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Volumn 1824, Issue 6, 2012, Pages 802-812

Cloning, expression, and characterization of a cellobiose dehydrogenase from Thielavia terrestris induced under cellulose growth conditions

Author keywords

Cellobiose dehydrogenase; Glycoside hydrolase family 61; Thielavia terrestris

Indexed keywords

BETA GLUCOSIDASE; CELLOBIOSE QUINONE OXIDOREDUCTASE; CELLULASE; CELLULOSE; FUNGAL PROTEIN; GLUCAN SYNTHASE; GLYCOSIDASE; LIGNOCELLULOSE; PHOSPHORIC ACID;

EID: 84860351767     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.03.009     Document Type: Article
Times cited : (24)

References (61)
  • 1
    • 0000866367 scopus 로고
    • Cellobiose:quinone oxidoreductase, a new wood-degrading enzyme from white-rot fungi
    • U. Westermark, and K.-E. Eriksson Cellobiose:quinone oxidoreductase, a new wood-degrading enzyme from white-rot fungi Acta Chem. Scand. B28 1974 209 214
    • (1974) Acta Chem. Scand. , vol.28 B , pp. 209-214
    • Westermark, U.1    Eriksson, K.-E.2
  • 2
    • 0016412938 scopus 로고
    • Purification and properties of cellobiose:quinone oxidoreductase from Sporotrichum pulverulentum
    • U. Westermark, and K.-E. Eriksson Purification and properties of cellobiose:quinone oxidoreductase from Sporotrichum pulverulentum Acta Chem. Scand. B29 1975 419 424
    • (1975) Acta Chem. Scand. , vol.29 B , pp. 419-424
    • Westermark, U.1    Eriksson, K.-E.2
  • 3
    • 0018122952 scopus 로고
    • Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum
    • A.R. Ayers, S.B. Ayers, and K.E. Eriksson Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum Eur. J. Biochem. 90 1978 171 181 (Pubitemid 9013140)
    • (1978) European Journal of Biochemistry , vol.90 , Issue.1 , pp. 171-181
    • Ayers, A.R.1    Ayers, S.B.2    Eriksson, K.E.3
  • 4
    • 0000866367 scopus 로고
    • Carbohydrate-dependent enzymic quinone reduction during lignin degradation
    • U. Westermark, and K.-E. Eriksson Carbohydrate-dependent enzymic quinone reduction during lignin degradation Acta Chem. Scand. B28 1974 204 208
    • (1974) Acta Chem. Scand. , vol.28 B , pp. 204-208
    • Westermark, U.1    Eriksson, K.-E.2
  • 5
    • 0034629232 scopus 로고    scopus 로고
    • A critical review of cellobiose dehydrogenases
    • DOI 10.1016/S0168-1656(00)00206-6, PII S0168165600002066
    • G. Henriksson, G. Johansson, and G. Pettersson A critical review of cellobiose dehydrogenases J. Biotechnol. 78 2000 93 113 (Pubitemid 30139553)
    • (2000) Journal of Biotechnology , vol.78 , Issue.2 , pp. 93-113
    • Henriksson, G.1    Johansson, G.2    Pettersson, G.3
  • 6
    • 0035252395 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase - An extracellular fungal flavocytochrome
    • DOI 10.1016/S0141-0229(00)00307-0, PII S0141022900003070
    • M.D. Cameron, and S.D. Aust Cellobiose dehydrogenase - an extracellular fungal flavocytochrome Enzyme Microb. Technol. 28 2001 129 138 (Pubitemid 32146630)
    • (2001) Enzyme and Microbial Technology , vol.28 , Issue.2-3 , pp. 129-138
    • Cameron, M.D.1    Aust, S.D.2
  • 8
    • 0019254299 scopus 로고
    • Induction and characterization of a cellobiose dehydrogenase produced by a species of Monilia
    • R.F.H. Dekker Induction and characterization of a cellobiose dehydrogenase produced by a species of Monilia J. Gen. Microbiol. 120 1980 309 316 (Pubitemid 11160147)
    • (1980) Journal of General Microbiology , vol.120 , Issue.2 , pp. 309-316
    • Dekker, R.F.H.1
  • 10
    • 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
    • M. Zámocký, C. Schümann, C. Sygmund, J. O'Callaghan, A.D.W. Dobson, R. Ludwig, D. Haltrich, and C.K. Peterbauer Cloning, sequence analysis and heterologous expression in Pichia pastoris of a gene encoding a thermostable cellobiose dehydrogenase from Myriococcum thermophilum Protein Expr. Purif. 59 2008 258 265
    • (2008) Protein Expr. Purif. , vol.59 , pp. 258-265
    • Zámocký, M.1    Schümann, C.2    Sygmund, C.3    O'Callaghan, J.4    Dobson, A.D.W.5    Ludwig, R.6    Haltrich, D.7    Peterbauer, C.K.8
  • 11
    • 0033562157 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile
    • DOI 10.1006/abbi.1999.1152
    • S.S. Subramaniam, S.R. Nagalla, and V. Renganathan Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile Arch. Biochem. Biophys. 365 1999 223 230 (Pubitemid 29391630)
    • (1999) Archives of Biochemistry and Biophysics , vol.365 , Issue.2 , pp. 223-230
    • Subramaniam, S.S.1    Nagalla, S.R.2    Renganathan, V.3
  • 13
    • 0032519528 scopus 로고    scopus 로고
    • Characterization of a cellobiose dehydrogenase from Humicola insolens
    • C. Schou, M.H. Christensen, and M. Schulein Characterization of a cellobiose dehydrogenase from Humicola insolens Biochem. J. 330 1998 565 571 (Pubitemid 28075788)
    • (1998) Biochemical Journal , vol.330 , Issue.1 , pp. 565-571
    • Schou, C.1    Christensen, M.H.2    Schulein, M.3
  • 15
    • 79959976450 scopus 로고    scopus 로고
    • Effects of xylan and starch on secretome of the basidiomycete Phanerochaete chrysosporium grown on cellulose
    • C. Hori, K. Igarashi, A. Katayama, and M. Samejima Effects of xylan and starch on secretome of the basidiomycete Phanerochaete chrysosporium grown on cellulose FEMS Microbiology Letters 321 2011 14 23
    • (2011) FEMS Microbiology Letters , vol.321 , pp. 14-23
    • Hori, C.1    Igarashi, K.2    Katayama, A.3    Samejima, M.4
  • 16
    • 42149110897 scopus 로고    scopus 로고
    • Degradation of cellulose by basidiomycetous fungi
    • P. Baldrian, and V. Valaskova Degradation of cellulose by basidiomycetous fungi FEMS Microbiol. Rev. 32 2008
    • (2008) FEMS Microbiol. Rev. , vol.32
    • Baldrian, P.1    Valaskova, V.2
  • 19
    • 0005189978 scopus 로고
    • Production and localization of cellulases and β-glucosidase from the thermophilic fungus Thielavia terrestris
    • C. Breuil, G. Wojtczak, and J.N. Saddler Production and localization of cellulases and β-glucosidase from the thermophilic fungus Thielavia terrestris Biotechnol. Lett. 8 1986 673 676
    • (1986) Biotechnol. Lett. , vol.8 , pp. 673-676
    • Breuil, C.1    Wojtczak, G.2    Saddler, J.N.3
  • 20
    • 0021405426 scopus 로고
    • Comparative study of cellulases and hemicellulases from four fungi: mesophiles Trichoderma reesei and Penicillium sp. and thermophiles Thielavia terrestris and Sporotrichum cellulophilum
    • DOI 10.1016/0141-0229(84)90027-9
    • H. Durand, P. Soucaille, and G. Tiraby Comparative study of cellulases and hemicellulases from four fungi: mesophiles Trichoderma reesei and Penicillium sp. and thermophiles Thielavia terrestris and Sporotrichum cellulophilum Enzyme Microb. Technol. 6 1984 175 180 (Pubitemid 14571791)
    • (1984) Enzyme and Microbial Technology , vol.6 , Issue.4 , pp. 175-180
    • Durand Henri1    Soucaille Philippe2    Tiraby Gerard3
  • 21
    • 0026799608 scopus 로고
    • Characterization of the enzymes present in the cellulase system of Thielavia terrestris 255B
    • M. Gilbert, C. Breuil, and J.N. Saddler Characterization of the enzymes present in the cellulase system of Thielavia terrestris 255B Bioresour. Technol. 39 1992 147 154
    • (1992) Bioresour. Technol. , vol.39 , pp. 147-154
    • Gilbert, M.1    Breuil, C.2    Saddler, J.N.3
  • 22
    • 33646017710 scopus 로고    scopus 로고
    • Efficiency of new fungal cellulase systems in boosting enzymatic degradation of barley straw lignocellulose
    • L. Rosgaard, S. Pedersen, J.R. Cherry, P. Harris, and A.S. Meyer Efficiency of new fungal cellulase systems in boosting enzymatic degradation of barley straw lignocellulose Biotechnol. Prog. 22 2006 493 498
    • (2006) Biotechnol. Prog. , vol.22 , pp. 493-498
    • Rosgaard, L.1    Pedersen, S.2    Cherry, J.R.3    Harris, P.4    Meyer, A.S.5
  • 23
    • 34548754522 scopus 로고    scopus 로고
    • Progress and challenges in enzyme development for biomass utilization
    • DOI 10.1007/10-2007-066, Biofuels
    • S. Merino, and J. Cherry Progress and challenges in enzyme development for biomass utilization L. Olsson, Advances in Biochemical Engineering Biotechnology Biofuels vol. 108 2007 Springer 95 120 (Pubitemid 47434544)
    • (2007) Advances in Biochemical Engineering/Biotechnology , vol.108 , pp. 95-120
    • Merino, S.T.1    Cherry, J.2
  • 26
    • 81755178934 scopus 로고    scopus 로고
    • Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61
    • J.A. Langston, T. Shaghasi, E. Abbate, F. Xu, E. Vlasenko, and M.D. Sweeney Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61 Appl. Environ. Microbiol. 77 19 2011 7007 7015
    • (2011) Appl. Environ. Microbiol. , vol.77 , Issue.19 , pp. 7007-7015
    • Langston, J.A.1    Shaghasi, T.2    Abbate, E.3    Xu, F.4    Vlasenko, E.5    Sweeney, M.D.6
  • 27
    • 0001963674 scopus 로고
    • A convenient growth medium for Neurospora medium N
    • H.J. Vogel A convenient growth medium for Neurospora medium N Microb. Genet. Bull. 13 1956 42 43
    • (1956) Microb. Genet. Bull. , vol.13 , pp. 42-43
    • Vogel, H.J.1
  • 28
    • 0038396111 scopus 로고    scopus 로고
    • Enzymatic properties of cellulases from Humicola insolens
    • DOI 10.1016/S0168-1656(97)00090-4, PII S0168165697000904
    • M. Schülein Enzymatic properties of cellulases from Humicola insolens J. Biotechnol. 57 1997 71 81 (Pubitemid 27397472)
    • (1997) Journal of Biotechnology , vol.57 , Issue.1-3 , pp. 71-81
    • Schulein, M.1
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 70350000268 scopus 로고    scopus 로고
    • Productive cellulase adsorption on cellulose
    • B.C. Saha, American Chemical Society Washington, DC
    • F. Xu, and H. Ding Productive cellulase adsorption on cellulose B.C. Saha, Lignocellulose Biodegradation 2004 American Chemical Society Washington, DC 154 169
    • (2004) Lignocellulose Biodegradation , pp. 154-169
    • Xu, F.1    Ding, H.2
  • 32
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • D. Wessel, and U.I. Flügge A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids Anal. Biochem. 138 1984 141 143 (Pubitemid 14146660)
    • (1984) Analytical Biochemistry , vol.138 , Issue.1 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2
  • 33
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • DOI 10.1021/ac0341261
    • A.I. Nesvizhskii, A. Keller, E. Kolker, and R. Aebersold A statistical model for identifying proteins by tandem mass spectrometry Anal. Chem. 75 2003 4646 4658 (Pubitemid 37082259)
    • (2003) Analytical Chemistry , vol.75 , Issue.17 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 34
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • DOI 10.1021/ac025747h
    • A. Keller, A.I. Nesvizhskii, E. Kolker, and R. Aebersold Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search Anal. Chem. 74 2002 5383 5392 (Pubitemid 35215372)
    • (2002) Analytical Chemistry , vol.74 , Issue.20 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 35
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • J. Dyrlov Bendtsen, H. Nielsen, G. von Heijne, and S. Brunak Improved prediction of signal peptides: SignalP 3.0 J. Mol. Biol. 340 2004 783 795 (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 36
    • 0034800374 scopus 로고    scopus 로고
    • InterProScan - An integration platform for the signature-recognition methods in InterPro
    • E.M. Zdobnov, and R. Apweiler InterProScan - an integration platform for the signature-recognition methods in InterPro Bioinformatics 17 2001 847 848 (Pubitemid 32970486)
    • (2001) Bioinformatics , vol.17 , Issue.9 , pp. 847-848
    • Zdobnov, E.M.1    Apweiler, R.2
  • 43
    • 0028088841 scopus 로고
    • The biological degradation of cellulose
    • DOI 10.1016/0168-6445(94)90099-X
    • P. Béguin, and J.-P. Aubert The biological degradation of cellulose FEMS Microbiol. Rev. 13 1994 25 58 (Pubitemid 24051006)
    • (1994) FEMS Microbiology Reviews , vol.13 , Issue.1 , pp. 25-58
    • Beguin, P.1    Aubert, J.-P.2
  • 44
    • 0024278187 scopus 로고
    • Synergism in cellulose hydrolysis by endoglucanases and exoglucanases purified from Trichoderma viride
    • G. Beldman, A.G.J. Voragen, F.M. Rombouts, and W. Pilnik Synergism in cellulose hydrolysis by endoglucanases and exoglucanases purified from Trichoderma viride Biotechnol. Bioeng. 31 1988 173 178 (Pubitemid 18566062)
    • (1988) Biotechnology and Bioengineering , vol.31 , Issue.2 , pp. 173-178
    • Beldman, G.1    Voragen, A.G.J.2    Rombouts, F.M.3    Pilnik, W.4
  • 45
    • 0027651651 scopus 로고
    • Activity studies of eight purified cellulases: Specificity, synergism, and binding domain effects
    • D.C. Irwin, M. Spezio, L.P. Walker, and D.B. Wilson Activity studies of eight purified cellulases: specificity, synergism, and binding domain effects Biotechnol. Bioeng. 42 1993 1002 1013 (Pubitemid 23288706)
    • (1993) Biotechnology and Bioengineering , vol.42 , Issue.8 , pp. 1002-1013
    • Irwin, D.C.1    Spezio, M.2    Walker, L.P.3    Wilson, D.B.4
  • 47
    • 0036637448 scopus 로고    scopus 로고
    • Impact of deglycosylation methods on two-dimensional gel electrophoresis and matrix assisted laser desorption/ionization-time of flight-mass spectrometry for proteomic analysis
    • B.G. Fryksdale, P.T. Jedrzejewski, D.L. Wong, A.L. Gaertner, and B.S. Miller Impact of deglycosylation methods on two-dimensional gel electrophoresis and matrix assisted laser desorption/ionization-time of flight-mass spectrometry for proteomic analysis Electrophoresis 23 2002 2184 2193
    • (2002) Electrophoresis , vol.23 , pp. 2184-2193
    • Fryksdale, B.G.1    Jedrzejewski, P.T.2    Wong, D.L.3    Gaertner, A.L.4    Miller, B.S.5
  • 48
    • 50449083920 scopus 로고    scopus 로고
    • Protein expression and enzymatic activity of cellulases produced by Trichoderma reesei Rut C-30 on rice straw
    • W.-C. Sun, C.-H. Cheng, and W.-C. Lee Protein expression and enzymatic activity of cellulases produced by Trichoderma reesei Rut C-30 on rice straw Process. Biochem. 43 2008 1083 1087
    • (2008) Process. Biochem. , vol.43 , pp. 1083-1087
    • Sun, W.-C.1    Cheng, C.-H.2    Lee, W.-C.3
  • 50
    • 0025865802 scopus 로고
    • Cellobiose dehydrogenases of Sporotrichum (Chrysosporium) thermophile
    • G. Canevascini, P. Borer, and J.-L. Dreyer Cellobiose dehydrogenases of Sporotrichum (Chrysosporium) thermophile Eur. J. Biochem. 198 1991 43 52
    • (1991) Eur. J. Biochem. , vol.198 , pp. 43-52
    • Canevascini, G.1    Borer, P.2    Dreyer, J.-L.3
  • 51
    • 0035318377 scopus 로고    scopus 로고
    • Purification and Characterization of Cellobiose Dehydrogenase from the Plant Pathogen Sclerotium (Athelia) rolfsii
    • DOI 10.1128/AEM.67.4.1766-1774.2001
    • U. Baminger, S.S. Subramaniam, V. Renganathan, and D. Haltrich Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii Appl. Environ. Microbiol. 67 2001 1766 1774 (Pubitemid 33647556)
    • (2001) Applied and Environmental Microbiology , vol.67 , Issue.4 , pp. 1766-1774
    • Baminger, U.1    Subramaniam, S.S.2    Renganathan, V.3    Haltrich, D.4
  • 53
    • 20444468865 scopus 로고    scopus 로고
    • The Phanerochaete chrysosporium secretome: Database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium
    • DOI 10.1016/j.jbiotec.2005.03.010, PII S0168165605001525
    • A. Vanden Wymelenberg, G. Sabat, D. Martinez, A.S. Rajangam, T.T. Teeri, J. Gaskell, P.J. Kersten, and D. Cullen The Phanerochaete chrysosporium secretome: database predictions and initial mass spectrometry peptide identifications in cellulose-grown medium J. Biotechnol. 118 2005 17 34 (Pubitemid 40814531)
    • (2005) Journal of Biotechnology , vol.118 , Issue.1 , pp. 17-34
    • Wymelenberg, A.V.1    Sabat, G.2    Martinez, D.3    Rajangam, A.S.4    Teeri, T.T.5    Gaskell, J.6    Kersten, P.J.7    Cullen, D.8
  • 55
    • 34748923122 scopus 로고    scopus 로고
    • Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum
    • DOI 10.1002/pmic.200700184
    • J.M. Paper, J.S. Scott-Craig, N.D. Adhikari, C.A. Cuomo, and J.D. Walton Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum Proteomics 7 2007 3171 3183 (Pubitemid 47477959)
    • (2007) Proteomics , vol.7 , Issue.17 , pp. 3171-3183
    • Paper, J.M.1    Scott-Craig, J.S.2    Adhikari, N.D.3    Cuomo, C.A.4    Walton, J.D.5
  • 56
    • 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
    • S. Nagendran, H.E. Hallen-Adams, J.M. Paper, N. Aslam, and J.D. Walton 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 2009 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
  • 57
    • 0030953976 scopus 로고    scopus 로고
    • Wide distribution of cellobiose-oxidizing enzymes in wood-rot fungus indicates a physiological importance in lignocellulosics degradation
    • J. Fang, Y. Qu, and P. Gao Wide distribution of cellobiose-oxidizing enzymes in wood-rot fungus indicates a physiological importance in lignocellulosics degradation Biotechnol. Tech. 11 1997 195 198
    • (1997) Biotechnol. Tech. , vol.11 , pp. 195-198
    • Fang, J.1    Qu, Y.2    Gao, P.3
  • 58
    • 0026540422 scopus 로고
    • Cellobiose oxidase of Phanerochaete chrysosporium enhances crystalline cellulose degradation by cellulases
    • W. Bao, and V. Renganathan Cellobiose oxidase of Phanerochaete chrysosporium enhances crystalline cellulose degradation by cellulases FEBS J. 302 1992 77 80
    • (1992) FEBS J. , vol.302 , pp. 77-80
    • Bao, W.1    Renganathan, V.2
  • 59
    • 0032573093 scopus 로고    scopus 로고
    • Overproduction of recombinant Trichoderma reesei cellulases by Aspergillus oryzae and their enzymatic properties
    • DOI 10.1016/S0168-1656(98)00084-4, PII S0168165698000844
    • S. Takashima, H. Iikura, A. Nakamura, M. Hidaka, H. Masaki, and T. Uozumi Overproduction of recombinant Trichoderma reesei cellulases by Aspergillus oryzae and their enzymatic properties J. Biotechnol. 65 1998 163 171 (Pubitemid 28488563)
    • (1998) Journal of Biotechnology , vol.65 , Issue.2-3 , pp. 163-171
    • Takashima, S.1    Iikura, H.2    Nakamura, A.3    Hidaka, M.4    Masaki, H.5    Uozumi, T.6
  • 60
    • 33646506148 scopus 로고    scopus 로고
    • Substrate specificity of Aspergillus oryzae family 3 β-glucosidase
    • J. Langston, N. Sheehy, and F. Xu Substrate specificity of Aspergillus oryzae family 3 β-glucosidase Biochim. Biophys. Acta (BBA) 1764 2006 972 978
    • (2006) Biochim. Biophys. Acta (BBA) , vol.1764 , pp. 972-978
    • Langston, J.1    Sheehy, N.2    Xu, F.3
  • 61
    • 84055197660 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa
    • C.M. Phillips, W.T. Beeson, J.H. Cate, and M.A. Marletta Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa ACS Chemical Biology 6 12 2011 1399 1406
    • (2011) ACS Chemical Biology , vol.6 , Issue.12 , pp. 1399-1406
    • Phillips, C.M.1    Beeson, W.T.2    Cate, J.H.3    Marletta, M.A.4


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