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Volumn 13, Issue , 2014, Pages 175-208

Degradation and modification of plant biomass by fungi

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EID: 85023602228     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-642-45218-5_8     Document Type: Chapter
Times cited : (33)

References (229)
  • 1
    • 4243064911 scopus 로고
    • Lignin chemistry - past, present and future
    • Adler E(1977)Lignin chemistry - past, present and future. Wood Sci Technol11:169-218
    • (1977) Wood Sci Technol , vol.11 , pp. 169-218
    • Adler, E.1
  • 2
    • 0033563869 scopus 로고    scopus 로고
    • Oxalate oxidase from Ceriporiopsis subvermispora: Biochemical and cytochemical studies
    • Aguilar C, UrzUa U, Koenig C, Vicuna R(1999)Oxalate oxidase from Ceriporiopsis subvermispora: biochemical and cytochemical studies. Arch Biochem Biophys366:275-282
    • (1999) Arch Biochem Biophys , vol.366 , pp. 275-282
    • Aguilar, C.1    Urzua, U.2    Koenig, C.3    Vicuna, R.4
  • 4
    • 84872827801 scopus 로고    scopus 로고
    • Mapping the polysaccharide degradation potential of Aspergillus niger
    • Andersen MR, Giese M, Vries PR, Nielsen J (2012)Mapping the polysaccharide degradation potential of Aspergillus niger.BMC Genomics13:313
    • (2012) BMC Genomics , vol.13 , pp. 313
    • Andersen, M.R.1    Giese, M.2    Vries, P.R.3    Nielsen, J.4
  • 5
    • 0035968258 scopus 로고    scopus 로고
    • ACEII, a novel transcriptional activator involved in regulation of cellulase and xylanase genes of Tricho-derma reesei
    • Aro N, Saloheimo M, Ilmen M, Penttila M (2001)ACEII, a novel transcriptional activator involved in regulation of cellulase and xylanase genes of Tricho-derma reesei.J Biol Chem276:24309-24314
    • (2001) J Biol Chem , vol.276 , pp. 24309-24314
    • Aro, N.1    Saloheimo, M.2    Ilmen, M.3    Penttila, M.4
  • 6
    • 0037226849 scopus 로고    scopus 로고
    • ACEI, of Trichoderma reesei is a repressor of cellulase and xylanase expression
    • Aro N, Saloheimo M, Ilmen M, Penttila M (2003)ACEI, of Trichoderma reesei is a repressor of cellulase and xylanase expression. Appl Environ Microbiol69:56-65
    • (2003) Appl Environ Microbiol , vol.69 , pp. 56-65
    • Aro, N.1    Saloheimo, M.2    Ilmen, M.3    Penttila, M.4
  • 8
    • 79960716870 scopus 로고    scopus 로고
    • Analysis of regulation of pentose utilisation in Aspergillus niger reveals evolutionary adaptations in the Eurotiales
    • Battaglia E, Visser L, Nijssen A, van Veluw J, Wosten HAB, de Vries RP (2011b)Analysis of regulation of pentose utilisation in Aspergillus niger reveals evolutionary adaptations in the Eurotiales. Stud Mycol69:31-38
    • (2011) Stud Mycol , vol.69 , pp. 31-38
    • Battaglia, E.1    Visser, L.2    Nijssen, A.3    Van Veluw, J.4    Wosten, H.5    De Vries, R.P.6
  • 9
    • 84866932780 scopus 로고    scopus 로고
    • Degradation of different pectins by fungi: Correlations and contrasts between the pectinolytic enzyme sets identified in genomes and the growth on pectins of different origin
    • Benoit I, Coutinho PM, Schols HA, Gerlach JP, Henrissat B, de Vries RP (2012)Degradation of different pectins by fungi: correlations and contrasts between the pectinolytic enzyme sets identified in genomes and the growth on pectins of different origin. BMC Genomics13:321
    • (2012) BMC Genomics , vol.13 , pp. 321
    • Benoit, I.1    Coutinho, P.M.2    Schols, H.A.3    Gerlach, J.P.4    Henrissat, B.5    De Vries, R.P.6
  • 11
    • 33744520321 scopus 로고    scopus 로고
    • Cytochromes P450 as versatile biocatalysts
    • Bernhardt R(2006)Cytochromes P450 as versatile biocatalysts. J Biotechnol124:128-145
    • (2006) J Biotechnol , vol.124 , pp. 128-145
    • Bernhardt, R.1
  • 12
    • 0000507332 scopus 로고
    • Degradation of the lignocellulose complex in wood
    • Blanchette RA(1995)Degradation of the lignocellulose complex in wood. Can J Bot73:S999-S1010
    • (1995) Can J Bot , vol.73
    • Blanchette, R.A.1
  • 13
    • 72649085431 scopus 로고    scopus 로고
    • Class II peroxidase-encoding genes are present in a phylogenetically wide range of ecto-mycorrhizal fungi
    • Bodeker IT, Nygren CMA, Taylor F, Olson A, Lindahl BD(2009)Class II peroxidase-encoding genes are present in a phylogenetically wide range of ecto-mycorrhizal fungi. ISME J3:1387-1395
    • (2009) ISME J , vol.3 , pp. 1387-1395
    • Bodeker, I.T.1    Nygren, C.2    Taylor, F.3    Olson, A.4    Lindahl, B.D.5
  • 15
    • 0029737394 scopus 로고    scopus 로고
    • Expression of lip genes during growth in soil and oxidation of anthracene by Phanerochaete chryso-sporium
    • Bogan B, Schoenike B, Lamar R, Cullen D (1996) Expression of lip genes during growth in soil and oxidation of anthracene by Phanerochaete chryso-sporium. Appl Environ Microbiol62:3697-3703
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3697-3703
    • Bogan, B.1    Schoenike, B.2    Lamar, R.3    Cullen, D.4
  • 16
    • 0029031691 scopus 로고
    • PCR-mediated analysis of lignocellulolytic gene transcription by Phanerochaete chrysosporium: Substrate-dependent differential expression within gene-families
    • Broda P, Birch PRJ, Brooks PR, Sims PFG(1995)PCR-mediated analysis of lignocellulolytic gene transcription by Phanerochaete chrysosporium: substrate-dependent differential expression within gene-families. Appl Environ Microbiol61:2358-2364
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2358-2364
    • Broda, P.1    Birch, P.2    Brooks, P.R.3    Sims, P.4
  • 18
    • 49649093960 scopus 로고    scopus 로고
    • Lignin in straw of herbaceous crops
    • Buranov AU, Mazza G(2008)Lignin in straw of herbaceous crops. Ind Crop Prod 28:237-259
    • (2008) Ind Crop Prod , vol.28 , pp. 237-259
    • Buranov, A.U.1    Mazza, G.2
  • 19
    • 0030864381 scopus 로고    scopus 로고
    • Relationship between the nature of lignin and the morphology of degradation performed by white-rot fungi
    • Burlat V, Ambert K, Ruel K, Joseleau J-P (1997) Relationship between the nature of lignin and the morphology of degradation performed by white-rot fungi. Plant Physiol Biochem35:645-654
    • (1997) Plant Physiol Biochem , vol.35 , pp. 645-654
    • Burlat, V.1    Ambert, K.2    Ruel, K.3    Joseleau, J.-P.4
  • 21
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth
    • Carpita NC, Gibeaut DM(1993)Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. Plant J3:1-30
    • (1993) Plant J , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 31
    • 0037364791 scopus 로고    scopus 로고
    • Regulation of Aspergillus genes encoding plant cell wall polysaccharide degrading enzymes; relevance for industrial production
    • de Vries RP(2003)Regulation of Aspergillus genes encoding plant cell wall polysaccharide degrading enzymes; relevance for industrial production. Appl Microbiol Biotechnol61:10-20
    • (2003) Appl Microbiol Biotechnol , vol.61 , pp. 10-20
    • De Vries, R.P.1
  • 32
    • 0035199524 scopus 로고    scopus 로고
    • Aspergillus enzymes involved in degradation of plant cell wall polysaccharides
    • de Vries RP, Visser J (2001) Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microb Mol Biol Rev65:497-522
    • (2001) Microb Mol Biol Rev , vol.65 , pp. 497-522
    • De Vries, R.P.1    Visser, J.2
  • 33
    • 0032758304 scopus 로고    scopus 로고
    • CreA modulates the XlnR-induced expression on xylose ofAspergillus niger genes involved in xylan degradation
    • de Vries RP, Visser J, de Graaff LH(1999)CreA modulates the XlnR-induced expression on xylose ofAspergillus niger genes involved in xylan degradation. Res Microbiol150:281-285
    • (1999) Res Microbiol , vol.150 , pp. 281-285
    • De Vries, R.P.1    Visser, J.2    De Graaff, L.H.3
  • 39
    • 0029660710 scopus 로고    scopus 로고
    • Oxalate production by fungi: Its role in pathogenicity and ecology in the soil environment
    • Dutton MV, Evans CS (1996)Oxalate production by fungi: its role in pathogenicity and ecology in the soil environment. Can J Microbiol42:881-895
    • (1996) Can J Microbiol , vol.42 , pp. 881-895
    • Dutton, M.V.1    Evans, C.S.2
  • 41
    • 0022572161 scopus 로고
    • Formation and partial characterization of glucose-2-oxidase, a hydrogen peroxide producing enzyme in Phanerochaete chrysosporium
    • Eriksson KE, Pettersson B, Volc J, Musilek V (1986)Formation and partial characterization of glucose-2-oxidase, a hydrogen peroxide producing enzyme in Phanerochaete chrysosporium. Appl Microbiol Biotechnol23:257-262
    • (1986) Appl Microbiol Biotechnol , vol.23 , pp. 257-262
    • Eriksson, K.E.1    Pettersson, B.2    Volc, J.3    Musilek, V.4
  • 44
    • 0028351015 scopus 로고
    • Enzymes and small molecular mass agents involved with lignocellulose degradation
    • Evans CS, Dutton MV, Guillen F, Veness RG (1994)Enzymes and small molecular mass agents involved with lignocellulose degradation. FEMS Microbiol Rev13:235-240
    • (1994) FEMS Microbiol Rev , vol.13 , pp. 235-240
    • Evans, C.S.1    Dutton, M.V.2    Guillen, F.3    Veness, R.G.4
  • 45
    • 84941833404 scopus 로고
    • Degradation of gymnosperm (Guaiacyl) vs. Angiosperm (syringyl/guaiacyl) lignins by Phanerochaete chrysosporium
    • Faix O, Mozuch MD, Kirk TK (1985)Degradation of gymnosperm (guaiacyl) vs. angiosperm (syringyl/guaiacyl) lignins by Phanerochaete chrysosporium. Holzforschung39:203-208
    • (1985) Holzforschung , vol.39 , pp. 203-208
    • Faix, O.1    Mozuch, M.D.2    Kirk, T.K.3
  • 53
    • 0034533834 scopus 로고    scopus 로고
    • Fungal pyranose oxidases: Occurrence, properties and biotechnical applications in carbohydrate chemistry
    • Giffhorn F (2000)Fungal pyranose oxidases: occurrence, properties and biotechnical applications in carbohydrate chemistry. Appl Microbiol Biotechnol54: 727-740
    • (2000) Appl Microbiol Biotechnol , vol.54 , pp. 727-740
    • Giffhorn, F.1
  • 54
    • 43849084710 scopus 로고    scopus 로고
    • How the walls come crumbling down: Recent structural biochemistry of plant polysaccharide degradation
    • Gilbert HJ, Stalbrand H, Brumer H (2008)How the walls come crumbling down: recent structural biochemistry of plant polysaccharide degradation. Curr Opin Plant Biol11:338-348
    • (2008) Curr Opin Plant Biol , vol.11 , pp. 338-348
    • Gilbert, H.J.1    Stalbrand, H.2    Brumer, H.3
  • 55
    • 0021101692 scopus 로고
    • An extracellular H2O2-requiring enzyme preparation involved in lignin biodegradation by the white rot basidiomycete Phanerochaete chrysosporium
    • 2-requiring enzyme preparation involved in lignin biodegradation by the white rot basidiomycete Phanerochaete chrysosporium.Biochem Biophys Res Commun114: 1077-1083
    • (1983) Biochem Biophys Res Commun , vol.114 , pp. 1077-1083
    • Glenn, J.K.1    Morgan, M.A.2    Mayfield, M.B.3    Kuwahara, M.4    Gold, M.H.5
  • 57
    • 67349230848 scopus 로고    scopus 로고
    • Abortiporus biennis tolerance to insoluble metal oxides: Oxalate secretion, oxalate oxidase activity, and mycelia morphology
    • Graz M, Jarosz-Wilkolazka A, Pawlikowska-Pawlga B (2009) Abortiporus biennis tolerance to insoluble metal oxides: oxalate secretion, oxalate oxidase activity, and mycelia morphology. Biometals22: 401-410
    • (2009) Biometals , vol.22 , pp. 401-410
    • Graz, M.1    Jarosz-Wilkolazka, A.2    Pawlikowska-Pawlga, B.3
  • 58
    • 84885850548 scopus 로고    scopus 로고
    • Novel transcriptional activators of Aspergillus involved in plant biomass utilization
    • PhD thesis, Utrecht University
    • Gruben BS (2012)Novel transcriptional activators of Aspergillus involved in plant biomass utilization. Microbiology. PhD thesis, Utrecht University
    • (2012) Microbiology
    • Gruben, B.S.1
  • 59
    • 0028173943 scopus 로고
    • Hydrogen peroxide-producing system of Pleurotus erygii involving the extracellular enzyme aryl-alcohol oxidase
    • Guillen F, Martinez AT, Martinez MJ, Evans CS (1994)Hydrogen peroxide-producing system of Pleurotus erygii involving the extracellular enzyme aryl-alcohol oxidase. Appl Microbiol Biotechnol41:465-470
    • (1994) Appl Microbiol Biotechnol , vol.41 , pp. 465-470
    • Guillen, F.1    Martinez, A.T.2    Martinez, M.J.3    Evans, C.S.4
  • 60
    • 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 Biol11:349-355
    • (2008) Curr Opin Plant Biol , vol.11 , pp. 349-355
    • Hammel, K.E.1    Cullen, D.2
  • 62
    • 0030815324 scopus 로고    scopus 로고
    • Structural characterization of novel L-galac-tose-containing oligosaccharide subunits of jojoba seed xyloglucans
    • Hantus S, Pauly M, Darvill AG, Albersheim P, York WS (1997)Structural characterization of novel L-galac-tose-containing oligosaccharide subunits of jojoba seed xyloglucans. Carbohydr Res304:11-20
    • (1997) Carbohydr Res , vol.304 , pp. 11-20
    • Hantus, S.1    Pauly, M.2    Darvill, A.G.3    Albersheim, P.4    York, W.S.5
  • 65
    • 0033028156 scopus 로고    scopus 로고
    • Cell wall crosslinking by ferulates and diferulates in grasses
    • Hatfield RD, Ralph J, Grabber JH (1999)Cell wall crosslinking by ferulates and diferulates in grasses. J Sci Food Agric79:403-407
    • (1999) J Sci Food Agric , vol.79 , pp. 403-407
    • Hatfield, R.D.1    Ralph, J.2    Grabber, J.H.3
  • 66
    • 0032145444 scopus 로고    scopus 로고
    • Purification and characterization of peroxidases from the dye-decolorizing fungus Bjerkandera adusta
    • Heinfling A, Martinez MJ, Martinez AT, Bergbauer M, Szewzyk U (1998a)Purification and characterization of peroxidases from the dye-decolorizing fungus Bjerkandera adusta.FEMS Microbiol Lett165:43-50
    • (1998) FEMS Microbiol Lett , vol.165 , pp. 43-50
    • Heinfling, A.1    Martinez, M.J.2    Martinez, A.T.3    Bergbauer, M.4    Szewzyk, U.5
  • 67
    • 0032577520 scopus 로고    scopus 로고
    • A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta
    • Heinfling A, Ruiz-Dueüas FJ, Martinez MJ, Bergbauer M, Szewzyk U, Martinez AT (1998b)A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta.FEBS Lett428:141-146
    • (1998) FEBS Lett , vol.428 , pp. 141-146
    • Heinfling, A.1    Ruiz-Dueüas, F.J.2    Martinez, M.J.3    Bergbauer, M.4    Szewzyk, U.5    Martinez, A.T.6
  • 68
    • 84857914934 scopus 로고    scopus 로고
    • Fungal aryl-alcohol oxidase: A peroxide-producing flavoenzyme involved in lignin degradation
    • Hernndez-Ortega A, Ferreira P, Martinez AT (2012)Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation. Appl Microbiol Biotechnol93:1395-1410
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 1395-1410
    • Hernndez-Ortega, A.1    Ferreira, P.2    Martinez, A.T.3
  • 70
    • 33644614039 scopus 로고    scopus 로고
    • Look back over the studies of lignin biochemistry
    • Higuchi T (2006)Look back over the studies of lignin biochemistry. J Wood Sci52:2-8
    • (2006) J Wood Sci , vol.52 , pp. 2-8
    • Higuchi, T.1
  • 71
    • 16244401504 scopus 로고    scopus 로고
    • The two manganese peroxidases Pr-MnP2 and Pr-MnP3 of Phlebia radiata, alignin-degradingbasidiomycete, are phylogenetically and structurally divergent
    • Hilden K, Martinez AT, Hatakka A, Lundell T (2005)The two manganese peroxidases Pr-MnP2 and Pr-MnP3 of Phlebia radiata, alignin-degradingbasidiomycete, are phylogenetically and structurally divergent. Fungal Genet Biol42:403-419
    • (2005) Fungal Genet Biol , vol.42 , pp. 403-419
    • Hilden, K.1    Martinez, A.T.2    Hatakka, A.3    Lundell, T.4
  • 72
    • 31444447716 scopus 로고    scopus 로고
    • Expression on wood, molecular cloning and characterization of three lignin peroxidase (LiP) encoding genes of the white rot fungus Phlebia radiata
    • Hilden KS, Mäkela MR, Hakala TK, Hatakka A, Lundell T (2006)Expression on wood, molecular cloning and characterization of three lignin peroxidase (LiP) encoding genes of the white rot fungus Phlebia radiata. Curr Genet49:97-105
    • (2006) Curr Genet , vol.49 , pp. 97-105
    • Hilden, K.S.1    Mäkela, M.R.2    Hakala, T.K.3    Hatakka, A.4    Lundell, T.5
  • 73
    • 0026413030 scopus 로고
    • The structure of plant cell walls. 31. A new undecasaccharide subunit of xyloglu-cans with 2 a-L-fucosyl residues
    • Hisamatsu M, Impallomeni G, York WS, Albersheim P, Darvill AG (1991)The structure of plant cell walls. 31. A new undecasaccharide subunit of xyloglu-cans with 2 a-L-fucosyl residues. Carbohydr Res211:117-129
    • (1991) Carbohydr Res , vol.211 , pp. 117-129
    • Hisamatsu, M.1    Impallomeni, G.2    York, W.S.3    Albersheim, P.4    Darvill, A.G.5
  • 74
    • 0027113468 scopus 로고
    • Characterization of seven xyloglucan oligosaccharides containing from seventeen to twenty glycosyl residues
    • Hisamatsu M, York WS, Darvill AG, Albersheim P (1992)Characterization of seven xyloglucan oligosaccharides containing from seventeen to twenty glycosyl residues. Carbohydr Res227:45-71
    • (1992) Carbohydr Res , vol.227 , pp. 45-71
    • Hisamatsu, M.1    York, W.S.2    Darvill, A.G.3    Albersheim, P.4
  • 75
    • 33646268426 scopus 로고    scopus 로고
    • Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences
    • Hoegger PJ, Kilaru S, James TY, Thacker JR, Kuäes U (2006)Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences. FEBS J273:2308-2326
    • (2006) FEBS J , vol.273 , pp. 2308-2326
    • Hoegger, P.J.1    Kilaru, S.2    James, T.Y.3    Thacker, J.R.4    Kuäes, U.5
  • 76
    • 33749051652 scopus 로고    scopus 로고
    • Heme-thiolate haloperox-idases: Versatile biocatalysts with biotechnological and environmental significance
    • Hofrichter M, Ullrich R (2006)Heme-thiolate haloperox-idases: versatile biocatalysts with biotechnological and environmental significance. Appl Microbiol Biotechnol71:276-288
    • (2006) Appl Microbiol Biotechnol , vol.71 , pp. 276-288
    • Hofrichter, M.1    Ullrich, R.2
  • 78
    • 79959976450 scopus 로고    scopus 로고
    • Effects of xylan and starch on secretome of the basidiomycete Phanerochaete chrysosporium grown on cellulose
    • Hori C, Igarashi K, Katayama A, Samejima M (2011)Effects of xylan and starch on secretome of the basidiomycete Phanerochaete chrysosporium grown on cellulose. FEMS Microbiol Lett321: 14-23
    • (2011) FEMS Microbiol Lett , vol.321 , pp. 14-23
    • Hori, C.1    Igarashi, K.2    Katayama, A.3    Samejima, M.4
  • 80
    • 84255186582 scopus 로고    scopus 로고
    • Fleming’s penicillin producing strain is not Penicillium chry-sogenum but P. Rubens
    • Houbraken J, Frisvad JC, Samson RA (2011)Fleming’s penicillin producing strain is not Penicillium chry-sogenum but P. rubens.IMA Fungus2:87-95
    • (2011) IMA Fungus , vol.2 , pp. 87-95
    • Houbraken, J.1    Frisvad, J.C.2    Samson, R.A.3
  • 81
    • 0342854313 scopus 로고    scopus 로고
    • Xyloglucan from soybean (Glycine max) meal is composed of XXXG-type building units
    • Huisman MMH, Weel KGC, Schols HA, Voragen AGJ (2000)Xyloglucan from soybean (Glycine max) meal is composed of XXXG-type building units. Carbohydr Polym42:185-191
    • (2000) Carbohydr Polym , vol.42 , pp. 185-191
    • Huisman, M.1    Weel, K.2    Schols, H.A.3    Voragen, A.4
  • 83
    • 34250346536 scopus 로고    scopus 로고
    • Multiple sequential steps involved in the binding of inhibitors to cytochrome P450 3A4
    • Isin EM, Guengerich FP (2007)Multiple sequential steps involved in the binding of inhibitors to cytochrome P450 3A4. J Biol Chem282:6863-6874
    • (2007) J Biol Chem , vol.282 , pp. 6863-6874
    • Isin, E.M.1    Guengerich, F.P.2
  • 85
    • 0037123263 scopus 로고    scopus 로고
    • Characterization of water-soluble hemicelluloses from spruce and aspen employing SEC/MALDI mass spectroscopy
    • Jacobs A, Lundqvist J, Stalbrand H, Tjerneld F, Dahl-man O (2002)Characterization of water-soluble hemicelluloses from spruce and aspen employing SEC/MALDI mass spectroscopy. Carbohydr Res337:711-717
    • (2002) Carbohydr Res , vol.337 , pp. 711-717
    • Jacobs, A.1    Lundqvist, J.2    Stalbrand, H.3    Tjerneld, F.4    Dahl-Man, O.5
  • 86
    • 0032169337 scopus 로고    scopus 로고
    • Expression of Phanerochaete chrysosporium genes encoding lignin peroxidases, manganese peroxidases, and glyoxal oxidase in wood
    • Janse BJH, Gaskell J, Akhtar M, Cullen D (1998)Expression of Phanerochaete chrysosporium genes encoding lignin peroxidases, manganese peroxidases, and glyoxal oxidase in wood. Appl Environ Microbiol64: 3536-3538
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3536-3538
    • Janse, B.1    Gaskell, J.2    Akhtar, M.3    Cullen, D.4
  • 88
    • 10144254415 scopus 로고    scopus 로고
    • Manganese-dependent cleavage of nonpheno-lic lignin structures by Ceriporiopsis subvermispora in the absence of lignin peroxidase
    • Jensen KA, Bao W, Kawai S, Srebotnik E, Hammel KE (1996)Manganese-dependent cleavage of nonpheno-lic lignin structures by Ceriporiopsis subvermispora in the absence of lignin peroxidase. Appl Environ Microbiol62:3679-3686
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3679-3686
    • Jensen, K.A.1    Bao, W.2    Kawai, S.3    Srebotnik, E.4    Hammel, K.E.5
  • 89
    • 0035379763 scopus 로고    scopus 로고
    • Pathways for extracellular Fenton chemistry in the brown rot basidiomycete Gloeophyllum trabeum
    • Jensen KAJ, Houtman CJ, Ryan ZC, Hammel KE (2001) Pathways for extracellular Fenton chemistry in the brown rot basidiomycete Gloeophyllum trabeum. Appl Environ Microbiol 67:2705-2711
    • (2001) Appl Environ Microbiol , vol.67 , pp. 2705-2711
    • Jensen, K.1    Houtman, C.J.2    Ryan, Z.C.3    Hammel, K.E.4
  • 90
    • 0029878517 scopus 로고    scopus 로고
    • A cluster of genes encoding major isozymes of lignin peroxidase and manganese peroxidase from the white-rot fungus Trametes versicolor
    • Johansson T, Nyman PO (1996) A cluster of genes encoding major isozymes of lignin peroxidase and manganese peroxidase from the white-rot fungus Trametes versicolor.Gene 170:31-38
    • (1996) Gene , vol.170 , pp. 31-38
    • Johansson, T.1    Nyman, P.O.2
  • 93
    • 80053368669 scopus 로고    scopus 로고
    • Carbohydrate degrading enzyme production by plant pathogenic mycelia and microsclerotia isolates of Macrophomina phaseolina through koji fermentation
    • Kaur S, Dhillon GS, Brar SK, Chauhan VB (2012) Carbohydrate degrading enzyme production by plant pathogenic mycelia and microsclerotia isolates of Macrophomina phaseolina through koji fermentation. Ind Crop Prod 36:140-148
    • (2012) Ind Crop Prod , vol.36 , pp. 140-148
    • Kaur, S.1    Dhillon, G.S.2    Brar, S.K.3    Chauhan, V.B.4
  • 94
    • 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 166:269-274
    • (1986) J Bacteriol , vol.166 , pp. 269-274
    • Kelley, R.L.1    Reddy, C.A.2
  • 95
    • 0032985079 scopus 로고    scopus 로고
    • Biodegradative mechanism of the brown rot basidiomycete Gloeo-phyllum trabeum: Evidence for an extracellular hydroquinone-driven fenton reaction
    • Kerem Z, Jensen KA, Hammel KE (1999) Biodegradative mechanism of the brown rot basidiomycete Gloeo-phyllum trabeum: evidence for an extracellular hydroquinone-driven fenton reaction. FEBS Lett 446:49-54
    • (1999) FEBS Lett , vol.446 , pp. 49-54
    • Kerem, Z.1    Jensen, K.A.2    Hammel, K.E.3
  • 96
    • 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 U S A 87: 2936-2940
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 2936-2940
    • Kersten, P.J.1
  • 97
    • 0027242188 scopus 로고
    • Cloning and characterization of a cDNA encoding glyoxal oxidase, a peroxide-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • Kersten P, Cullen D (1993) Cloning and characterization of a cDNA encoding glyoxal oxidase, a peroxide-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium. Proc Natl Acad Sci U S A 90:7411-7413
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 7411-7413
    • Kersten, P.1    Cullen, D.2
  • 98
    • 0025883180 scopus 로고
    • Molecular analysis of a Bjerkandera adusta lignin peroxidase gene
    • Kimura Y, Asada Y, Oka T, Kuwahara M (1991) Molecular analysis of a Bjerkandera adusta lignin peroxidase gene. Appl Microbiol Biotechnol 35:510-514
    • (1991) Appl Microbiol Biotechnol , vol.35 , pp. 510-514
    • Kimura, Y.1    Asada, Y.2    Oka, T.3    Kuwahara, M.4
  • 99
    • 0003014888 scopus 로고    scopus 로고
    • Enzymology and molecular genetics of wood degradation by white-rot fungi
    • Young RA, Akhtar M, Wiley, New York
    • Kirk TK, Cullen D (1998) Enzymology and molecular genetics of wood degradation by white-rot fungi. In: Young RA, Akhtar M (eds) Environmentally friendly technologies for the pulp and paper industry. Wiley, New York, pp 273-307
    • (1998) Environmentally Friendly Technologies for the Pulp and Paper Industry , pp. 273-307
    • Kirk, T.K.1    Cullen, D.2
  • 100
    • 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
  • 101
    • 0025043403 scopus 로고
    • Quantification and identification of the main components of the Trichoderma cellulase complex with monoclonal antibodies using an enzyme-linked immunosorbent assay (ELISA)
    • Kolbe J, Kubicek CP (1990) Quantification and identification of the main components of the Trichoderma cellulase complex with monoclonal antibodies using an enzyme-linked immunosorbent assay (ELISA). Appl Microbiol Biotechnol 34:26-30
    • (1990) Appl Microbiol Biotechnol , vol.34 , pp. 26-30
    • Kolbe, J.1    Kubicek, C.P.2
  • 102
    • 0016937944 scopus 로고
    • Determination of the structure ofcellulose II
    • Kolpak FJ, Blackwell J (1976) Determination of the structure ofcellulose II. Macromolecules 9:273-278
    • (1976) Macromolecules , vol.9 , pp. 273-278
    • Kolpak, F.J.1    Blackwell, J.2
  • 103
    • 0026576254 scopus 로고
    • Evidence that cellobiose oxidase from Phanerochete chrysosporium is primarily an Fe(III) reductase
    • Kremer SM, Wood PM (1992a) Evidence that cellobiose oxidase from Phanerochete chrysosporium is primarily an Fe(III) reductase. Eur J Biochem 205:133-138
    • (1992) Eur J Biochem , vol.205 , pp. 133-138
    • Kremer, S.M.1    Wood, P.M.2
  • 104
    • 0026674531 scopus 로고
    • Production of Fenton’s reagent by cellobiose oxidase from cellulolytic cultures of Phanerochaete chrysosporium
    • Kremer SM, Wood PM (1992b) Production of Fenton’s reagent by cellobiose oxidase from cellulolytic cultures of Phanerochaete chrysosporium. Eur J Bio-chem 208:807-814
    • (1992) Eur J Bio-Chem , vol.208 , pp. 807-814
    • Kremer, S.M.1    Wood, P.M.2
  • 105
    • 79955575438 scopus 로고    scopus 로고
    • Multiple multi-copper oxidase gene families in Basidiomycetes - what for?
    • Kües U, Rühl M (2011) Multiple multi-copper oxidase gene families in Basidiomycetes - what for? Curr Genomics 12:72-94
    • (2011) Curr Genomics , vol.12 , pp. 72-94
    • Kües, U.1    Rühl, M.2
  • 106
    • 0029120976 scopus 로고
    • The manganese binding site of manganese peroxidase: Characterization of an Asp179Asn site-directed mutant protein
    • Kusters-van Someren M, Kishi K, Lundell T, Gold MH (1995) The manganese binding site of manganese peroxidase: characterization of an Asp179Asn site-directed mutant protein. Biochemistry 34: 10620-10627
    • (1995) Biochemistry , vol.34 , pp. 10620-10627
    • Kusters-Van Someren, M.1    Kishi, K.2    Lundell, T.3    Gold, M.H.4
  • 107
    • 81755178934 scopus 로고    scopus 로고
    • Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61
    • Langston JA, Shaghasi T, Abbate E, Xu F, Vlasenko E, Sweeney MD (2011) Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61. Appl Environ Microbiol 77:7007-7015
    • (2011) Appl Environ Microbiol , vol.77 , pp. 7007-7015
    • Langston, J.A.1    Shaghasi, T.2    Abbate, E.3    Xu, F.4    Vlasenko, E.5    Sweeney, M.D.6
  • 109
    • 0035862065 scopus 로고    scopus 로고
    • Heterologous expression of a thermostable manganese peroxidase from Dichomitus squalens in Phanerochaete chrysosporium
    • Li DM, Youngs HL, Gold MH (2001) Heterologous expression of a thermostable manganese peroxidase from Dichomitus squalens in Phanerochaete chrysosporium. Arch Biochem Biophys 385: 348-356
    • (2001) Arch Biochem Biophys , vol.385 , pp. 348-356
    • Li, D.M.1    Youngs, H.L.2    Gold, M.H.3
  • 110
    • 34547741043 scopus 로고    scopus 로고
    • Identification of genes encoding microbial glucuronoyl esterase
    • Li X-L, Spnikov S, de Vries RP, Biely P (2007) Identification of genes encoding microbial glucuronoyl esterase. FEBS Lett 581:4029-4036
    • (2007) FEBS Lett , vol.581 , pp. 4029-4036
    • Li, X.-L.1    Spnikov, S.2    De Vries, R.P.3    Biely, P.4
  • 112
    • 76849083614 scopus 로고    scopus 로고
    • DyP-like peroxidases of the jelly fungus Auri-cularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes
    • Liers C, Bobeth C, Pecyna M, Ullrich R, Hofrichter M (2010) DyP-like peroxidases of the jelly fungus Auri-cularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes. Appl Microbiol Biotechnol 85:1869-1879
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 1869-1879
    • Liers, C.1    Bobeth, C.2    Pecyna, M.3    Ullrich, R.4    Hofrichter, M.5
  • 113
    • 77950948619 scopus 로고    scopus 로고
    • The intra- and extracellular proteome of Aspergillus niger growing on defined medium with xylose or maltose as carbon substrate
    • Lu X, Sun J, Nimtz M, Wissing J, Zeng AP, Rinas U (2010) The intra- and extracellular proteome of Aspergillus niger growing on defined medium with xylose or maltose as carbon substrate. Microb Cell Fact 9:23
    • (2010) Microb Cell Fact , vol.9 , pp. 23
    • Lu, X.1    Sun, J.2    Nimtz, M.3    Wissing, J.4    Zeng, A.P.5    Rinas, U.6
  • 114
    • 77049096911 scopus 로고    scopus 로고
    • Lignin-modifying enzymes in filamentous basidio-mycetes: Ecological, functional and phylogenetic review
    • Lundell T, Makela MR, Hilden K (2010) Lignin-modifying enzymes in filamentous basidio-mycetes: ecological, functional and phylogenetic review. J Basic Microbiol 50:5-20
    • (2010) J Basic Microbiol , vol.50 , pp. 5-20
    • Lundell, T.1    Makela, M.R.2    Hilden, K.3
  • 116
    • 79958235330 scopus 로고    scopus 로고
    • Transcrip-tomic responses of the softwood-degrading white-rot fungus Phanerochaete carnosaduring growth on coniferous and deciduous wood
    • MacDonald J, Doering M, Canam T, Gong YC, Guttman DS, Campbell MM, Master ER (2011) Transcrip-tomic responses of the softwood-degrading white-rot fungus Phanerochaete carnosaduring 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    Canam, T.3    Gong, Y.C.4    Guttman, D.S.5    Campbell, M.M.6    Master, E.R.7
  • 117
    • 77952882025 scopus 로고    scopus 로고
    • Proteomic characterization of lignocellulose-degrading enzymes secreted by Phanerochaete carnosa grown on spruce and microcrystalline cellulose
    • Mahajan S, Master ER (2010) Proteomic characterization of lignocellulose-degrading enzymes secreted by Phanerochaete carnosa grown on spruce and microcrystalline cellulose. Appl Microbiol Biotechnol 86:1903-1914
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 1903-1914
    • Mahajan, S.1    Master, E.R.2
  • 118
    • 69949176414 scopus 로고    scopus 로고
    • Oxalate decarboxylase of the white-rot fungus Dichomitus squalens demonstrates a novel enzyme primary structure and non-induced expression on wood and in liquid cultures
    • Makela MR, Hilden K, Hatakka A, Lundell TK (2009) Oxalate decarboxylase of the white-rot fungus Dichomitus squalens demonstrates a novel enzyme primary structure and non-induced expression on wood and in liquid cultures. Microbiology 155: 2726-2738
    • (2009) Microbiology , vol.155 , pp. 2726-2738
    • Makela, M.R.1    Hilden, K.2    Hatakka, A.3    Lundell, T.K.4
  • 119
    • 77955660027 scopus 로고    scopus 로고
    • Oxalate decarboxylase: Biotechnological update and prevalence of the enzyme in filamentous fungi
    • Makela MR, Hilden K, Lundell T (2010) Oxalate decarboxylase: biotechnological update and prevalence of the enzyme in filamentous fungi. Appl Microbiol Biotechnol 87:801-814
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 801-814
    • Makela, M.R.1    Hilden, K.2    Lundell, T.3
  • 120
    • 84895544034 scopus 로고    scopus 로고
    • Oxalate-metabolising genes of the white-rot fungus Dichomitus squalens are dif-ferentially induced on wood and at high proton concentration
    • Makela MR, Sietio O-M, de Vries RP, Timonen S, Hildeen KS (2014) Oxalate-metabolising genes of the white-rot fungus Dichomitus squalens are dif-ferentially induced on wood and at high proton concentration. PLoS One 9:e87959
    • (2014) Plos One , vol.9
    • Makela, M.R.1    Sietio, O.-M.2    De Vries, R.P.3    Timonen, S.4    Hildeen, K.S.5
  • 121
    • 82455171991 scopus 로고    scopus 로고
    • ITRAQ-based quantitative secretome analysis of Phanerochaete chrysosporium
    • Manavalan A, Adav SS, Sze SK (2011) ITRAQ-based quantitative secretome analysis of Phanerochaete chrysosporium. J Proteomics 75:642-654
    • (2011) J Proteomics , vol.75 , pp. 642-654
    • Manavalan, A.1    Adav, S.S.2    Sze, S.K.3
  • 123
    • 0029926079 scopus 로고    scopus 로고
    • Purification and catalytic properties of two manganese-peroxidase isoenzymes from Pleurotus eryngii
    • Martínez MJ, Ruiz-Dueñas FJ, Guillén F, Martínez AT (1996) Purification and catalytic properties of two manganese-peroxidase isoenzymes from Pleurotus eryngii. Eur J Biochem 237:424-432
    • (1996) Eur J Biochem , vol.237 , pp. 424-432
    • Martínez, M.J.1    Ruiz-Dueñas, F.J.2    Guillén, F.3    Martínez, A.T.4
  • 128
  • 129
    • 41649114122 scopus 로고    scopus 로고
    • A xyloglucan-specific family 12 glycosyl hydrolase from Aspergillus niger. Recombinant expression, purification and characterization
    • Master ER, Zheng Y, Storms R, Tsang A, Powlowski J (2008) A xyloglucan-specific family 12 glycosyl hydrolase from Aspergillus niger. recombinant expression, purification and characterization. Bio-chem J 411:161-170
    • (2008) Bio-Chem J , vol.411 , pp. 161-170
    • Master, E.R.1    Zheng, Y.2    Storms, R.3    Tsang, A.4    Powlowski, J.5
  • 130
    • 0022406038 scopus 로고
    • Purification and properties of an alpha-D-xylosidase from Aspergillus niger
    • Matsushita J, Kato Y, Matsuda K (1985) Purification and properties of an alpha-D-xylosidase from Aspergillus niger. J Biochem 98:825-832
    • (1985) J Biochem , vol.98 , pp. 825-832
    • Matsushita, J.1    Kato, Y.2    Matsuda, K.3
  • 131
    • 85024470744 scopus 로고
    • Characterization of a-D-xylosidase II from Aspergillus niger
    • Matsushita J, Kato Y, Matsuda K (1987) Characterization of a-D-xylosidase II from Aspergillus niger. Agric Biol Chem 51:2
    • (1987) Agric Biol Chem , vol.51 , pp. 2
    • Matsushita, J.1    Kato, Y.2    Matsuda, K.3
  • 132
    • 76349090892 scopus 로고    scopus 로고
    • Molecular characterization of lignin peroxidase from the white-rot basidiomycete Trametes cervina: A novel fungal peroxidase
    • Miki Y, Ichinose H, Wariishi H (2010) Molecular characterization of lignin peroxidase from the white-rot basidiomycete Trametes cervina: a novel fungal peroxidase. FEMS Microbiol Lett 304:39-46
    • (2010) FEMS Microbiol Lett , vol.304 , pp. 39-46
    • Miki, Y.1    Ichinose, H.2    Wariishi, H.3
  • 133
    • 0001060734 scopus 로고    scopus 로고
    • Biosynthesis of pectins and galacto-mannans
    • Barton D, Nakanishi K, Meth-Cohn O, Elsevier, Dordrecht
    • Mohnen D (1999) Biosynthesis of pectins and galacto-mannans. In: Barton D, Nakanishi K, Meth-Cohn O (eds) Comprehensive natural products chemistry. Elsevier, Dordrecht, pp 497-527
    • (1999) Comprehensive Natural Products Chemistry , pp. 497-527
    • Mohnen, D.1
  • 134
    • 78049254041 scopus 로고    scopus 로고
    • Characterization of three mnp genes of Fomitiporia mediterranea and report of additional class II peroxidases in the order Hymenochaetales
    • Morgenstern I, Robertson DL, Hibbett DS (2010) Characterization of three mnp genes of Fomitiporia mediterranea and report of additional class II peroxidases in the order Hymenochaetales. Appl Environ Microbiol 76:6431-6440
    • (2010) Appl Environ Microbiol , vol.76 , pp. 6431-6440
    • Morgenstern, I.1    Robertson, D.L.2    Hibbett, D.S.3
  • 136
    • 64049118903 scopus 로고    scopus 로고
    • Reduced genomic potential for secreted plant cell-wall-degrading enzymes in the ectomycorrhizal fungus Amanita bisporigera, based on the secretome of Trichoderma reesei
    • Nagendran S, Hallen-Adams HE, Paper JM, Aslam N, Walton JD (2009) Reduced genomic potential for secreted plant cell-wall-degrading enzymes in the ectomycorrhizal fungus Amanita bisporigera, based on the secretome of Trichoderma reesei. Fungal Genet Biol 46:427-435
    • (2009) Fungal Genet Biol , vol.46 , pp. 427-435
    • Nagendran, S.1    Hallen-Adams, H.E.2    Paper, J.M.3    Aslam, N.4    Walton, J.D.5
  • 137
    • 84856252744 scopus 로고    scopus 로고
    • The effect of acetylated xylan and sugar beet pulp on the expres-sion and secretion of enzymes by Penicillium purpurogenum
    • Navarrete M, Callegari E, Eyzaguirre J (2012) The effect of acetylated xylan and sugar beet pulp on the expres-sion and secretion of enzymes by Penicillium purpurogenum. Appl Microbiol Biotechnol 93: 723-741
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 723-741
    • Navarrete, M.1    Callegari, E.2    Eyzaguirre, J.3
  • 139
    • 0024288734 scopus 로고
    • Ligninolytic enzymes of the white-rot fungus Phlebia radiata
    • Niku-Paavola M-L, Karhunen E, Salola P, Raunio V (1988) Ligninolytic enzymes of the white-rot fungus Phlebia radiata. Biochem J 254:877-884
    • (1988) Biochem J , vol.254 , pp. 877-884
    • Niku-Paavola, M.-L.1    Karhunen, E.2    Salola, P.3    Raunio, V.4
  • 141
    • 0029788024 scopus 로고    scopus 로고
    • Rhamno-galacturonan-II, a pectic polysaccharide in the walls of growing plant cell, forms a dimer that is covalently-linked by a borate ester
    • O’Neill MA, Warrenfeltz D, Kates K, Pellerin P, Doci T, Darvill AG, Albersheim P (1996) Rhamno-galacturonan-II, a pectic polysaccharide in the walls of growing plant cell, forms a dimer that is covalently-linked by a borate ester. J Biol Chem 271:22923-22930
    • (1996) J Biol Chem , vol.271 , pp. 22923-22930
    • O’neill, M.A.1    Warrenfeltz, D.2    Kates, K.3    Pellerin, P.4    Doci, T.5    Darvill, A.G.6    Albersheim, P.7
  • 142
    • 84869880446 scopus 로고    scopus 로고
    • ManR, a novel Zn(II)(2)Cys(6) transcriptional activator, controls the beta-mannan utilization system in Aspergillus oryzae
    • Ogawa M, Kobayashi T, Koyama Y (2012) ManR, a novel Zn(II)(2)Cys(6) transcriptional activator, controls the beta-mannan utilization system in Aspergillus oryzae. Fungal Genet Biol 49:987-995
    • (2012) Fungal Genet Biol , vol.49 , pp. 987-995
    • Ogawa, M.1    Kobayashi, T.2    Koyama, Y.3
  • 146
    • 27644453559 scopus 로고    scopus 로고
    • Alcohol oxidase: A complex peroxisomal, oligomeric flavoprotein
    • Ozimek P, Veenhuis M, van der Klei IJ (2005) Alcohol oxidase: a complex peroxisomal, oligomeric flavoprotein. FEMS Yeast Res 5:975-983
    • (2005) FEMS Yeast Res , vol.5 , pp. 975-983
    • Ozimek, P.1    Veenhuis, M.2    Van Der Klei, I.J.3
  • 148
    • 0032942942 scopus 로고    scopus 로고
    • A xyloglucan-specific endo-beta-1,4-glucanase from Aspergillus aculeatus: Expression cloning in yeast, purification and characterization of the recombinant enzyme
    • Pauly M, Andersen LN, Kauppinen S, Kofod LV, York WS, Albersheim P, Darvill A (1999) A xyloglucan-specific endo-beta-1,4-glucanase from Aspergillus aculeatus: expression cloning in yeast, purification and characterization of the recombinant enzyme. Glycobiology 9:93-100
    • (1999) Glycobiology , vol.9 , pp. 93-100
    • Pauly, M.1    Ersen, L.N.2    Kauppinen, S.3    Kofod, L.V.4    York, W.S.5    Albersheim, P.6    Darvill, A.7
  • 150
    • 27644552270 scopus 로고    scopus 로고
    • Versatile peroxidase oxidation of high redox potential aromatic compounds: Site-directed mutagenesis, spectroscopic and crystallo-graphic investigation of three long-range electron transfer pathways
    • Pérez-Boada M, Ruiz-Duefias FJ, Pogni R, Basosi R, Choinowski T, Martinez MJ, Piontek K, Martinez AT (2005) Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallo-graphic investigation of three long-range electron transfer pathways. J Mol Biol 354:385-402
    • (2005) J Mol Biol , vol.354 , pp. 385-402
    • Pérez-Boada, M.1    Ruiz-Duefias, F.J.2    Pogni, R.3    Basosi, R.4    Choinowski, T.5    Martinez, M.J.6    Piontek, K.7    Martinez, A.T.8
  • 151
    • 0033381253 scopus 로고    scopus 로고
    • A new transcriptional activator for amylase genes in Aspergillus
    • Petersen KL, Lehmbeck J, Christensen T (1999) A new transcriptional activator for amylase genes in Aspergillus. Mol Gen Genet 262:668-676
    • (1999) Mol Gen Genet , vol.262 , pp. 668-676
    • Petersen, K.L.1    Lehmbeck, J.2    Christensen, T.3
  • 152
    • 79958286762 scopus 로고    scopus 로고
    • Secretome of the coprophilous fungus Doratomyces stemonitis C8, isolated from koala feces
    • Peterson R, Grinyer J, Nevalainen H (2011) Secretome of the coprophilous fungus Doratomyces stemonitis C8, isolated from koala feces. Appl Environ Microbiol 77:3793-3801
    • (2011) Appl Environ Microbiol , vol.77 , pp. 3793-3801
    • Peterson, R.1    Grinyer, J.2    Nevalainen, H.3
  • 153
    • 84055197660 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa
    • Phillips CM, Beeson WT, Cate JH, Marletta MA (2011a) Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. ACS Chem Biol 6:1399-1406
    • (2011) ACS Chem Biol , vol.6 , pp. 1399-1406
    • Phillips, C.M.1    Beeson, W.T.2    Cate, J.H.3    Marletta, M.A.4
  • 154
    • 80052450370 scopus 로고    scopus 로고
    • Quantitative proteomic approach for cellulose degradation by Neurospora crassa
    • Phillips CM, Iavarone AT, Marletta MA (2011b) Quantitative proteomic approach for cellulose degradation by Neurospora crassa. J Proteome Res 10:4177-4185
    • (2011) J Proteome Res , vol.10 , pp. 4177-4185
    • Phillips, C.M.1    Iavarone, A.T.2    Marletta, M.A.3
  • 155
    • 0027514481 scopus 로고
    • Low pH crystal structure of glyoxylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 A resolution
    • Piontek K, Glumoff T, Winterhalter K (1993) Low pH crystal structure of glyoxylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 A resolution. FEBS Lett 315:119-124
    • (1993) FEBS Lett , vol.315 , pp. 119-124
    • Piontek, K.1    Glumoff, T.2    Winterhalter, K.3
  • 158
    • 0027514159 scopus 로고
    • Crystallographic refinement of lignin peroxidase at 2-A
    • Poulos T, Edwards S, Wariishi H, Gold M (1993) Crystallographic refinement of lignin peroxidase at 2-A. J Biol Chem 268:4429-4440
    • (1993) J Biol Chem , vol.268 , pp. 4429-4440
    • Poulos, T.1    Edwards, S.2    Wariishi, H.3    Gold, M.4
  • 160
    • 6344288191 scopus 로고    scopus 로고
    • Lignins: Natural polymers from oxidativecoupling of 4-hydroxyphenylpropanoids
    • Ralph J, Lundquist K, Brunow G, Lu F, Kim H, Schatz PF et al (2004) Lignins: natural polymers from oxidativecoupling of 4-hydroxyphenylpropanoids. Phytochem Rev 3:29-60
    • (2004) Phytochem Rev , vol.3 , pp. 29-60
    • Ralph, J.1    Lundquist, K.2    Brunow, G.3    Lu, F.4    Kim, H.5    Schatz, P.F.6
  • 162
    • 0035800186 scopus 로고    scopus 로고
    • Pectins: Structure, biosynthesis, and oligogalacturonide-related signaling
    • Ridley BL, O’Neill MA, Mohnen D (2001) Pectins: structure, biosynthesis, and oligogalacturonide-related signaling. Phytochemistry 57:929-967
    • (2001) Phytochemistry , vol.57 , pp. 929-967
    • Ridley, B.L.1    O’neill, M.A.2    Mohnen, D.3
  • 164
    • 79952051826 scopus 로고    scopus 로고
    • Molecular and structural modeling of the Phanerochaete flavido-alba extracellular laccase reveals its ferroxidase structure
    • Rodriguez-Rincon F, Suarez A, Lucas M, Larrondo LF, de laRubia T, Polaina J, Martinez J (2010) Molecular and structural modeling of the Phanerochaete flavido-alba extracellular laccase reveals its ferroxidase structure. Arch Microbiol 192:883-892
    • (2010) Arch Microbiol , vol.192 , pp. 883-892
    • Rodriguez-Rincon, F.1    Suarez, A.2    Lucas, M.3    Larrondo, L.F.4    De Larubia, T.5    Polaina, J.6    Martinez, J.7
  • 166
    • 0030739496 scopus 로고    scopus 로고
    • Carbon repression in aspergilli
    • Ruijter GJG, Visser J (1997) Carbon repression in aspergilli. FEMS Microbiol Lett 151:103-114
    • (1997) FEMS Microbiol Lett , vol.151 , pp. 103-114
    • Ruijter, G.1    Visser, J.2
  • 167
    • 36849060628 scopus 로고    scopus 로고
    • Evaluation of steam explosion pretreatment for enzymatic hydrolysis of sunflower stalks
    • Ruiz E, Cara C, Manzanares P, Ballesteros M, Castro E (2008) Evaluation of steam explosion pretreatment for enzymatic hydrolysis of sunflower stalks. Enzyme Microb Technol 42:160-166
    • (2008) Enzyme Microb Technol , vol.42 , pp. 160-166
    • Ruiz, E.1    Cara, C.2    Manzanares, P.3    Ballesteros, M.4    Castro, E.5
  • 168
    • 67649799362 scopus 로고    scopus 로고
    • Microbial degradation of lignin: How a bulky recalcitrant polymer is efficiently recycled in nature and how we can take advantage of this
    • Ruiz-Duefias FJ, Martinez AT (2009) Microbial degradation of lignin: how a bulky recalcitrant polymer is efficiently recycled in nature and how we can take advantage of this. Microb Biotechnol 2: 164-177
    • (2009) Microb Biotechnol , vol.2 , pp. 164-177
    • Ruiz-Duefias, F.J.1    Martinez, A.T.2
  • 171
    • 0034253281 scopus 로고    scopus 로고
    • Alpha-L-arabinofuranosidases: Biochemistry, molecular biology and application in biotechnology
    • Saha BC (2000) Alpha-L-arabinofuranosidases: biochemistry, molecular biology and application in biotechnology. Biotechnol Adv 18:403-423
    • (2000) Biotechnol Adv , vol.18 , pp. 403-423
    • Saha, B.C.1
  • 172
    • 62949114581 scopus 로고    scopus 로고
    • Cloning of Lentinula edodes lemnp2, a manganese peroxidase that is secreted abundantly in sawdust medium
    • Sakamoto Y, Nakade K, Nagai M, Uchimiya H, Sato T (2009) Cloning of Lentinula edodes lemnp2, a manganese peroxidase that is secreted abundantly in sawdust medium. Mycoscience 50:116-122
    • (2009) Mycoscience , vol.50 , pp. 116-122
    • Sakamoto, Y.1    Nakade, K.2    Nagai, M.3    Uchimiya, H.4    Sato, T.5
  • 173
    • 34948842973 scopus 로고    scopus 로고
    • Expression analysis of extracellular proteins from Phanerochaete chrysosporium grown on different liquid and solid substrates
    • Sato S, Liu F, Koc H, Tien M (2007) Expression analysis of extracellular proteins from Phanerochaete chrysosporium grown on different liquid and solid substrates. Microbiology 153:3023-3033
    • (2007) Microbiology , vol.153 , pp. 3023-3033
    • Sato, S.1    Liu, F.2    Koc, H.3    Tien, M.4
  • 174
    • 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, Iyer P, Tien M (2009) The first genome-level transcriptome of the wood-degrading fungus Phanerochaete chrysosporium grown on red oak. Curr Genet 55:273-286
    • (2009) Curr Genet , vol.55 , pp. 273-286
    • Sato, S.1    Feltus, F.A.2    Iyer, P.3    Tien, M.4
  • 176
    • 34250112701 scopus 로고
    • The failure of nitrogen and lignin control of decomposition in a North American desert
    • Schaefer D, Steinberger Y, Whitford WG (1985) The failure of nitrogen and lignin control of decomposition in a North American desert. Oecologia 65: 382-386
    • (1985) Oecologia , vol.65 , pp. 382-386
    • Schaefer, D.1    Steinberger, Y.2    Whitford, W.G.3
  • 177
    • 29144497204 scopus 로고    scopus 로고
    • Envoy, a PAS/LOV domain protein of Hypocrea jecorina (Anamorph Trichoderma reesei), modulates cellu-lase gene transcription in response to light
    • Schmoll M, Franchi L, Kubicek CP (2005) Envoy, a PAS/LOV domain protein of Hypocrea jecorina (Anamorph Trichoderma reesei), modulates cellu-lase gene transcription in response to light. Eukar-yot Cell 4:1998-2007
    • (2005) Eukar-Yot Cell , vol.4 , pp. 1998-2007
    • Schmoll, M.1    Franchi, L.2    Kubicek, C.P.3
  • 178
    • 84859091370 scopus 로고    scopus 로고
    • Unravelling the molecular basis for light modulated cellulase gene expression - the role of photoreceptors in Neurospora crassa
    • Schmoll M, Tian C, Sun J, Tisch D, Glass NL (2012) Unravelling the molecular basis for light modulated cellulase gene expression - the role of photoreceptors in Neurospora crassa. BMC Genomics 13:127
    • (2012) BMC Genomics , vol.13 , pp. 127
    • Schmoll, M.1    Tian, C.2    Sun, J.3    Tisch, D.4    Glass, N.L.5
  • 179
    • 0000020415 scopus 로고    scopus 로고
    • Complex pectins: Structure elucidation using enzymes
    • Visser J, Voragen AGJ, Elsevier Science, Amsterdam
    • Schols HA, Voragen AGJ (1996) Complex pectins: structure elucidation using enzymes. In: Visser J, Voragen AGJ (eds) Pectin and pectinases. Elsevier Science, Amsterdam, pp 793-798
    • (1996) Pectin and Pectinases , pp. 793-798
    • Schols, H.A.1    Voragen, A.2
  • 180
  • 181
    • 67649172586 scopus 로고    scopus 로고
    • A proteomic study of pectin-degrading enzymes secreted by Botrytis cinerea grown in liquid culture
    • Shah P, Gutierrez-Sanchez G, Orlando R, Bergmann C (2009) A proteomic study of pectin-degrading enzymes secreted by Botrytis cinerea grown in liquid culture. Proteomics 9:3126-3135
    • (2009) Proteomics , vol.9 , pp. 3126-3135
    • Shah, P.1    Gutierrez-Sanchez, G.2    Orlando, R.3    Bergmann, C.4
  • 183
    • 0001157257 scopus 로고
    • Microbial, enzymatic and biomimetic degradation of lignin
    • Hon DNS, Shiraishi N (eds),. Dekker, New York
    • Shimada M, Higuchi T (1991) Microbial, enzymatic and biomimetic degradation of lignin. In: Hon DNS, Shiraishi N (eds) Wood and cellulosic chemistry. Dekker, New York, pp 557-619
    • (1991) Wood and Cellulosic Chemistry , pp. 557-619
    • Shimada, M.1    Higuchi, T.2
  • 184
    • 0342941155 scopus 로고    scopus 로고
    • Possible biochemical roles of oxalic acid as a low molecular weight compound involved in brown-rot and white-rot wood decays
    • Shimada M, Akamatsu Y, Tokimatsu T, Mii K, Hattori T (1997) Possible biochemical roles of oxalic acid as a low molecular weight compound involved in brown-rot and white-rot wood decays. J Biotech-nol 53:103-113
    • (1997) J Biotech-Nol , vol.53 , pp. 103-113
    • Shimada, M.1    Akamatsu, Y.2    Tokimatsu, T.3    Mii, K.4    Hattori, T.5
  • 186
    • 0001614479 scopus 로고    scopus 로고
    • Chemical composition of wood and pulps: Basic components and their distribution
    • Sjostrom E, Alen R, Springer, Berlin
    • Sjostrom E, Westermark U (1998) Chemical composition of wood and pulps: basic components and their distribution. In: Sjostrom E, Alen R (eds) Analytical methods in wood chemistry, pulping, and papermaking. Springer, Berlin, pp 1-35
    • (1998) Analytical Methods in Wood Chemistry, Pulping, and Papermaking , pp. 1-35
    • Sjostrom, E.1    Westermark, U.2
  • 188
    • 16844376038 scopus 로고    scopus 로고
    • Seed galactomannans: An overview
    • Srivastava M, Kapoor VP (2005) Seed galactomannans: an overview. Chem Biodivers 2:295-317
    • (2005) Chem Biodivers , vol.2 , pp. 295-317
    • Srivastava, M.1    Kapoor, V.P.2
  • 190
    • 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
  • 191
    • 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, Vanden Wymelenberg A, Gaskell J, Cullen D (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    Vanden Wymelenberg, A.3    Gaskell, J.4    Cullen, D.5
  • 192
    • 67349235552 scopus 로고    scopus 로고
    • DyP-type peroxidases comprise a novel heme peroxidase family
    • Sugano Y (2009) DyP-type peroxidases comprise a novel heme peroxidase family. Cell Mol Life Sci 66:1387-1403
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1387-1403
    • Sugano, Y.1
  • 193
    • 69949132971 scopus 로고    scopus 로고
    • Cloning and homologous expression of novel lignin peroxidase genes in the white-rot fungus Phanerochaete sordida YK-624
    • Sugiura T, Yamagishi K, Kimura T, Nishida T, Kawa-gishi H, Hirai H (2009) Cloning and homologous expression of novel lignin peroxidase genes in the white-rot fungus Phanerochaete sordida YK-624. Biosci Biotechnol Biochem 73:1793-1798
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 1793-1798
    • Sugiura, T.1    Yamagishi, K.2    Kimura, T.3    Nishida, T.4    Kawa-Gishi, H.5    Hirai, H.6
  • 194
    • 80053321725 scopus 로고    scopus 로고
    • Identification of the CRE-1 cellulolytic regulon in Neurospora crassa
    • Sun J, Glass NL (2011) Identification of the CRE-1 cellulolytic regulon in Neurospora crassa. PLoS One 6:e25654
    • (2011) Plos One , vol.6
    • Sun, J.1    Glass, N.L.2
  • 195
    • 0028587337 scopus 로고
    • The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution
    • Sundaramoorthy M, Kishi K, Gold M, Poulos T (1994) The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution. J Biol Chem 269:32759-32767
    • (1994) J Biol Chem , vol.269 , pp. 32759-32767
    • Sundaramoorthy, M.1    Kishi, K.2    Gold, M.3    Poulos, T.4
  • 197
    • 77956818710 scopus 로고    scopus 로고
    • Cellotriose and cellotetraose as inducers of the genes encoding cellobiohydrolases in the basidiomycete Pha-nerochaete chrysosporium
    • Suzuki H, Igarashi K, Samejima M (2010) Cellotriose and cellotetraose as inducers of the genes encoding cellobiohydrolases in the basidiomycete Pha-nerochaete chrysosporium. Appl Environ Microbiol 76:6164-6170
    • (2010) Appl Environ Microbiol , vol.76 , pp. 6164-6170
    • Suzuki, H.1    Igarashi, K.2    Samejima, M.3
  • 199
    • 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 38:339363
    • (2012) Crit Rev Microbiol , vol.38 , pp. 339363
    • Syed, K.1    Yadav, J.S.2
  • 200
    • 0032488874 scopus 로고    scopus 로고
    • Purification and characterization of two lignin peroxidase isozymes produced by Bjerkan-dera sp. Strain BOS55
    • ten Have R, Hartmans S, Teunissen PJM, Field JA (1998) Purification and characterization of two lignin peroxidase isozymes produced by Bjerkan-dera sp. strain BOS55. FEBS Lett 422:391-394
    • (1998) FEBS Lett , vol.422 , pp. 391-394
    • Ten Have, R.1    Hartmans, S.2    Teunissen, P.3    Field, J.A.4
  • 202
    • 0000230699 scopus 로고
    • Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, char-acterizationand catalytic properties of a unique H2O2-requiring oxygenase
    • 2-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
  • 203
    • 0031985659 scopus 로고    scopus 로고
    • Manganese peroxidase-dependent oxidation of glyoxylic acid synthetized by Ceriporiopsis subvermispora produces extracellular hydrogen peroxide
    • Urziua U, Kersten PJ, Vicuña R (1998) Manganese peroxidase-dependent oxidation of glyoxylic acid synthetized by Ceriporiopsis subvermispora produces extracellular hydrogen peroxide. Appl Environ Microbiol 64:68-73
    • (1998) Appl Environ Microbiol , vol.64 , pp. 68-73
    • Urziua, U.1    Kersten, P.J.2    Vicuña, R.3
  • 204
  • 206
    • 0031660773 scopus 로고    scopus 로고
    • The transcriptional activator XlnR regulates both xylanolytic and endogluca-nase gene expression in Aspergillus niger
    • van PeijN, Gielkens MMC, de Vries RP, Visser J, de Graaff LH (1998a) The transcriptional activator XlnR regulates both xylanolytic and endogluca-nase gene expression in Aspergillus niger. Appl Environ Microbiol 64:3615-3619
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3615-3619
    • Van, P.1    Gielkens, M.2    De Vries, R.P.3    Visser, J.4    De Graaff, L.H.5
  • 207
    • 0031962771 scopus 로고    scopus 로고
    • Isolation and analysis of xlnR, encoding a transcriptional activator co-ordinating xylanolytic expression in Aspergillus niger
    • van PeijNN, Visser J, de Graaff LH (1998b) Isolation and analysis of xlnR, encoding a transcriptional activator co-ordinating xylanolytic expression in Aspergillus niger. Mol Microbiol 27:131-142
    • (1998) Mol Microbiol , vol.27 , pp. 131-142
    • Van, P.1    Visser, J.2    De Graaff, L.H.3
  • 209
    • 20444468865 scopus 로고    scopus 로고
    • The Phanerochaete chrysosporium secre-tome: Database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium
    • Vanden Wymelenberg AV, Sabat G, Martinez D, Rajan-gam AS, Teeri TT, Gaskell J, Kersten PJ, Cullen D (2005) The Phanerochaete chrysosporium secre-tome: database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium. J Biotechnol 118:17-34
    • (2005) J Biotechnol , vol.118 , pp. 17-34
    • Vanden Wymelenberg, A.V.1    Sabat, G.2    Martinez, D.3    Rajan-Gam, A.S.4    Teeri, T.T.5    Gaskell, J.6    Kersten, P.J.7    Cullen, D.8
  • 211
    • 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, Mozuch M, Kersten PJ, Cullen D, Blanchette RA (2006b) Structure, organization, and transcriptional regulation of a family of copper radical oxidase genes in the lignin-degrading basidiomycete Phanerochaete chrysosporium. Appl Environ Microbiol 72:48714877
    • (2006) Appl Environ Microbiol , vol.72 , pp. 48714877
    • Vanden Wymelenberg, A.1    Sabat, G.2    Mozuch, M.3    Kersten, P.J.4    Cullen, D.5    Blanchette, R.A.6
  • 215
    • 0142104391 scopus 로고    scopus 로고
    • Effect of pH and oxalate on hydroquinone-derived hydroxyl radical formation during brown rot wood degradation
    • Varela E, Tien M (2003) Effect of pH and oxalate on hydroquinone-derived hydroxyl radical formation during brown rot wood degradation. Appl Environ Microbiol 69:6025-6031
    • (2003) Appl Environ Microbiol , vol.69 , pp. 6025-6031
    • Varela, E.1    Tien, M.2
  • 216
    • 0035831250 scopus 로고    scopus 로고
    • Expression of Pleurotus eryngii aryl-alcohol oxidase in Aspergillus nidulans: Purification and characterization of the recombinant enzyme
    • Varela E, Guillén F, Martínez AT, Martínez MJ (2001) Expression of Pleurotus eryngii aryl-alcohol oxidase in Aspergillus nidulans: purification and characterization of the recombinant enzyme. Bio-chim Biophys Acta 1546:107-113
    • (2001) Bio-Chim Biophys Acta , vol.1546 , pp. 107-113
    • Varela, E.1    Guillén, F.2    Martínez, A.T.3    Martínez, M.J.4
  • 217
    • 0028803412 scopus 로고
    • Lignin peroxidases, manganese peroxidases, and other ligninolytic enzymes produced by Phlebia radiata during solid-state fermentation of wheat straw
    • Vares T, Kalsi M, Hatakka A (1995) Lignin peroxidases, manganese peroxidases, and other ligninolytic enzymes produced by Phlebia radiata during solid-state fermentation of wheat straw. Appl Environ Microbiol 61:3515-3520
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3515-3520
    • Vares, T.1    Kalsi, M.2    Hatakka, A.3
  • 218
    • 0034734003 scopus 로고    scopus 로고
    • Structural characterization of the pectic polysaccharide rhamnogalacturonan II: Evidence for the backbone location of the aceric acid-containing oligoglycosyl side chain
    • Vidal S, Doco T, Williams P, Pellerin P, York WS, O’Neill MA, Glushka J, Darvill AG, Albersheim P (2000) Structural characterization of the pectic polysaccharide rhamnogalacturonan II: evidence for the backbone location of the aceric acid-containing oligoglycosyl side chain. Carbohydr Res 326:227-294
    • (2000) Carbohydr Res , vol.326 , pp. 227-294
    • Vidal, S.1    Doco, T.2    Williams, P.3    Pellerin, P.4    York, W.S.5    O’neill, M.A.6    Glushka, J.7    Darvill, A.G.8    Albersheim, P.9
  • 219
    • 0031131631 scopus 로고    scopus 로고
    • Two general branching patterns of xyloglucan, XXXG and XXGG
    • Vincken J-P, York WS, Beldman G, Voragen AGJ (1997) Two general branching patterns of xyloglucan, XXXG and XXGG. Plant Physiol 114:9-13
    • (1997) Plant Physiol , vol.114 , pp. 9-13
    • Vincken, J.-P.1    York, W.S.2    Beldman, G.3    Voragen, A.4
  • 221
    • 0036403372 scopus 로고    scopus 로고
    • Galactose oxidase
    • Valentine JS, Gralla EB (eds),. Academic, New York
    • Whittaker JW (2002) Galactose oxidase. In: Valentine JS, Gralla EB (eds) Advances in protein chemistry. Academic, New York, pp 1-49
    • (2002) Advances in Protein Chemistry , pp. 1-49
    • Whittaker, J.W.1
  • 223
  • 224
    • 67649815010 scopus 로고    scopus 로고
    • Cellulases and biofuels
    • Wilson DB (2009) Cellulases and biofuels. Curr Opin Biotechnol 20:295-299
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 295-299
    • Wilson, D.B.1
  • 225
    • 44849095141 scopus 로고    scopus 로고
    • Evidence for cleavage of lignin by a brown rot basidiomycete
    • Yelle DJ, Ralph J, Lu F, Hammel KE (2008) Evidence for cleavage of lignin by a brown rot basidiomycete. Environ Microbiol 10:1844-1849
    • (2008) Environ Microbiol , vol.10 , pp. 1844-1849
    • Yelle, D.J.1    Ralph, J.2    Lu, F.3    Hammel, K.E.4
  • 226
    • 0027651223 scopus 로고
    • Isolation of Aspergillus flavus MO-5 producing two types of intracellular a-D-xylosidases: Purification and characterization of a-D-xylosidase I
    • Yoshikawa K, Yamamoto K, Okada S (1993a) Isolation of Aspergillus flavus MO-5 producing two types of intracellular a-D-xylosidases: purification and characterization of a-D-xylosidase I. Biosci Biotechnol Biochem 57:1275-1280
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 1275-1280
    • Yoshikawa, K.1    Yamamoto, K.2    Okada, S.3
  • 227
    • 0027651103 scopus 로고
    • Purification and characterization of an intracellular a-D-xylosidase II from Aspergillus flavus MO-5
    • Yoshikawa K, Yamamoto K, Okada S (1993b) Purification and characterization of an intracellular a-D-xylosidase II from Aspergillus flavus MO-5. Biosci Biotechnol Biochem 57:1281-1285
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 1281-1285
    • Yoshikawa, K.1    Yamamoto, K.2    Okada, S.3
  • 229
    • 84864112250 scopus 로고    scopus 로고
    • Fungal polysaccharide monooxygenases: New players in the decomposition of cellulose
    • Zifckov L, Baldrian P (2012) Fungal polysaccharide monooxygenases: new players in the decomposition of cellulose. Fungal Ecol 5:481-489
    • (2012) Fungal Ecol , vol.5 , pp. 481-489
    • Zifckov, L.1    Baldrian, P.2


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