombinant Pichia strain. J Environ Sci (China).21(2):218-222
    • (2009) J Environ Sci (China) , vol.21 , Issue.2 , pp. 218-222
    • Wang, W.1    Wen, X.2
  • 281
    • 21644452479 scopus 로고    scopus 로고
    • Heterologous expression of lignin peroxidase of Phanerochaete chrysosporium in Pichia methanolica
    • Wang H, Lu F et al.(2004) Heterologous expression of lignin peroxidase of Phanerochaete chrysosporium in Pichia methanolica. Biotechnol Lett.26(20):1569-1573
    • (2004) Biotechnol Lett , vol.26 , Issue.20 , pp. 1569-1573
    • Wang, H.1    Lu, F.2
  • 282
    • 0025769643 scopus 로고
    • In vitro depolymerization of lignin bymanganese peroxidase of Phanerochaete chrysosporium
    • Wariishi H, Valli K et al.(1991) In vitro depolymerization of lignin bymanganese peroxidase of Phanerochaete chrysosporium. Biochem Biophys Res Comm.176:269-275
    • (1991) Biochem Biophys Res Comm , vol.176 , pp. 269-275
    • Wariishi, H.1    Valli, K.2
  • 283
    • 77952754981 scopus 로고    scopus 로고
    • Characterization of a Delta12-fatty acid desaturase gene from Ceriporiopsis subvermispora, a selective lignin-degrading fungus
    • Watanabe T, Tsuda S et al.(2010) Characterization of a Delta12-fatty acid desaturase gene from Ceriporiopsis subvermispora, a selective lignin-degrading fungus. Appl Microbiol Biotechnol.87(1):215-224
    • (2010) Appl Microbiol Biotechnol , vol.87 , Issue.1 , pp. 215-224
    • Watanabe, T.1    Tsuda, S.2
  • 284
    • 0242661223 scopus 로고    scopus 로고
    • White-rot fungi and their enzymes for the treatment of industrial dye effluents
    • Wesenberg D, Kyriakides I et al.(2003) White-rot fungi and their enzymes for the treatment of industrial dye effluents. Biotechnol Adv.22(1-2):161-187
    • (2003) Biotechnol Adv , vol.22 , Issue.1-2 , pp. 161-187
    • Wesenberg, D.1    Kyriakides, I.2
  • 285
    • 81755166559 scopus 로고    scopus 로고
    • The putative endoglucanase PcGH61D from Phanerochaete chrysosporium is a metal-dependent oxidative enzyme that cleaves cellulose
    • Westereng B, Ishida T et al.(2011) The putative endoglucanase PcGH61D from Phanerochaete chrysosporium is a metal-dependent oxidative enzyme that cleaves cellulose. PLoS One.6(11):e27807
    • (2011) PLoS One , vol.6 , Issue.11
    • Westereng, B.1    Ishida, T.2
  • 286
  • 287
    • 0030046267 scopus 로고    scopus 로고
    • Glyoxal oxidase from Phanerochaete chrysosporium is a new radical-copper oxidase
    • Whittaker MM, Kersten PJ et al.(1996) Glyoxal oxidase from Phanerochaete chrysosporium is a new radical-copper oxidase. J Biol Chem.271(2):681-687
    • (1996) J Biol Chem , vol.271 , Issue.2 , pp. 681-687
    • Whittaker, M.M.1    Kersten, P.J.2
  • 288
    • 0033579474 scopus 로고    scopus 로고
    • Identification of catalytic residues in glyoxal oxidase by targeted mutagenesis
    • Whittaker MM, Kersten PJ et al.(1999) Identification of catalytic residues in glyoxal oxidase by targeted mutagenesis. J Biol Chem.274(51):36226-36232
    • (1999) J Biol Chem , vol.274 , Issue.51 , pp. 36226-36232
    • Whittaker, M.M.1    Kersten, P.J.2
  • 289
    • 84655160840 scopus 로고    scopus 로고
    • Biodegradation of dyes and polyaromatic hydrocarbons by two allelic forms of Lentinula edodes laccase expressed from Pichia pastoris
    • Wong KS, Huang Q et al.(2012) Biodegradation of dyes and polyaromatic hydrocarbons by two allelic forms of Lentinula edodes laccase expressed from Pichia pastoris. Bioresour Technol.104:157-164
    • (2012) Bioresour Technol , vol.104 , pp. 157-164
    • Wong, K.S.1    Huang, Q.2
  • 290
    • 81555196346 scopus 로고    scopus 로고
    • Identification of a catalytic base for sugar oxidation in the pyranose 2-oxidase reaction
    • Wongnate T, Sucharitakul J et al.(2011) Identification of a catalytic base for sugar oxidation in the pyranose 2-oxidase reaction. Chembiochem.12(17):2577-2586
    • (2011) Chembiochem , vol.12 , Issue.17 , pp. 2577-2586
    • Wongnate, T.1    Sucharitakul, J.2
  • 291
    • 0030093368 scopus 로고    scopus 로고
    • The integrative transformation of Pleurotus ostreatus using bialaphos resistance as a dominant selectable marker
    • Yanai K, Yonekura K et al.(1996) The integrative transformation of Pleurotus ostreatus using bialaphos resistance as a dominant selectable marker. Biosci Biotechnol Biochem.60(3):472-475
    • (1996) Biosci Biotechnol Biochem , vol.60 , Issue.3 , pp. 472-475
    • Yanai, K.1    Yonekura, K.2
  • 292
    • 0030605259 scopus 로고    scopus 로고
    • Cloning and characterization of three laccase genes from the white-rot basidiomycete Trametes villosa: Genomic organization of the laccase gene family
    • Yaver D, Golightly E.(1996) Cloning and characterization of three laccase genes from the white-rot basidiomycete Trametes villosa: genomic organization of the laccase gene family. Gene.181:95-102
    • (1996) Gene , vol.181 , pp. 95-102
    • Yaver, D.1    Golightly, E.2
  • 293
    • 13344270383 scopus 로고    scopus 로고
    • The purification, characterization, molecular cloning and expression of two laccase genes from the white-rot basidiomycete Trametes villosa
    • Yaver D, Xu F et al.(1996) The purification, characterization, molecular cloning and expression of two laccase genes from the white-rot basidiomycete Trametes villosa. Appl Environ Microbiol.62:834-841
    • (1996) Appl Environ Microbiol , vol.62 , pp. 834-841
    • Yaver, D.1    Xu, F.2
  • 294
    • 0032731212 scopus 로고    scopus 로고
    • Molecular characterization of laccase genes from the basidiomycete Coprinus cinereus and heterologous expression of the laccase lcc1
    • Yaver DS, Overjero MD et al.(1999) Molecular characterization of laccase genes from the basidiomycete Coprinus cinereus and heterologous expression of the laccase lcc1. Appl Environ Microbiol.65(11):4943-4948
    • (1999) Appl Environ Microbiol , vol.65 , Issue.11 , pp. 4943-4948
    • Yaver, D.S.1    Overjero, M.D.2
  • 295
    • 0035465380 scopus 로고    scopus 로고
    • Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris
    • Yoshida M, Ohira T et al.(2001) Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris. Biosci Biotechnol Biochem.65(9):2050-2057
    • (2001) Biosci Biotechnol Biochem , vol.65 , Issue.9 , pp. 2050-2057
    • Yoshida, M.1    Ohira, T.2
  • 296
    • 33745090845 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase- a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi
    • Zamocky M, Ludwig R et al.(2006) Cellobiose dehydrogenase- a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi. Curr Protein Pept Sci.7(3):255-280
    • (2006) Curr Protein Pept Sci , vol.7 , Issue.3 , pp. 255-280
    • Zamocky, M.1    Ludwig, R.2
  • 297
    • 42749094404 scopus 로고    scopus 로고
    • Cloning, sequence analysis and heterologous expression in Pichia pastoris of a gene encoding a thermostable cellobiose dehydrogenase from Myriococcum thermophilum
    • Zamocky M, Schumann C et al.(2008) Cloning, sequence analysis and heterologous expression in Pichia pastoris of a gene encoding a thermostable cellobiose dehydrogenase from Myriococcum thermophilum. Protein Expr Purif.59(2):258-265
    • (2008) Protein Expr Purif , vol.59 , Issue.2 , pp. 258-265
    • Zamocky, M.1    Schumann, C.2
  • 298
    • 0031867812 scopus 로고    scopus 로고
    • Cloning of Phanerochaete chrysosporium leu2 by complementation of bacterial auxotrophs and transformation of fungal auxotrophs
    • Zapanta LS, Hattori T et al.(1998) Cloning of Phanerochaete chrysosporium leu2 by complementation of bacterial auxotrophs and transformation of fungal auxotrophs. Appl Environ Microbiol.64(7):2624-2629
    • (1998) Appl Environ Microbiol , vol.64 , Issue.7 , pp. 2624-2629
    • Zapanta, L.S.1    Hattori, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.