메뉴 건너뛰기




Volumn 88, Issue , 2014, Pages 103-165

Carbohydrate-Binding Modules of Fungal Cellulases. Occurrence in Nature, Function, and Relevance in Industrial Biomass Conversion

Author keywords

Adsorption; Ascomycetes; Basidiomycetes; Brown rot; Carbohydrate binding modules; Cellulases; Desorption; Fungi; High substrate concentration; Lignocellulose biomass conversion; White rot

Indexed keywords

BETA MANNOSIDASE; CARBOHYDRATE; CELLULASE; CELLULOSE; CELLULOSE 1,4 BETA CELLOBIOSIDASE; FUNGAL CELLULASE; FUNGAL ENZYME; HEMICELLULOSE; HYDROLASE; LIGNIN; LIGNOCELLULOSE; MONOSACCHARIDE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 84899154526     PISSN: 00652164     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-800260-5.00004-8     Document Type: Chapter
Times cited : (128)

References (205)
  • 1
    • 68149168191 scopus 로고    scopus 로고
    • Technoeconomic analysis of the dilute sulfuric acid and enzymatic hydrolysis process for the conversion of corn stover to ethanol
    • Aden A., Foust T. Technoeconomic analysis of the dilute sulfuric acid and enzymatic hydrolysis process for the conversion of corn stover to ethanol. Cellulose 2009, 16:535-545.
    • (2009) Cellulose , vol.16 , pp. 535-545
    • Aden, A.1    Foust, T.2
  • 2
    • 84981590387 scopus 로고
    • Selective degradation of wood components by white-rot fungi
    • Ander P., Eriksson K.-E. Selective degradation of wood components by white-rot fungi. Physiologia Plantarum 1977, 41:239-248.
    • (1977) Physiologia Plantarum , vol.41 , pp. 239-248
    • Ander, P.1    Eriksson, K.-E.2
  • 3
    • 77950356429 scopus 로고    scopus 로고
    • Access to cellulose limits the efficiency of enzymatic hydrolysis: The role of amorphogenesis
    • Arantes V., Saddler J.N. Access to cellulose limits the efficiency of enzymatic hydrolysis: The role of amorphogenesis. Biotechnology for Biofuels 2010, 3:4.
    • (2010) Biotechnology for Biofuels , vol.3 , pp. 4
    • Arantes, V.1    Saddler, J.N.2
  • 4
    • 36048972648 scopus 로고
    • Native cellulose: A composite of two distinct crystalline forms
    • Atalla R.H., Van der Hart D.L. Native cellulose: A composite of two distinct crystalline forms. Science 1984, 223:283-285.
    • (1984) Science , vol.223 , pp. 283-285
    • Atalla, R.H.1    Van der Hart, D.L.2
  • 5
    • 42149110897 scopus 로고    scopus 로고
    • Degradation of cellulose by basidiomycetous fungi
    • Baldrian P., Valášková V. Degradation of cellulose by basidiomycetous fungi. FEMS Microbiology Reviews 2008, 32:501-521.
    • (2008) FEMS Microbiology Reviews , vol.32 , pp. 501-521
    • Baldrian, P.1    Valášková, V.2
  • 6
    • 34249949390 scopus 로고    scopus 로고
    • The potential of cellulases and cellulosomes for cellulosic waste management
    • Bayer E.A., Lamed R., Himmel M.E. The potential of cellulases and cellulosomes for cellulosic waste management. Current Opinion in Biotechnology 2007, 18:237-245. 10.1016/j.copbio.2007.04.004.
    • (2007) Current Opinion in Biotechnology , vol.18 , pp. 237-245
    • Bayer, E.A.1    Lamed, R.2    Himmel, M.E.3
  • 8
    • 76249113333 scopus 로고    scopus 로고
    • Identification of amino acids responsible for processivity in a family 1 carbohydrate-binding module from a fungal cellulase
    • Beckham G.T., Matthews J.F., Bomble Y.J., Bu L., Adney W.S., Himmel M.E., et al. Identification of amino acids responsible for processivity in a family 1 carbohydrate-binding module from a fungal cellulase. Journal of Physical Chemistry B 2010, 113:1447-1453.
    • (2010) Journal of Physical Chemistry B , vol.113 , pp. 1447-1453
    • Beckham, G.T.1    Matthews, J.F.2    Bomble, Y.J.3    Bu, L.4    Adney, W.S.5    Himmel, M.E.6
  • 9
    • 33746901704 scopus 로고    scopus 로고
    • Inhibition of cellulase, xylanase and β-glucosidase activities by softwood lignin preparations
    • Berlin A., Balakshin M., Gilkes N., Kadla J., Maximenko V., Kubo S., et al. Inhibition of cellulase, xylanase and β-glucosidase activities by softwood lignin preparations. Journal of Biotechnology 2006, 125:198-209.
    • (2006) Journal of Biotechnology , vol.125 , pp. 198-209
    • Berlin, A.1    Balakshin, M.2    Gilkes, N.3    Kadla, J.4    Maximenko, V.5    Kubo, S.6
  • 10
    • 18844427544 scopus 로고    scopus 로고
    • Weak lignin-binding enzymes-A novel approach to improve activity of cellulases for hydrolysis of lignocellulosics
    • Berlin A., Gilkes N., Kurabi A., Bura R., Tu M.B., Kilburn D., et al. Weak lignin-binding enzymes-A novel approach to improve activity of cellulases for hydrolysis of lignocellulosics. Applied Biochemistry and Biotechnology 2005, 121:163-170.
    • (2005) Applied Biochemistry and Biotechnology , vol.121 , pp. 163-170
    • Berlin, A.1    Gilkes, N.2    Kurabi, A.3    Bura, R.4    Tu, M.B.5    Kilburn, D.6
  • 12
    • 0025908702 scopus 로고
    • The endo-1,4-β-glucanase I from Trichoderma reesei. Action on β-1,4-oligomers and polymers derived from D-glucose and D-xylose
    • Biely P., Vršanská M., Claeyssens M. The endo-1,4-β-glucanase I from Trichoderma reesei. Action on β-1,4-oligomers and polymers derived from D-glucose and D-xylose. European Journal of Biochemistry 1991, 200:157-163.
    • (1991) European Journal of Biochemistry , vol.200 , pp. 157-163
    • Biely, P.1    Vršanská, M.2    Claeyssens, M.3
  • 13
    • 0034029116 scopus 로고    scopus 로고
    • Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A
    • Boisset C., Fraschini C., Schülein M., Henrissat B., Chanzy H. Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A. Applied and Environmental Microbiology 2000, 66:1444-1452.
    • (2000) Applied and Environmental Microbiology , vol.66 , pp. 1444-1452
    • Boisset, C.1    Fraschini, C.2    Schülein, M.3    Henrissat, B.4    Chanzy, H.5
  • 15
    • 33847325663 scopus 로고    scopus 로고
    • Enhanced enzymatic conversion of softwood lignocellulose by poly(ethylene glycol) addition
    • Börjesson J., Peterson R., Tjerneld F. Enhanced enzymatic conversion of softwood lignocellulose by poly(ethylene glycol) addition. Enzyme and Microbial Technology 2007, 40:754-762.
    • (2007) Enzyme and Microbial Technology , vol.40 , pp. 754-762
    • Börjesson, J.1    Peterson, R.2    Tjerneld, F.3
  • 16
    • 0345355169 scopus 로고    scopus 로고
    • Adsorption and activity profiles of cellulases during hydrolysis of two Douglas fir pulps
    • Boussaid A., Saddler J.N. Adsorption and activity profiles of cellulases during hydrolysis of two Douglas fir pulps. Enzyme and Microbial Technology 1999, 24:138-143.
    • (1999) Enzyme and Microbial Technology , vol.24 , pp. 138-143
    • Boussaid, A.1    Saddler, J.N.2
  • 17
    • 68149156908 scopus 로고    scopus 로고
    • The energy landscape for interaction of the family 1 carbohydrate-binding module and the cellulose surface is altered by hydrolyzed glycosidic bonds
    • Bu L., Beckham G.T., Crowley M.F., Chang C.H., Matthews J.F., Bomble Y.J., et al. The energy landscape for interaction of the family 1 carbohydrate-binding module and the cellulose surface is altered by hydrolyzed glycosidic bonds. Journal of Physical Chemistry B 2009, 113:10994-11002.
    • (2009) Journal of Physical Chemistry B , vol.113 , pp. 10994-11002
    • Bu, L.1    Beckham, G.T.2    Crowley, M.F.3    Chang, C.H.4    Matthews, J.F.5    Bomble, Y.J.6
  • 19
    • 0001240227 scopus 로고
    • A new Phanerochaete with a Chrysosporium imperfect state
    • Burdsall H.H., Eslyn W. A new Phanerochaete with a Chrysosporium imperfect state. Mycotaxon 1974, 1:124.
    • (1974) Mycotaxon , vol.1 , pp. 124
    • Burdsall, H.H.1    Eslyn, W.2
  • 20
    • 84862173322 scopus 로고    scopus 로고
    • Production and effect of aldonic acids during enzymatic hydrolysis of lignocellulose at high dry matter content
    • Cannella D., Hsieh C.W., Felby C., Jørgensen H. Production and effect of aldonic acids during enzymatic hydrolysis of lignocellulose at high dry matter content. Biotechnology for Biofuels 2012, 5:26.
    • (2012) Biotechnology for Biofuels , vol.5 , pp. 26
    • Cannella, D.1    Hsieh, C.W.2    Felby, C.3    Jørgensen, H.4
  • 21
    • 0000138828 scopus 로고
    • Limiting diameters of pores and the surface structure of plant cell walls
    • Carpita N.C. Limiting diameters of pores and the surface structure of plant cell walls. Science 1982, 218:813-814.
    • (1982) Science , vol.218 , pp. 813-814
    • Carpita, N.C.1
  • 23
    • 84899150253 scopus 로고    scopus 로고
    • Compositions and methods comprising cellulase variants with reduced affinity to non-cellulosic materials. Application no. WO/2009/149202. Publication date 10/12/2009.
    • Cascao-Pereira, L., Kaper, T., Kelemen, B. R., & Liu, A. (2009). Compositions and methods comprising cellulase variants with reduced affinity to non-cellulosic materials. Application no. WO/2009/149202. Publication date 10/12/2009.
    • (2009)
    • Cascao-Pereira, L.1    Kaper, T.2    Kelemen, B.R.3    Liu, A.4
  • 24
    • 84863299258 scopus 로고    scopus 로고
    • Genome sequence of the model medicinal mushroom Ganoderma lucidum
    • Chen S., Xu J., Liu C., Zhu Y., Nelson D.R., Zhou S., et al. Genome sequence of the model medicinal mushroom Ganoderma lucidum. Nature Communications 2012, 3:913. 10.1038/ncomms1923.
    • (2012) Nature Communications , vol.3 , pp. 913
    • Chen, S.1    Xu, J.2    Liu, C.3    Zhu, Y.4    Nelson, D.R.5    Zhou, S.6
  • 25
    • 33748749072 scopus 로고    scopus 로고
    • Effect of ethanol and yeast on cellulase activity and hydrolysis of crystalline cellulose
    • Cheng H., Jin S. Effect of ethanol and yeast on cellulase activity and hydrolysis of crystalline cellulose. Enzyme and Microbial Technology 2006, 39:1430-1432.
    • (2006) Enzyme and Microbial Technology , vol.39 , pp. 1430-1432
    • Cheng, H.1    Jin, S.2
  • 27
    • 84864386570 scopus 로고    scopus 로고
    • Precipitation of Trichoderma reesei commercial cellulase preparations under standard enzymatic hydrolysis conditions for lignocelluloses
    • Chylenski P., Felby C., Haven M.Ø., Gama M., Selig M.J. Precipitation of Trichoderma reesei commercial cellulase preparations under standard enzymatic hydrolysis conditions for lignocelluloses. Biotechnology Letters 2012, 34:1475-1482.
    • (2012) Biotechnology Letters , vol.34 , pp. 1475-1482
    • Chylenski, P.1    Felby, C.2    Haven, M.Ø.3    Gama, M.4    Selig, M.J.5
  • 28
    • 18444373877 scopus 로고    scopus 로고
    • Processive endoglucanase active in crystalline cellulose hydrolysis by the brown rot basidiomycete Gloeophyllum trabeum
    • Cohen R., Suzuki M.R., Hammel K.E. Processive endoglucanase active in crystalline cellulose hydrolysis by the brown rot basidiomycete Gloeophyllum trabeum. Applied and Environmental Microbiology 2005, 71:2412-2417.
    • (2005) Applied and Environmental Microbiology , vol.71 , pp. 2412-2417
    • Cohen, R.1    Suzuki, M.R.2    Hammel, K.E.3
  • 29
    • 84946633762 scopus 로고
    • The properties of fungal and bacterial cellulases with comment on their production and application
    • Coughlan M.P. The properties of fungal and bacterial cellulases with comment on their production and application. Biotechnology and Genetic Engineering Reviews 1985, 3:37-109.
    • (1985) Biotechnology and Genetic Engineering Reviews , vol.3 , pp. 37-109
    • Coughlan, M.P.1
  • 31
    • 84890537940 scopus 로고    scopus 로고
    • Transient kinetics and rate-limiting steps for the processive cellobiohydrolase Cel7A: Effects of substrate structure and carbohydrate binding domain
    • Cruys-Bagger N., Tatsumi H., Ren G.R., Borch K., Westh P. Transient kinetics and rate-limiting steps for the processive cellobiohydrolase Cel7A: Effects of substrate structure and carbohydrate binding domain. Biochemistry 2013, 52:8938-8948.
    • (2013) Biochemistry , vol.52 , pp. 8938-8948
    • Cruys-Bagger, N.1    Tatsumi, H.2    Ren, G.R.3    Borch, K.4    Westh, P.5
  • 33
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995, 3:853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 34
    • 33748753698 scopus 로고    scopus 로고
    • Blackwell Publishing, Oxford, UK
    • Deacon J. Fungal biology 2005, 371. Blackwell Publishing, Oxford, UK.
    • (2005) Fungal biology , pp. 371
    • Deacon, J.1
  • 35
    • 67949106387 scopus 로고    scopus 로고
    • Biorefineries for biofuel upgrading: A critical review
    • Demirbas M.F. Biorefineries for biofuel upgrading: A critical review. Applied Energy 2009, 86:S151-S161.
    • (2009) Applied Energy , vol.86
    • Demirbas, M.F.1
  • 36
    • 0030899429 scopus 로고    scopus 로고
    • The role of the cellulolytic high molecular mass (HMM) complex of the anaerobic fungus Piromyces sp. Strain E2 in the hydrolysis of microcrystalline cellulose
    • Dijkerman R., Op den Camp H.J.M., van der Drift C., Vogels G.D. The role of the cellulolytic high molecular mass (HMM) complex of the anaerobic fungus Piromyces sp. Strain E2 in the hydrolysis of microcrystalline cellulose. Archives of Microbiology 1997, 167:137-142.
    • (1997) Archives of Microbiology , vol.167 , pp. 137-142
    • Dijkerman, R.1    Op den Camp, H.J.M.2    van der Drift, C.3    Vogels, G.D.4
  • 37
    • 0027968302 scopus 로고
    • The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei
    • Divne C., Ståhlberg J., Reinikainen T., Ruohonen L., Pettersson G., Knowles J.K., et al. The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science 1994, 265:524-528.
    • (1994) Science , vol.265 , pp. 524-528
    • Divne, C.1    Ståhlberg, J.2    Reinikainen, T.3    Ruohonen, L.4    Pettersson, G.5    Knowles, J.K.6
  • 38
    • 0345676498 scopus 로고    scopus 로고
    • High-resolution crystal structures reveal how a cellulose chain is bound in the 50 ångstrom long tunnel of cellobiohydrolase I from Trichoderma reesei
    • Divne C., Ståhlberg J., Teeri T.T., Jones T.A. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 ångstrom long tunnel of cellobiohydrolase I from Trichoderma reesei. Journal of Molecular Biology 1998, 275:309-325.
    • (1998) Journal of Molecular Biology , vol.275 , pp. 309-325
    • Divne, C.1    Ståhlberg, J.2    Teeri, T.T.3    Jones, T.A.4
  • 39
    • 34249883838 scopus 로고    scopus 로고
    • Cellulose microfibril aggregates and their size variation with cell wall type
    • Donaldson L. Cellulose microfibril aggregates and their size variation with cell wall type. Wood Science and Technology 2007, 41:443-460.
    • (2007) Wood Science and Technology , vol.41 , pp. 443-460
    • Donaldson, L.1
  • 41
    • 79961228770 scopus 로고    scopus 로고
    • The plant cell wall-decomposing machinery underlies the functional diversity of forest fungi
    • Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P., Aerts A., et al. The plant cell wall-decomposing machinery underlies the functional diversity of forest fungi. Science 2011, 333:762-765.
    • (2011) Science , vol.333 , pp. 762-765
    • Eastwood, D.C.1    Floudas, D.2    Binder, M.3    Majcherczyk, A.4    Schneider, P.5    Aerts, A.6
  • 42
    • 0003981072 scopus 로고
    • Microbial and enzymatic degradation of wood and wood components
    • Springer Verlag, Berlin, Heidelberg, Germany
    • Eriksson K.-E.L., Blanchette R.A., Ander P. Microbial and enzymatic degradation of wood and wood components. Springer series in wood science 1990, Springer Verlag, Berlin, Heidelberg, Germany.
    • (1990) Springer series in wood science
    • Eriksson, K.-E.L.1    Blanchette, R.A.2    Ander, P.3
  • 43
    • 0037008410 scopus 로고    scopus 로고
    • Mechanism of surfactant effect in enzymatic hydrolysis of lignocellulose
    • Eriksson T., Börjesson J., Tjerneld F. Mechanism of surfactant effect in enzymatic hydrolysis of lignocellulose. Enzyme and Microbial Technology 2002, 31:353-364.
    • (2002) Enzyme and Microbial Technology , vol.31 , pp. 353-364
    • Eriksson, T.1    Börjesson, J.2    Tjerneld, F.3
  • 44
    • 84954875039 scopus 로고
    • The 1,4-β-D-glucan cellobiohydrolases of T. reesei QM 9414. A new type of cellulolytic synergism
    • Fägerstam L.G., Pettersson L.G. The 1,4-β-D-glucan cellobiohydrolases of T. reesei QM 9414. A new type of cellulolytic synergism. FEBS Letters 1980, 119:97-100.
    • (1980) FEBS Letters , vol.119 , pp. 97-100
    • Fägerstam, L.G.1    Pettersson, L.G.2
  • 45
    • 50649122075 scopus 로고    scopus 로고
    • Cellulose-water interactions during enzymatic hydrolysis as studied by time domain NMR
    • Felby C., Thygesen L.G., Kristensen J.B., Jørgensen H., Elder T. Cellulose-water interactions during enzymatic hydrolysis as studied by time domain NMR. Cellulose 2008, 15:703-710.
    • (2008) Cellulose , vol.15 , pp. 703-710
    • Felby, C.1    Thygesen, L.G.2    Kristensen, J.B.3    Jørgensen, H.4    Elder, T.5
  • 47
    • 0142022169 scopus 로고    scopus 로고
    • A new wood-decaying basidiomycete species associated with esca of grapevine: Fomitiporia mediterranea (Hymenochaetales)
    • Fischer M. A new wood-decaying basidiomycete species associated with esca of grapevine: Fomitiporia mediterranea (Hymenochaetales). Mycological Progress 2002, 1:315-324.
    • (2002) Mycological Progress , vol.1 , pp. 315-324
    • Fischer, M.1
  • 48
    • 84862977387 scopus 로고    scopus 로고
    • The Paleozoic origin of enzymatic lignin decomposition reconstructed from 31 fungal genomes
    • Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B., et al. The Paleozoic origin of enzymatic lignin decomposition reconstructed from 31 fungal genomes. Science 2012, 336:1715-1719. 10.1126/science.1221748.
    • (2012) Science , vol.336 , pp. 1715-1719
    • Floudas, D.1    Binder, M.2    Riley, R.3    Barry, K.4    Blanchette, R.A.5    Henrissat, B.6
  • 50
    • 0042099120 scopus 로고    scopus 로고
    • Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and linker sequence of cellobiohydrolase I from Penicillium janthinellum
    • Gao P.-J., Chen G.-J., Wang T.-H., Zhang Y.-S., Liu J. Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and linker sequence of cellobiohydrolase I from Penicillium janthinellum. Acta Biochimica et Biophysica Sinica 2001, 33:13-18.
    • (2001) Acta Biochimica et Biophysica Sinica , vol.33 , pp. 13-18
    • Gao, P.-J.1    Chen, G.-J.2    Wang, T.-H.3    Zhang, Y.-S.4    Liu, J.5
  • 51
    • 33947256880 scopus 로고    scopus 로고
    • Cellulosomes: Microbial nanomachines that display plasticity in quaternary structure
    • Gilbert H.J. Cellulosomes: Microbial nanomachines that display plasticity in quaternary structure. Molecular Microbiology 2007, 63:1568-1576.
    • (2007) Molecular Microbiology , vol.63 , pp. 1568-1576
    • Gilbert, H.J.1
  • 54
    • 0001051337 scopus 로고
    • The cellulase system of Trichoderma. Relationships between purified extracellular enzymes from induced or cellulose-grown cells
    • Gritzali M., Brown R.D. The cellulase system of Trichoderma. Relationships between purified extracellular enzymes from induced or cellulose-grown cells. Advances in Chemistry Series 1979, 81:237-260.
    • (1979) Advances in Chemistry Series , vol.81 , pp. 237-260
    • Gritzali, M.1    Brown, R.D.2
  • 57
    • 84877736930 scopus 로고    scopus 로고
    • Binding specificity and thermodynamics of cellulose-binding modules from Trichoderma reesei Cel7A and Cel6A
    • Guo J., Catchmark J.M. Binding specificity and thermodynamics of cellulose-binding modules from Trichoderma reesei Cel7A and Cel6A. Biomacromolecules 2013, 14:1268-1277.
    • (2013) Biomacromolecules , vol.14 , pp. 1268-1277
    • Guo, J.1    Catchmark, J.M.2
  • 58
    • 0442276356 scopus 로고    scopus 로고
    • Evaluation of novel wood-rotting polypores and corticioid fungi for the decay and biopulping of Norway spruce (Picea abies) wood
    • Hakala T.K., Maijala P., Konn J., Hatakka A. Evaluation of novel wood-rotting polypores and corticioid fungi for the decay and biopulping of Norway spruce (Picea abies) wood. Enzyme and Microbial Technology 2004, 34:255-263.
    • (2004) Enzyme and Microbial Technology , vol.34 , pp. 255-263
    • Hakala, T.K.1    Maijala, P.2    Konn, J.3    Hatakka, A.4
  • 59
    • 80052394586 scopus 로고    scopus 로고
    • The cellulose-binding domain of cellobiohydrolase Cel7A from Trichoderma reesei is also a thermostabilizing domain
    • Hall M., Rubin J., Behrens S.H., Bommarius A.S. The cellulose-binding domain of cellobiohydrolase Cel7A from Trichoderma reesei is also a thermostabilizing domain. Journal of Biotechnology 2011, 155:370-376.
    • (2011) Journal of Biotechnology , vol.155 , pp. 370-376
    • Hall, M.1    Rubin, J.2    Behrens, S.H.3    Bommarius, A.S.4
  • 61
    • 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 P.V., Welner D., McFarland K.C., Re E., Navarro Poulsen J.C., Brown K., et al. Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: Structure and function of a large, enigmatic family. Biochemistry 2010, 49:3305-3316.
    • (2010) Biochemistry , vol.49 , pp. 3305-3316
    • Harris, P.V.1    Welner, D.2    McFarland, K.C.3    Re, E.4    Navarro Poulsen, J.C.5    Brown, K.6
  • 62
    • 84856287089 scopus 로고    scopus 로고
    • Fungal chitinases: Diversity, mechanistic properties and biotechnological potential
    • Hartl L., Zach S., Seidl-Seiboth V. Fungal chitinases: Diversity, mechanistic properties and biotechnological potential. Applied Microbiology and Biotechnology 2012, 93:533-543.
    • (2012) Applied Microbiology and Biotechnology , vol.93 , pp. 533-543
    • Hartl, L.1    Zach, S.2    Seidl-Seiboth, V.3
  • 63
    • 84899133766 scopus 로고    scopus 로고
    • Fungal biodegradation of lignocelluloses. In K. Esser (Ed-in-chief), The Mycota: A comprehensive treatise on fungi as experimental systems for basic and applied research (2nd ed.). In M. Hofrichter (Vol. Ed.), Mycota X. Industrial applications (pp. 319-340). Springer-Verlag, Berlin, Heidelberg (chapter 15).
    • Hatakka, A., & Hammel, K. E. (2010). Fungal biodegradation of lignocelluloses. In K. Esser (Ed-in-chief), The Mycota: A comprehensive treatise on fungi as experimental systems for basic and applied research (2nd ed.). In M. Hofrichter (Vol. Ed.), Mycota X. Industrial applications (pp. 319-340). Springer-Verlag, Berlin, Heidelberg (chapter 15).
    • (2010)
    • Hatakka, A.1    Hammel, K.E.2
  • 65
    • 33846951759 scopus 로고    scopus 로고
    • Biomass recalcitrance: Engineering plants and enzymes for biofuels production
    • Himmel M.E., Ding S.Y., Johnson D.K., Adney W.S., Nimlos M.R., Brady J.W., et al. Biomass recalcitrance: Engineering plants and enzymes for biofuels production. Science 2007, 315:804-807.
    • (2007) Science , vol.315 , pp. 804-807
    • Himmel, M.E.1    Ding, S.Y.2    Johnson, D.K.3    Adney, W.S.4    Nimlos, M.R.5    Brady, J.W.6
  • 66
    • 84892379836 scopus 로고    scopus 로고
    • Genome-wide analysis of polysaccharides degrading enzymes in 11 white- and brown-rot Polyporales provides insight into mechanisms of wood decay
    • Hori C., Gaskell J., Igarashi K., Samejima M., Hibbett D., Henrissat B., et al. Genome-wide analysis of polysaccharides degrading enzymes in 11 white- and brown-rot Polyporales provides insight into mechanisms of wood decay. Mycologia 2013, 105:1412-1427.
    • (2013) Mycologia , vol.105 , pp. 1412-1427
    • Hori, C.1    Gaskell, J.2    Igarashi, K.3    Samejima, M.4    Hibbett, D.5    Henrissat, B.6
  • 69
    • 82855161474 scopus 로고    scopus 로고
    • Bioconversion of lignocellulose into bioethanol: Process intensification and mechanism research
    • Huang R., Su R., Qi W., He Z. Bioconversion of lignocellulose into bioethanol: Process intensification and mechanism research. Bioenergy Research 2011, 4:225-245.
    • (2011) Bioenergy Research , vol.4 , pp. 225-245
    • Huang, R.1    Su, R.2    Qi, W.3    He, Z.4
  • 71
    • 73649106924 scopus 로고    scopus 로고
    • High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase I on crystalline cellulose
    • Igarashi K., Koivula A., Wada M., Kimura S., Penttilä M., Samejima M. High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase I on crystalline cellulose. Journal of Biological Chemistry 2009, 284:36186-36190.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 36186-36190
    • Igarashi, K.1    Koivula, A.2    Wada, M.3    Kimura, S.4    Penttilä, M.5    Samejima, M.6
  • 72
    • 80052514287 scopus 로고    scopus 로고
    • Traffic jams reduce hydrolytic efficiency of cellulase on cellulose surface
    • Igarashi K., Uchihashi T., Koivula A., Wada M., Kimura S., Okamoto T., et al. Traffic jams reduce hydrolytic efficiency of cellulase on cellulose surface. Science 2011, 333:1279-1282.
    • (2011) Science , vol.333 , pp. 1279-1282
    • Igarashi, K.1    Uchihashi, T.2    Koivula, A.3    Wada, M.4    Kimura, S.5    Okamoto, T.6
  • 73
    • 0031666637 scopus 로고    scopus 로고
    • Unidirectional processive action of cellobiohydrolase Cel7A on Valonia cellulose microcrystals
    • Imai T., Boisset C., Samejima M., Igarashi K., Sugiyama J. Unidirectional processive action of cellobiohydrolase Cel7A on Valonia cellulose microcrystals. FEBS Letters 1998, 432:113-116.
    • (1998) FEBS Letters , vol.432 , pp. 113-116
    • Imai, T.1    Boisset, C.2    Samejima, M.3    Igarashi, K.4    Sugiyama, J.5
  • 75
    • 77955691535 scopus 로고    scopus 로고
    • Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis
    • Jalak J., Väljamäe P. Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis. Biotechnology and Bioengineering 2010, 106:871-883.
    • (2010) Biotechnology and Bioengineering , vol.106 , pp. 871-883
    • Jalak, J.1    Väljamäe, P.2
  • 76
    • 84860359533 scopus 로고    scopus 로고
    • A novel integrated biological process for cellulosic ethanol production featuring high ethanol productivity, enzyme recycling and yeast cells reuse
    • Jin M.J., Gunawan C., Uppugundla N., Balan V., Dale B.E. A novel integrated biological process for cellulosic ethanol production featuring high ethanol productivity, enzyme recycling and yeast cells reuse. Energy & Environmental Science 2012, 5:7168-7175.
    • (2012) Energy & Environmental Science , vol.5 , pp. 7168-7175
    • Jin, M.J.1    Gunawan, C.2    Uppugundla, N.3    Balan, V.4    Dale, B.E.5
  • 78
    • 70350590693 scopus 로고    scopus 로고
    • The genes encoding glycoside hydrolase family 6 and 7 cellulases from the brown-rot fungus Coniophora puteana
    • Kajisa T., Igarashi K., Samejima M. The genes encoding glycoside hydrolase family 6 and 7 cellulases from the brown-rot fungus Coniophora puteana. Journal of Wood Science 2009, 55:376-380.
    • (2009) Journal of Wood Science , vol.55 , pp. 376-380
    • Kajisa, T.1    Igarashi, K.2    Samejima, M.3
  • 79
    • 0037048802 scopus 로고    scopus 로고
    • Enzymatic properties of the low molecular mass endoglucanases Cel12A (EG III) and Cel45A (EG V) of Trichoderma reesei
    • Karlsson J., Siika-aho M., Tenkanen M., Tjerneld F. Enzymatic properties of the low molecular mass endoglucanases Cel12A (EG III) and Cel45A (EG V) of Trichoderma reesei. Journal of Biotechnology 2002, 99:63-78.
    • (2002) Journal of Biotechnology , vol.99 , pp. 63-78
    • Karlsson, J.1    Siika-aho, M.2    Tenkanen, M.3    Tjerneld, F.4
  • 80
    • 0030841474 scopus 로고    scopus 로고
    • Adsorption behaviors of two cellobiohydrolases and their core proteins from Trichoderma reesei on Avicel PH101
    • Kim D.W., Jang Y.H., Jeong Y.K. Adsorption behaviors of two cellobiohydrolases and their core proteins from Trichoderma reesei on Avicel PH101. Biotechnology Letters 1997, 19:893-897.
    • (1997) Biotechnology Letters , vol.19 , pp. 893-897
    • Kim, D.W.1    Jang, Y.H.2    Jeong, Y.K.3
  • 81
    • 0001035759 scopus 로고
    • Quantitative changes in structural components of conifer wood during decay by white-rot and brown-rot fungi
    • Kirk T.K., Highley T.L. Quantitative changes in structural components of conifer wood during decay by white-rot and brown-rot fungi. Phytopathology 1973, 63:1338-1342.
    • (1973) Phytopathology , vol.63 , pp. 1338-1342
    • Kirk, T.K.1    Highley, T.L.2
  • 82
    • 0029743877 scopus 로고    scopus 로고
    • The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size
    • Kleman-Leyer K.M., Siika-aho M., Teeri T.T., Kirk T.K. The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size. Applied and Environmental Microbiology 1996, 62:2883-2887.
    • (1996) Applied and Environmental Microbiology , vol.62 , pp. 2883-2887
    • Kleman-Leyer, K.M.1    Siika-aho, M.2    Teeri, T.T.3    Kirk, T.K.4
  • 83
    • 0032537565 scopus 로고    scopus 로고
    • Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A
    • Koivula A., Kinnari T., Harjunpää V., Ruohonen L., Teleman A., Drakenberg T., et al. Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A. FEBS Letters 1998, 429:341-346.
    • (1998) FEBS Letters , vol.429 , pp. 341-346
    • Koivula, A.1    Kinnari, T.2    Harjunpää, V.3    Ruohonen, L.4    Teleman, A.5    Drakenberg, T.6
  • 84
    • 84055221845 scopus 로고    scopus 로고
    • Synergistic interactions in cellulose hydrolysis
    • Kostylev M., Wilson D. Synergistic interactions in cellulose hydrolysis. Biofuels 2012, 3:61-70.
    • (2012) Biofuels , vol.3 , pp. 61-70
    • Kostylev, M.1    Wilson, D.2
  • 85
    • 0001958030 scopus 로고    scopus 로고
    • Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II and the corresponding core proteins on steam pretreated willow
    • Kotiranta P., Karlsson J., Siika-aho M., Medve J., Viikari L., Tjerneld F., et al. Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II and the corresponding core proteins on steam pretreated willow. Applied Biochemistry and Biotechnology 1999, 81:81-90.
    • (1999) Applied Biochemistry and Biotechnology , vol.81 , pp. 81-90
    • Kotiranta, P.1    Karlsson, J.2    Siika-aho, M.3    Medve, J.4    Viikari, L.5    Tjerneld, F.6
  • 86
    • 0024962351 scopus 로고
    • Determination of the 3-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic-resonance and hybrid distance geometry dynamical simulated annealing
    • Kraulis P.J., Clore G.M., Nilges M., Jones T.A., Pettersson G., Knowles J., et al. Determination of the 3-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic-resonance and hybrid distance geometry dynamical simulated annealing. Biochemistry 1989, 28:7241-7257.
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, P.J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6
  • 88
    • 82455164783 scopus 로고    scopus 로고
    • The lignin present in steam pretreated softwood binds enzymes and limits cellulose accessibility
    • Kumar L., Arantes V., Chandra R., Saddler J. The lignin present in steam pretreated softwood binds enzymes and limits cellulose accessibility. Bioresource Technology 2012, 103:201-208.
    • (2012) Bioresource Technology , vol.103 , pp. 201-208
    • Kumar, L.1    Arantes, V.2    Chandra, R.3    Saddler, J.4
  • 89
    • 78650950110 scopus 로고    scopus 로고
    • Processivity of cellobiohydrolases is limited by the substrate
    • Kurasin M., Väljamäe P. Processivity of cellobiohydrolases is limited by the substrate. Journal of Biological Chemistry 2011, 286:169-177.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 169-177
    • Kurasin, M.1    Väljamäe, P.2
  • 91
    • 84899131461 scopus 로고    scopus 로고
    • Family 6 cellulase with decreased inactivation by lignin. Application no. WO/2010/012102. Publication date 04/02/2010.
    • Lavigne, J., Scott, B., Whissel, M., & Tomashek, J. (2010). Family 6 cellulase with decreased inactivation by lignin. Application no. WO/2010/012102. Publication date 04/02/2010.
    • (2010)
    • Lavigne, J.1    Scott, B.2    Whissel, M.3    Tomashek, J.4
  • 92
    • 84879583804 scopus 로고    scopus 로고
    • The role of carbohydrate binding module (CBM) at high substrate consistency: Comparison of Trichoderma reesei and Thermoascus aurantiacus Cel7A (CBH I) and Cel5A (EG II)
    • Le Costaouëc T., Pakarinen A., Várnai A., Puranen T., Viikari L. The role of carbohydrate binding module (CBM) at high substrate consistency: Comparison of Trichoderma reesei and Thermoascus aurantiacus Cel7A (CBH I) and Cel5A (EG II). Bioresource Technology 2013, 143:196-203.
    • (2013) Bioresource Technology , vol.143 , pp. 196-203
    • Le Costaouëc, T.1    Pakarinen, A.2    Várnai, A.3    Puranen, T.4    Viikari, L.5
  • 93
    • 0033979485 scopus 로고    scopus 로고
    • The mechanism of cellulase action on cotton fibers: Evidence from atomic force microscopy
    • Lee I., Evans B.R., Woodward J. The mechanism of cellulase action on cotton fibers: Evidence from atomic force microscopy. Ultramicroscopy 2000, 82:213-221.
    • (2000) Ultramicroscopy , vol.82 , pp. 213-221
    • Lee, I.1    Evans, B.R.2    Woodward, J.3
  • 94
    • 0029239562 scopus 로고
    • Evaluation of cellulase recycling strategies for the hydrolysis of lignocellulosic substrates
    • Lee D., Yu A.H.C., Saddler J.N. Evaluation of cellulase recycling strategies for the hydrolysis of lignocellulosic substrates. Biotechnology and Bioengineering 1995, 45:328-336.
    • (1995) Biotechnology and Bioengineering , vol.45 , pp. 328-336
    • Lee, D.1    Yu, A.H.C.2    Saddler, J.N.3
  • 97
    • 0030780751 scopus 로고    scopus 로고
    • Two cellulases, CelA and CelC, from the polycentric anaerobic fungus Orpinomyces strain PC-2 contain N-terminal docking domains for a cellulase±hemicellulase complex
    • Li X.L., Chen H., Ljungdahl L.G. Two cellulases, CelA and CelC, from the polycentric anaerobic fungus Orpinomyces strain PC-2 contain N-terminal docking domains for a cellulase±hemicellulase complex. Applied and Environmental Microbiology 1997, 63:4721-4728.
    • (1997) Applied and Environmental Microbiology , vol.63 , pp. 4721-4728
    • Li, X.L.1    Chen, H.2    Ljungdahl, L.G.3
  • 98
    • 34247141555 scopus 로고    scopus 로고
    • Lignin depolymerisation/repolymerization and its critical role for delignification of aspen wood by steam explosion
    • Li J., Henriksson G., Gellerstedt G. Lignin depolymerisation/repolymerization and its critical role for delignification of aspen wood by steam explosion. Bioresource Technology 2007, 98:3061-3068.
    • (2007) Bioresource Technology , vol.98 , pp. 3061-3068
    • Li, J.1    Henriksson, G.2    Gellerstedt, G.3
  • 100
    • 84884131639 scopus 로고    scopus 로고
    • Recycling cellulases for cellulosic ethanol production at industrial relevant conditions: Potential and temperature dependency at high solid processes
    • Lindedam J., Haven M.Ø., Chylenski P., Jørgensen H., Felby C. Recycling cellulases for cellulosic ethanol production at industrial relevant conditions: Potential and temperature dependency at high solid processes. Bioresource Technology 2013, 148:180-188.
    • (2013) Bioresource Technology , vol.148 , pp. 180-188
    • Lindedam, J.1    Haven, M.Ø.2    Chylenski, P.3    Jørgensen, H.4    Felby, C.5
  • 101
    • 0029023464 scopus 로고
    • Identification of functionally important amino acids in the cellulose-binding domain of Trichoderma reesei cellobiohydrolase I
    • Linder M., Mattinen M.L., Kontteli M., Lindeberg G., Ståhlberg J., Drakenberg T., et al. Identification of functionally important amino acids in the cellulose-binding domain of Trichoderma reesei cellobiohydrolase I. Protein Science 1995, 4:1056-1064.
    • (1995) Protein Science , vol.4 , pp. 1056-1064
    • Linder, M.1    Mattinen, M.L.2    Kontteli, M.3    Lindeberg, G.4    Ståhlberg, J.5    Drakenberg, T.6
  • 102
    • 0029861144 scopus 로고    scopus 로고
    • The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose
    • Linder M., Teeri T.T. The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose. Proceedings of the National Academy of Sciences of the United States of America 1996, 93:12251-12255.
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , pp. 12251-12255
    • Linder, M.1    Teeri, T.T.2
  • 105
    • 0036240767 scopus 로고    scopus 로고
    • Cellulase adsorption and an evaluation of enzyme recycle during hydrolysis of steam-exploded softwood residues
    • Lu Y., Yang B., Gregg D., Saddler J.N., Mansfield S.D. Cellulase adsorption and an evaluation of enzyme recycle during hydrolysis of steam-exploded softwood residues. Applied Biochemistry and Biotechnology 2002, 98-100:641-654.
    • (2002) Applied Biochemistry and Biotechnology , pp. 641-654
    • Lu, Y.1    Yang, B.2    Gregg, D.3    Saddler, J.N.4    Mansfield, S.D.5
  • 108
    • 42749089142 scopus 로고    scopus 로고
    • The enzymatic hydrolysis rate of cellulose decreases with irreversible adsorption of cellobiohydrolase I
    • Ma A., Hu Q., Qua Y., Bai Z., Liu W., Zhuang G. The enzymatic hydrolysis rate of cellulose decreases with irreversible adsorption of cellobiohydrolase I. Enzyme and Microbial Technology 2008, 42:543-547.
    • (2008) Enzyme and Microbial Technology , vol.42 , pp. 543-547
    • Ma, A.1    Hu, Q.2    Qua, Y.3    Bai, Z.4    Liu, W.5    Zhuang, G.6
  • 109
    • 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., Canam T., Gong Y.C., Guttman D.S., Campbell M.M., et al. Transcriptomic responses of the softwood-degrading white-rot fungus Phanerochaete carnosa during growth on coniferous and deciduous wood. Applied and Environmental Microbiology 2011, 77:3211-3218.
    • (2011) Applied and Environmental Microbiology , 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
  • 110
    • 84863395511 scopus 로고    scopus 로고
    • Expression and regulation of genes encoding lignocellulose-degrading activity in the genus Phanerochaete
    • MacDonald J., Suzuki H., Master E.R. Expression and regulation of genes encoding lignocellulose-degrading activity in the genus Phanerochaete. Applied Microbiology and Biotechnology 2012, 94:339-351.
    • (2012) Applied Microbiology and Biotechnology , vol.94 , pp. 339-351
    • MacDonald, J.1    Suzuki, H.2    Master, E.R.3
  • 111
    • 77952882025 scopus 로고    scopus 로고
    • Lignocellulose-degrading enzymes secreted by Phanerochaeate carnosa grown on spruce and microcrystalline cellulose
    • Mahajan S., Master E.R. Lignocellulose-degrading enzymes secreted by Phanerochaeate carnosa grown on spruce and microcrystalline cellulose. Applied Microbiology and Biotechnology 2010, 86:1903-1914.
    • (2010) Applied Microbiology and Biotechnology , vol.86 , pp. 1903-1914
    • Mahajan, S.1    Master, E.R.2
  • 112
    • 84899138567 scopus 로고    scopus 로고
    • Degradation and modification of plant biomass by fungi. In K. Esser & M. Nowrousian (Eds.), The Mycota: A comprehensive treatise on fungi as experimental systems for basic and applied research. In M. Nowrousian (Vol. Ed.), Fungal genomics. Springer-Verlag (in press).
    • Mäkelä, M. R., Hildén, K. S., & de Vries, R. P. (2014). Degradation and modification of plant biomass by fungi. In K. Esser & M. Nowrousian (Eds.), The Mycota: A comprehensive treatise on fungi as experimental systems for basic and applied research. In M. Nowrousian (Vol. Ed.), Fungal genomics. Springer-Verlag (in press).
    • (2014)
    • Mäkelä, M.R.1    Hildén, K.S.2    De Vries, R.P.3
  • 113
    • 0029884769 scopus 로고    scopus 로고
    • Adsorption of poly(ethylene glycol) amphiphiles to form coatings which inhibit protein adsorption
    • Malmsten M., van Alstine J.M. Adsorption of poly(ethylene glycol) amphiphiles to form coatings which inhibit protein adsorption. Journal of Colloid and Interface Science 1996, 177:502-512.
    • (1996) Journal of Colloid and Interface Science , vol.177 , pp. 502-512
    • Malmsten, M.1    van Alstine, J.M.2
  • 114
    • 43449098828 scopus 로고    scopus 로고
    • Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina)
    • Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E., et al. Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina). Nature Biotechnology 2008, 26:553-560.
    • (2008) Nature Biotechnology , vol.26 , pp. 553-560
    • Martinez, D.1    Berka, R.M.2    Henrissat, B.3    Saloheimo, M.4    Arvas, M.5    Baker, S.E.6
  • 116
    • 2542601548 scopus 로고    scopus 로고
    • Genome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78
    • Martinez D., Larrondo L.F., Putnam N., Gelpke M.D., Huang K., Chapman J., et al. Genome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78. Nature Biotechnology 2004, 22:695-700.
    • (2004) Nature Biotechnology , vol.22 , pp. 695-700
    • Martinez, D.1    Larrondo, L.F.2    Putnam, N.3    Gelpke, M.D.4    Huang, K.5    Chapman, J.6
  • 118
    • 0032487130 scopus 로고    scopus 로고
    • Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei: Adsorption, sugar production pattern, and synergism of the enzymes
    • Medve J., Karlsson J., Lee D., Tjerneld F. Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei: Adsorption, sugar production pattern, and synergism of the enzymes. Biotechnology and Bioengineering 1998, 59:621-634.
    • (1998) Biotechnology and Bioengineering , vol.59 , pp. 621-634
    • Medve, J.1    Karlsson, J.2    Lee, D.3    Tjerneld, F.4
  • 119
    • 0028765765 scopus 로고
    • Adsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline cellulose
    • Medve J., Ståhlberg J., Tjerneld F. Adsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline cellulose. Biotechnology and Bioengineering 1994, 44:1064-1073.
    • (1994) Biotechnology and Bioengineering , vol.44 , pp. 1064-1073
    • Medve, J.1    Ståhlberg, J.2    Tjerneld, F.3
  • 120
    • 85027952469 scopus 로고    scopus 로고
    • Trends in bioconversion of lignocellulose: Biofuels, platform chemicals & biorefinery concept
    • Menon V., Rao M. Trends in bioconversion of lignocellulose: Biofuels, platform chemicals & biorefinery concept. Progress in Energy and Combustion Science 2012, 38:522-550.
    • (2012) Progress in Energy and Combustion Science , vol.38 , pp. 522-550
    • Menon, V.1    Rao, M.2
  • 121
    • 84875361266 scopus 로고    scopus 로고
    • Hydrolysis of konjac glucomannan by Trichoderma reesei mannanase and endoglucanases Cel7B and Cel5A for the production of glucomanno-oligosaccharides
    • Mikkelson A., Maaheimo H., Hakala T.K. Hydrolysis of konjac glucomannan by Trichoderma reesei mannanase and endoglucanases Cel7B and Cel5A for the production of glucomanno-oligosaccharides. Carbohydrate Research 2013, 372:60-68.
    • (2013) Carbohydrate Research , vol.372 , pp. 60-68
    • Mikkelson, A.1    Maaheimo, H.2    Hakala, T.K.3
  • 122
    • 0032079694 scopus 로고    scopus 로고
    • The effect of initial pore volume and lignin content on the enzymatic hydrolysis of softwoods
    • Mooney C.A., Mansfield S.D., Touhy M.G., Saddler J.N. The effect of initial pore volume and lignin content on the enzymatic hydrolysis of softwoods. Bioresource Technology 1998, 64:113-119.
    • (1998) Bioresource Technology , vol.64 , pp. 113-119
    • Mooney, C.A.1    Mansfield, S.D.2    Touhy, M.G.3    Saddler, J.N.4
  • 125
    • 79551689708 scopus 로고    scopus 로고
    • The isolation, characterization and effect of lignin isolated from steam pretreated Douglas-fir on the enzymatic hydrolysis of cellulose
    • Nakagame S., Chandra R.P., Kadla J.F., Saddler J.N. The isolation, characterization and effect of lignin isolated from steam pretreated Douglas-fir on the enzymatic hydrolysis of cellulose. Bioresource Technology 2011, 102:4507-4517.
    • (2011) Bioresource Technology , vol.102 , pp. 4507-4517
    • Nakagame, S.1    Chandra, R.P.2    Kadla, J.F.3    Saddler, J.N.4
  • 126
    • 84905483809 scopus 로고    scopus 로고
    • The influence of lignin on the enzymatic hydrolysis of pretreated biomass substrates
    • American Chemical Society, Washington, DC, chapter 6, J.Y. Zhu, X. Zhang, X.J. Pan (Eds.) Sustainable production of fuels, chemicals, and fibers from forest biomass
    • Nakagame S., Chandra R.P., Saddler J.N. The influence of lignin on the enzymatic hydrolysis of pretreated biomass substrates. ACS Symposium Series 2011, Vol. 1067:145-167. American Chemical Society, Washington, DC, chapter 6. J.Y. Zhu, X. Zhang, X.J. Pan (Eds.).
    • (2011) ACS Symposium Series , vol.1067 , pp. 145-167
    • Nakagame, S.1    Chandra, R.P.2    Saddler, J.N.3
  • 127
    • 84877698510 scopus 로고    scopus 로고
    • The tryptophan residue at the active site tunnel entrance of Trichoderma reesei cellobiohydrolase Cel7A is important for initiation of degradation of crystalline cellulose
    • Nakamura A., Tsukuda T., Auer S., Furuta T., Wada M., Koivula A., et al. The tryptophan residue at the active site tunnel entrance of Trichoderma reesei cellobiohydrolase Cel7A is important for initiation of degradation of crystalline cellulose. The Journal of Biological Chemistry 2013, 288:13503-13510.
    • (2013) The Journal of Biological Chemistry , vol.288 , pp. 13503-13510
    • Nakamura, A.1    Tsukuda, T.2    Auer, S.3    Furuta, T.4    Wada, M.5    Koivula, A.6
  • 128
    • 0013265869 scopus 로고
    • A new species, Phlebia brevispora, a cause of internal decay in utility poles
    • Nakasone K.K., Eslyn W.E. A new species, Phlebia brevispora, a cause of internal decay in utility poles. Mycologia 1981, 73:803-810.
    • (1981) Mycologia , vol.73 , pp. 803-810
    • Nakasone, K.K.1    Eslyn, W.E.2
  • 129
    • 0028483694 scopus 로고
    • Specific quantification of Trichoderma reesei cellulases in reconstituted mixtures and its application to cellulase-cellulose binding studies
    • Nidetzky B., Claeyssens M. Specific quantification of Trichoderma reesei cellulases in reconstituted mixtures and its application to cellulase-cellulose binding studies. Biotechnology and Bioengineering 1994, 44:961-966.
    • (1994) Biotechnology and Bioengineering , vol.44 , pp. 961-966
    • Nidetzky, B.1    Claeyssens, M.2
  • 130
    • 0028152402 scopus 로고
    • Cellulose hydrolysis by the cellulases from Trichoderma reesei: Adsorptions of two cellobiohydrolases, two endocellulases and their core proteins on filter paper and their relation to hydrolysis
    • Nidetzky B., Steiner W., Claeyssens M. Cellulose hydrolysis by the cellulases from Trichoderma reesei: Adsorptions of two cellobiohydrolases, two endocellulases and their core proteins on filter paper and their relation to hydrolysis. The Biochemical Journal 1994, 303:817-823.
    • (1994) The Biochemical Journal , vol.303 , pp. 817-823
    • Nidetzky, B.1    Steiner, W.2    Claeyssens, M.3
  • 131
    • 0242275021 scopus 로고    scopus 로고
    • The kelo tree, a vanishing substrate of specified wood-inhabiting fungi
    • Niemelä T., Wallenius T., Kotiranta H. The kelo tree, a vanishing substrate of specified wood-inhabiting fungi. Polish Botanical Journal 2002, 47:91-101.
    • (2002) Polish Botanical Journal , vol.47 , pp. 91-101
    • Niemelä, T.1    Wallenius, T.2    Kotiranta, H.3
  • 132
    • 84862004181 scopus 로고    scopus 로고
    • Binding preferences, surface attachment, diffusivity, and orientation of a family 1 carbohydrate-binding module on cellulose
    • Nimlos M.R., Beckham G.T., Matthews J.F., Bu L., Himmel M.E., Crowley M.F. Binding preferences, surface attachment, diffusivity, and orientation of a family 1 carbohydrate-binding module on cellulose. Journal of Biological Chemistry 2012, 287:20603-20612.
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 20603-20612
    • Nimlos, M.R.1    Beckham, G.T.2    Matthews, J.F.3    Bu, L.4    Himmel, M.E.5    Crowley, M.F.6
  • 134
    • 0030532365 scopus 로고    scopus 로고
    • Driving forces for protein adsorption at solid surfaces
    • Norde W. Driving forces for protein adsorption at solid surfaces. Macromolecular Symposia 1996, 103:5-18.
    • (1996) Macromolecular Symposia , vol.103 , pp. 5-18
    • Norde, W.1
  • 135
    • 77952931940 scopus 로고    scopus 로고
    • Improved enzymatic hydrolysis of microcrystalline cellulose (Avicel PH101) by polyethylene glycol addition
    • Ouyang J., Dong Z., Song X., Lee X., Chen M., Yong Q. Improved enzymatic hydrolysis of microcrystalline cellulose (Avicel PH101) by polyethylene glycol addition. Bioresource Technology 2010, 101:6685-6691.
    • (2010) Bioresource Technology , vol.101 , pp. 6685-6691
    • Ouyang, J.1    Dong, Z.2    Song, X.3    Lee, X.4    Chen, M.5    Yong, Q.6
  • 137
    • 0346363683 scopus 로고    scopus 로고
    • Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin
    • Palonen H., Tjerneld F., Zacchi G., Tenkanen M. Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin. Journal of Biotechnology 2004, 107:65-72.
    • (2004) Journal of Biotechnology , vol.107 , pp. 65-72
    • Palonen, H.1    Tjerneld, F.2    Zacchi, G.3    Tenkanen, M.4
  • 138
    • 63949083111 scopus 로고    scopus 로고
    • Optimization of hydrothermal pretreatment of wheat straw for production of bioethanol at low water consumption without addition of chemicals
    • Petersen M.Ø., Larsen J., Thomsen M.H. Optimization of hydrothermal pretreatment of wheat straw for production of bioethanol at low water consumption without addition of chemicals. Biomass and Bioenergy 2009, 33:834-840.
    • (2009) Biomass and Bioenergy , vol.33 , pp. 834-840
    • Petersen, M.Ø.1    Larsen, J.2    Thomsen, M.H.3
  • 139
    • 84856412882 scopus 로고    scopus 로고
    • The adsorption and enzyme activity profiles of specific Trichoderma reesei cellulase/xylanase components when hydrolyzing steam pretreated corn stover
    • Priwobo A., Arantes V., Saddler J.N. The adsorption and enzyme activity profiles of specific Trichoderma reesei cellulase/xylanase components when hydrolyzing steam pretreated corn stover. Enzyme and Microbial Technology 2012, 50:195-203.
    • (2012) Enzyme and Microbial Technology , vol.50 , pp. 195-203
    • Priwobo, A.1    Arantes, V.2    Saddler, J.N.3
  • 140
    • 84872786974 scopus 로고    scopus 로고
    • Assessing the molecular structure basis for biomass recalcitrance during dilute acid and hydrothermal pretreatments
    • Pu Y., Hu F., Huang F., Davison B.H., Ragauskas A.J. Assessing the molecular structure basis for biomass recalcitrance during dilute acid and hydrothermal pretreatments. Biotechnology for Biofuels 2013, 6:15.
    • (2013) Biotechnology for Biofuels , vol.6 , pp. 15
    • Pu, Y.1    Hu, F.2    Huang, F.3    Davison, B.H.4    Ragauskas, A.J.5
  • 144
    • 84874373872 scopus 로고    scopus 로고
    • Inhibitory effect of lignin during cellulose bioconversion: The effect of lignin chemistry on non-productive enzyme adsorption
    • Rahikainen J.L., Martin-Sampedro R., Heikkinen H., Rovio S., Marjamaa K., Tamminen T., et al. Inhibitory effect of lignin during cellulose bioconversion: The effect of lignin chemistry on non-productive enzyme adsorption. Bioresource Technology 2013, 133:270-278.
    • (2013) Bioresource Technology , vol.133 , pp. 270-278
    • Rahikainen, J.L.1    Martin-Sampedro, R.2    Heikkinen, H.3    Rovio, S.4    Marjamaa, K.5    Tamminen, T.6
  • 145
    • 80054037883 scopus 로고    scopus 로고
    • Inhibition of enzymatic hydrolysis by residual lignins from softwood-Study of enzyme binding and inactivation on lignin-rich surface
    • Rahikainen J., Mikander S., Marjamaa K., Tamminen T., Lappas A., Viikari L., et al. Inhibition of enzymatic hydrolysis by residual lignins from softwood-Study of enzyme binding and inactivation on lignin-rich surface. Biotechnology and Bioengineering 2011, 108:2823-2834.
    • (2011) Biotechnology and Bioengineering , vol.108 , pp. 2823-2834
    • Rahikainen, J.1    Mikander, S.2    Marjamaa, K.3    Tamminen, T.4    Lappas, A.5    Viikari, L.6
  • 146
    • 84881225487 scopus 로고    scopus 로고
    • Effect of temperature on lignin-derived inhibition studied with three structurally different cellobiohydrolases
    • Rahikainen J.L., Moilanen U., Nurmi-Rantala S., Lappas A., Koivula A., Viikari L., et al. Effect of temperature on lignin-derived inhibition studied with three structurally different cellobiohydrolases. Bioresource Technology 2013, 146:118-125.
    • (2013) Bioresource Technology , vol.146 , pp. 118-125
    • Rahikainen, J.L.1    Moilanen, U.2    Nurmi-Rantala, S.3    Lappas, A.4    Koivula, A.5    Viikari, L.6
  • 147
    • 0001651637 scopus 로고
    • Enzyme recycling during fed-batch hydrolysis of cellulose derived from steam-exploded Eucalyptus viminalis
    • Ramos L.P., Saddler J.N. Enzyme recycling during fed-batch hydrolysis of cellulose derived from steam-exploded Eucalyptus viminalis. Applied Biochemistry and Biotechnology 1994, 45:193-207.
    • (1994) Applied Biochemistry and Biotechnology , vol.45 , pp. 193-207
    • Ramos, L.P.1    Saddler, J.N.2
  • 148
    • 0030747617 scopus 로고    scopus 로고
    • The effect of oxidative pretreatment on cellulose degradation by Poria placenta and Trichoderma reesei cellulases
    • Rättö M., Ritschkoff A.-C., Viikari L. The effect of oxidative pretreatment on cellulose degradation by Poria placenta and Trichoderma reesei cellulases. Applied Microbiology and Biotechnology 1997, 48:53-57.
    • (1997) Applied Microbiology and Biotechnology , vol.48 , pp. 53-57
    • Rättö, M.1    Ritschkoff, A.-C.2    Viikari, L.3
  • 151
    • 0025182502 scopus 로고
    • Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei
    • Rouvinen J., Bergfors T., Teeri T., Knowles J.K., Jones T.A. Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. Science 1990, 249:380-386.
    • (1990) Science , vol.249 , pp. 380-386
    • Rouvinen, J.1    Bergfors, T.2    Teeri, T.3    Knowles, J.K.4    Jones, T.A.5
  • 152
    • 84908510106 scopus 로고    scopus 로고
    • Transcriptional analysis of selected cellulose-acting enzymes encoding genes of the white-rot fungus Dichomitus squalens on spruce wood and microcrystalline cellulose
    • in press
    • Rytioja J., Hildén K., Hatakka A., Mäkelä M.R. Transcriptional analysis of selected cellulose-acting enzymes encoding genes of the white-rot fungus Dichomitus squalens on spruce wood and microcrystalline cellulose. Fungal Genetics and Biology 2014, in press. 10.1016/j.fgb.2013.12.008.
    • (2014) Fungal Genetics and Biology
    • Rytioja, J.1    Hildén, K.2    Hatakka, A.3    Mäkelä, M.R.4
  • 153
    • 0026623553 scopus 로고
    • Characterization of the cellulolytic enzyme system from the brown-rot fungus Coniophora puteana
    • Schmidhalter D.R., Canevascini G. Characterization of the cellulolytic enzyme system from the brown-rot fungus Coniophora puteana. Applied Microbiology and Biotechnology 1992, 37:431-436.
    • (1992) Applied Microbiology and Biotechnology , vol.37 , pp. 431-436
    • Schmidhalter, D.R.1    Canevascini, G.2
  • 154
    • 84899138732 scopus 로고    scopus 로고
    • Novel lignin-resistant cellulase enzymes. Application no. WO2010096931. Publication date 02/09/2010.
    • Scott, B. R., StPierre, P., Lavigne, J., Masri, N., White, T. C., & Tomashek, J.J. (2010). Novel lignin-resistant cellulase enzymes. Application no. WO2010096931. Publication date 02/09/2010.
    • (2010)
    • Scott, B.R.1    StPierre, P.2    Lavigne, J.3    Masri, N.4    White, T.C.5    Tomashek, J.J.6
  • 155
    • 41849103104 scopus 로고    scopus 로고
    • Synergistic enhancement of cellobiohydrolase performance on pretreated corn stover by addition of xylanase and esterase activities
    • Selig M.J., Knoshaug E.P., Adney W.S., Himmel M.E., Decker S.R. Synergistic enhancement of cellobiohydrolase performance on pretreated corn stover by addition of xylanase and esterase activities. Bioresource Technology 2008, 99:4997-5005.
    • (2008) Bioresource Technology , vol.99 , pp. 4997-5005
    • Selig, M.J.1    Knoshaug, E.P.2    Adney, W.S.3    Himmel, M.E.4    Decker, S.R.5
  • 156
    • 0031983974 scopus 로고    scopus 로고
    • Plant-cell-wall-degrading enzymes produced by the white-rot fungus Ceriporiopsis subvermispora
    • Sethuraman A., Akin D.E., Eriksson K.-E.L. Plant-cell-wall-degrading enzymes produced by the white-rot fungus Ceriporiopsis subvermispora. Biotechnology and Applied Biochemistry 1998, 27:37-47.
    • (1998) Biotechnology and Applied Biochemistry , vol.27 , pp. 37-47
    • Sethuraman, A.1    Akin, D.E.2    Eriksson, K.-E.L.3
  • 161
    • 0024278446 scopus 로고
    • A binding-site-deficient, catalytically active, core protein of endoglucanase III from the culture filtrate of Trichoderma reesei
    • Ståhlberg J., Johansson G., Pettersson G. A binding-site-deficient, catalytically active, core protein of endoglucanase III from the culture filtrate of Trichoderma reesei. European Journal of Biochemistry 1988, 173:179-183.
    • (1988) European Journal of Biochemistry , vol.173 , pp. 179-183
    • Ståhlberg, J.1    Johansson, G.2    Pettersson, G.3
  • 162
    • 14744278342 scopus 로고
    • A new model for enzymatic hydrolysis of cellulose based on the two-domain structure of cellobiohydrolase I
    • Ståhlberg J., Johansson G., Pettersson G. A new model for enzymatic hydrolysis of cellulose based on the two-domain structure of cellobiohydrolase I. Nature Biotechnology 1991, 9:286-290.
    • (1991) Nature Biotechnology , vol.9 , pp. 286-290
    • Ståhlberg, J.1    Johansson, G.2    Pettersson, G.3
  • 163
    • 77956818710 scopus 로고    scopus 로고
    • Cellotriose and cellotetraose as inducers of the genes encoding cellobiohydrolases in the basidiomycete Phanerochaete chrysosporium
    • Suzuki H., Igarashi K., Samejima M. Cellotriose and cellotetraose as inducers of the genes encoding cellobiohydrolases in the basidiomycete Phanerochaete chrysosporium. Applied and Environmental Microbiology 2010, 76:6164-6170.
    • (2010) Applied and Environmental Microbiology , vol.76 , pp. 6164-6170
    • Suzuki, H.1    Igarashi, K.2    Samejima, M.3
  • 164
    • 78650690076 scopus 로고    scopus 로고
    • Liquefaction of hydrothermally pretreated wheat straw at high-solids content by purified Trichoderma enzymes
    • Szijártó N., Siika-aho M., Sontag-Strohm T., Viikari L. Liquefaction of hydrothermally pretreated wheat straw at high-solids content by purified Trichoderma enzymes. Bioresource Technology 2011, 102:1968-1974.
    • (2011) Bioresource Technology , vol.102 , pp. 1968-1974
    • Szijártó, N.1    Siika-aho, M.2    Sontag-Strohm, T.3    Viikari, L.4
  • 165
    • 33745194828 scopus 로고    scopus 로고
    • Enzymatic saccharification of wheat straw for bioethanol production by a combined cellulase xylanase and feruloyl esterase treatment
    • Tabka M.G., Herpoël-Gimbert I., Monod F., Asther M., Sigoillot J.C. Enzymatic saccharification of wheat straw for bioethanol production by a combined cellulase xylanase and feruloyl esterase treatment. Enzyme and Microbial Technology 2006, 39:897-902.
    • (2006) Enzyme and Microbial Technology , vol.39 , pp. 897-902
    • Tabka, M.G.1    Herpoël-Gimbert, I.2    Monod, F.3    Asther, M.4    Sigoillot, J.C.5
  • 166
    • 36849067496 scopus 로고    scopus 로고
    • Correlation between cellulose binding and activity of cellulose-binding domain mutants of Humicola grisea cellobiohydrolase 1
    • Takashima S., Ohno M., Hidaka M., Nakamura A., Masaki H., Uozumi T. Correlation between cellulose binding and activity of cellulose-binding domain mutants of Humicola grisea cellobiohydrolase 1. FEBS Letters 2007, 581:5891-5896.
    • (2007) FEBS Letters , vol.581 , pp. 5891-5896
    • Takashima, S.1    Ohno, M.2    Hidaka, M.3    Nakamura, A.4    Masaki, H.5    Uozumi, T.6
  • 167
    • 84856248919 scopus 로고    scopus 로고
    • Computational investigation of glycosylation effects on a family 1 carbohydrate-binding module
    • Taylor C.B., Talib M.F., McCabe C., Bu L., et al. Computational investigation of glycosylation effects on a family 1 carbohydrate-binding module. Journal of Biological Chemistry 2012, 287:3147-3155.
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 3147-3155
    • Taylor, C.B.1    Talib, M.F.2    McCabe, C.3    Bu, L.4
  • 168
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: New insight into the function of cellobiohydrolases
    • Teeri T.T. Crystalline cellulose degradation: New insight into the function of cellobiohydrolases. Trends in Biotechnology 1997, 15:160-167.
    • (1997) Trends in Biotechnology , vol.15 , pp. 160-167
    • Teeri, T.T.1
  • 169
    • 0028232933 scopus 로고
    • Enzyme-catalyzed hydrolysis and recycling in cellulose bioconversion
    • Tjerneld F. Enzyme-catalyzed hydrolysis and recycling in cellulose bioconversion. Methods in Enzymology 1994, 228:549-558.
    • (1994) Methods in Enzymology , vol.228 , pp. 549-558
    • Tjerneld, F.1
  • 170
    • 84899157294 scopus 로고    scopus 로고
    • Carbohydrate binding modules with reduced binding to lignin. Application no. WO/2011/097713. Publication date 18/08/2011.
    • Tomashek, J. J., Scott, B. R., & Kolczynski, D. (2011). Carbohydrate binding modules with reduced binding to lignin. Application no. WO/2011/097713. Publication date 18/08/2011.
    • (2011)
    • Tomashek, J.J.1    Scott, B.R.2    Kolczynski, D.3
  • 171
    • 0024277381 scopus 로고
    • Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis
    • Tomme P., van Tilbeurgh H., Pettersson G., van Damme J., Vandekerckhove J., Knowles J., et al. Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis. European Journal of Biochemistry 1988, 170:575-581.
    • (1988) European Journal of Biochemistry , vol.170 , pp. 575-581
    • Tomme, P.1    van Tilbeurgh, H.2    Pettersson, G.3    van Damme, J.4    Vandekerckhove, J.5    Knowles, J.6
  • 172
    • 34247226135 scopus 로고    scopus 로고
    • Evaluating the distribution of cellulases and the recycling of free cellulases during the hydrolysis of lignocellulosic substrates
    • Tu M., Chandra R.P., Saddler J.N. Evaluating the distribution of cellulases and the recycling of free cellulases during the hydrolysis of lignocellulosic substrates. Biotechnology Progress 2007, 23:398-406.
    • (2007) Biotechnology Progress , vol.23 , pp. 398-406
    • Tu, M.1    Chandra, R.P.2    Saddler, J.N.3
  • 173
    • 35348835366 scopus 로고    scopus 로고
    • Recycling cellulases during the hydrolysis of steam exploded and ethanol pretreated lodgepole pine
    • Tu M., Chandra R.P., Saddler J.N. Recycling cellulases during the hydrolysis of steam exploded and ethanol pretreated lodgepole pine. Biotechnology Progress 2007, 23:1130-1137.
    • (2007) Biotechnology Progress , vol.23 , pp. 1130-1137
    • Tu, M.1    Chandra, R.P.2    Saddler, J.N.3
  • 174
    • 69049087608 scopus 로고    scopus 로고
    • The potential of enzyme recycling during the hydrolysis of a mixed softwood feedstock
    • Tu M., Zhang X., Paice M., MacFarlane P., Saddler J.N. The potential of enzyme recycling during the hydrolysis of a mixed softwood feedstock. Bioresource Technology 2009, 100:6407-6415.
    • (2009) Bioresource Technology , vol.100 , pp. 6407-6415
    • Tu, M.1    Zhang, X.2    Paice, M.3    MacFarlane, P.4    Saddler, J.N.5
  • 175
    • 0025992531 scopus 로고
    • The 1,4-beta-D-glucan glucanohydrolases from Phanerochaete chrysosporium. Re-assessment of their significance in cellulose degradation mechanisms
    • Uzcategui E., Johansson G., Ek B., Pettersson G. The 1,4-beta-D-glucan glucanohydrolases from Phanerochaete chrysosporium. Re-assessment of their significance in cellulose degradation mechanisms. Journal of Biotechnology 1991, 21:143-160.
    • (1991) Journal of Biotechnology , vol.21 , pp. 143-160
    • Uzcategui, E.1    Johansson, G.2    Ek, B.3    Pettersson, G.4
  • 176
    • 77957727454 scopus 로고    scopus 로고
    • An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides
    • Vaaje-Kolstad G., Westereng B., Horn S.J., Liu Z., Zhai H., Sørlie M., et al. An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 2010, 330:219-222.
    • (2010) Science , vol.330 , pp. 219-222
    • Vaaje-Kolstad, G.1    Westereng, B.2    Horn, S.J.3    Liu, Z.4    Zhai, H.5    Sørlie, M.6
  • 179
    • 0000103970 scopus 로고
    • Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei-Separation of functional domains
    • van Tilbeurgh H., Tomme P., Claeyssens M., Bhikhabhai R., Pettersson G. Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei-Separation of functional domains. FEBS Letters 1986, 204:223-227.
    • (1986) FEBS Letters , vol.204 , pp. 223-227
    • van Tilbeurgh, H.1    Tomme, P.2    Claeyssens, M.3    Bhikhabhai, R.4    Pettersson, G.5
  • 181
    • 80052367273 scopus 로고    scopus 로고
    • Synergistic action of xylanase and mannanase improves the total hydrolysis of softwood
    • Várnai A., Huikko L., Pere J., Siika-aho M., Viikari L. Synergistic action of xylanase and mannanase improves the total hydrolysis of softwood. Bioresource Technology 2011, 102:9096-9104.
    • (2011) Bioresource Technology , vol.102 , pp. 9096-9104
    • Várnai, A.1    Huikko, L.2    Pere, J.3    Siika-aho, M.4    Viikari, L.5
  • 182
  • 183
    • 84874208200 scopus 로고    scopus 로고
    • Carbohydrate-binding modules (CBMs) revisited. Reduced amount of water counterbalances the need for CBMs
    • Várnai A., Siika-aho M., Viikari L. Carbohydrate-binding modules (CBMs) revisited. Reduced amount of water counterbalances the need for CBMs. Biotechnology for Biofuels 2013, 6:30.
    • (2013) Biotechnology for Biofuels , vol.6 , pp. 30
    • Várnai, A.1    Siika-aho, M.2    Viikari, L.3
  • 184
    • 78650714894 scopus 로고    scopus 로고
    • Adsorption of monocomponent enzymes in enzyme mixture analyzed quantitatively during hydrolysis of lignocellulose substrates
    • Várnai A., Viikari L., Marjamaa K., Siika-aho M. Adsorption of monocomponent enzymes in enzyme mixture analyzed quantitatively during hydrolysis of lignocellulose substrates. Bioresource Technology 2011, 102:1220-1227.
    • (2011) Bioresource Technology , vol.102 , pp. 1220-1227
    • Várnai, A.1    Viikari, L.2    Marjamaa, K.3    Siika-aho, M.4
  • 185
    • 0031566314 scopus 로고    scopus 로고
    • Substrate specificity of endoglucanases: What determines xyloglucanase activity?
    • Vincken J.-P., Beldman G., Voragen A.G.J. Substrate specificity of endoglucanases: What determines xyloglucanase activity?. Carbohydrate Research 1997, 298:299-310.
    • (1997) Carbohydrate Research , vol.298 , pp. 299-310
    • Vincken, J.-P.1    Beldman, G.2    Voragen, A.G.J.3
  • 186
    • 77951228328 scopus 로고    scopus 로고
    • Substrate specificity of family 5, 6, 7, 9, 12, and 45 endoglucanases
    • Vlasenko E., Schülein M., Cherry J., Xu F. Substrate specificity of family 5, 6, 7, 9, 12, and 45 endoglucanases. Bioresource Technology 2010, 101:2405-2411.
    • (2010) Bioresource Technology , vol.101 , pp. 2405-2411
    • Vlasenko, E.1    Schülein, M.2    Cherry, J.3    Xu, F.4
  • 187
    • 47349122440 scopus 로고    scopus 로고
    • A novel function for the cellulose binding module of cellobiohydrolase I
    • Wang L., Zhang Y., Gao P. A novel function for the cellulose binding module of cellobiohydrolase I. Science in China. Series B 2008, 51:620-629.
    • (2008) Science in China. Series B , vol.51 , pp. 620-629
    • Wang, L.1    Zhang, Y.2    Gao, P.3
  • 188
    • 84862801071 scopus 로고    scopus 로고
    • Kinetics of adsorption, desorption, and re-adsorption of a commercial endoglucanase in lignocellulosic suspensions
    • Wang Q.Q., Zhu J.Y., Hunt C.G., Zhan H.Y. Kinetics of adsorption, desorption, and re-adsorption of a commercial endoglucanase in lignocellulosic suspensions. Biotechnology and Bioengineering 2012, 109:1965-1975.
    • (2012) Biotechnology and Bioengineering , vol.109 , pp. 1965-1975
    • Wang, Q.Q.1    Zhu, J.Y.2    Hunt, C.G.3    Zhan, H.Y.4
  • 190
    • 38849122120 scopus 로고    scopus 로고
    • Spruce-derived mannans-A potential raw material for hydrocolloids and novel advanced natural materials
    • Willför S., Sundberg K., Tenkanen M., Holmbom B. Spruce-derived mannans-A potential raw material for hydrocolloids and novel advanced natural materials. Carbohydrate Polymers 2008, 72:197-210.
    • (2008) Carbohydrate Polymers , vol.72 , pp. 197-210
    • Willför, S.1    Sundberg, K.2    Tenkanen, M.3    Holmbom, B.4
  • 192
    • 0026547982 scopus 로고
    • The anaerobic fungus Neocallimastix frontalis: Isolation and properties of a cellulosome-type enzyme fraction with the capacity to solubilize hydrogen-bond-ordered cellulose
    • Wilson C.A., Wood T.M. The anaerobic fungus Neocallimastix frontalis: Isolation and properties of a cellulosome-type enzyme fraction with the capacity to solubilize hydrogen-bond-ordered cellulose. Applied Microbiology and Biotechnology 1992, 37:125-129.
    • (1992) Applied Microbiology and Biotechnology , vol.37 , pp. 125-129
    • Wilson, C.A.1    Wood, T.M.2
  • 193
    • 0042443510 scopus 로고    scopus 로고
    • Techno-economic evaluation of producing ethanol from softwood: Comparison of SSF and SHF and identification of bottlenecks
    • Wingren A., Galbe M., Zacchi G. Techno-economic evaluation of producing ethanol from softwood: Comparison of SSF and SHF and identification of bottlenecks. Biotechnology Progress 2003, 19:1109-1117.
    • (2003) Biotechnology Progress , vol.19 , pp. 1109-1117
    • Wingren, A.1    Galbe, M.2    Zacchi, G.3
  • 194
    • 0029128066 scopus 로고
    • Studies on the capacity of the cellulase of the anaerobic rumen fungus Piromonas communis P to degrade hydrogen bond-ordered cellulose
    • Wood T.M., Wilson C.A. Studies on the capacity of the cellulase of the anaerobic rumen fungus Piromonas communis P to degrade hydrogen bond-ordered cellulose. Applied Microbiology and Biotechnology 1995, 43:572-578.
    • (1995) Applied Microbiology and Biotechnology , vol.43 , pp. 572-578
    • Wood, T.M.1    Wilson, C.A.2
  • 195
    • 11244345992 scopus 로고    scopus 로고
    • Effects of sugar inhibition on cellulases and β-glucosidase during enzymatic hydrolysis of softwood substrates
    • Xiao Z., Zhang X., Gregg D.J., Saddler J.N. Effects of sugar inhibition on cellulases and β-glucosidase during enzymatic hydrolysis of softwood substrates. Applied Biochemistry and Biotechnology 2004, 113-116:1115-1126.
    • (2004) Applied Biochemistry and Biotechnology , pp. 1115-1126
    • Xiao, Z.1    Zhang, X.2    Gregg, D.J.3    Saddler, J.N.4
  • 197
    • 84879500789 scopus 로고    scopus 로고
    • Genes associated with lignin degradation in the polyphagous white-rot pathogen Heterobasidion irregulare show substrate-specific regulation
    • Yakovlev I.A., Hietala A.M., Courty P.-E., Lundell T., Solheim H., Fossdal C.G. Genes associated with lignin degradation in the polyphagous white-rot pathogen Heterobasidion irregulare show substrate-specific regulation. Fungal Genetics and Biology 2013, 56:17-24.
    • (2013) Fungal Genetics and Biology , vol.56 , pp. 17-24
    • Yakovlev, I.A.1    Hietala, A.M.2    Courty, P.-E.3    Lundell, T.4    Solheim, H.5    Fossdal, C.G.6
  • 198
    • 33745793410 scopus 로고    scopus 로고
    • BSA treatment to enhance enzymatic hydrolysis of cellulose in lignin containing substrates
    • Yang B., Wyman C.E. BSA treatment to enhance enzymatic hydrolysis of cellulose in lignin containing substrates. Biotechnology and Bioengineering 2006, 94:611-617.
    • (2006) Biotechnology and Bioengineering , vol.94 , pp. 611-617
    • Yang, B.1    Wyman, C.E.2
  • 199
    • 55849106319 scopus 로고    scopus 로고
    • Pretreatment: The key to unlocking low-cost cellulosic ethanol
    • Yang B., Wyman C.E. Pretreatment: The key to unlocking low-cost cellulosic ethanol. Biofuels, Bioproducts and Biorefineries 2008, 2:26-40.
    • (2008) Biofuels, Bioproducts and Biorefineries , vol.2 , pp. 26-40
    • Yang, B.1    Wyman, C.E.2
  • 200
    • 45849139328 scopus 로고    scopus 로고
    • Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola
    • Yoon J.J., Cha C.J., Kim Y.S., Kim W. Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola. Biotechnology Letters 2008, 30:1373-1378.
    • (2008) Biotechnology Letters , vol.30 , pp. 1373-1378
    • Yoon, J.J.1    Cha, C.J.2    Kim, Y.S.3    Kim, W.4
  • 201
    • 84860831446 scopus 로고    scopus 로고
    • Development of feedstocks for cellulosic biofuels
    • Available at:
    • Youngs H., Somerville C. Development of feedstocks for cellulosic biofuels. Biology Reports 2012, 4:10. Available at:. http://f1000.com/reports/b/4/10.
    • (2012) Biology Reports , vol.4 , pp. 10
    • Youngs, H.1    Somerville, C.2
  • 202
    • 10844286172 scopus 로고    scopus 로고
    • Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems
    • Zhang Y.H.P., Lynd L.R. Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems. Biotechnology and Bioengineering 2004, 88:797-824.
    • (2004) Biotechnology and Bioengineering , vol.88 , pp. 797-824
    • Zhang, Y.H.P.1    Lynd, L.R.2
  • 203
    • 83655183347 scopus 로고    scopus 로고
    • The role of acetyl xylan esterase in solubilisation of xylan and enzymatic hydrolysis of wheat straw and giant reed
    • Zhang J., Siika-aho M., Tenkanen M., Viikari L. The role of acetyl xylan esterase in solubilisation of xylan and enzymatic hydrolysis of wheat straw and giant reed. Biotechnology for Biofuels 2011, 4:60.
    • (2011) Biotechnology for Biofuels , vol.4 , pp. 60
    • Zhang, J.1    Siika-aho, M.2    Tenkanen, M.3    Viikari, L.4
  • 204
    • 84864406375 scopus 로고    scopus 로고
    • Xylans inhibit enzymatic hydrolysis of lignocellulosic materials by cellulases
    • Zhang J., Tang M., Viikari L. Xylans inhibit enzymatic hydrolysis of lignocellulosic materials by cellulases. Bioresource Technology 2012, 121:8-12.
    • (2012) Bioresource Technology , vol.121 , pp. 8-12
    • Zhang, J.1    Tang, M.2    Viikari, L.3
  • 205
    • 70349191386 scopus 로고    scopus 로고
    • Computational simulations of the Trichoderma reesei cellobiohydrolase I acting on microcrystalline cellulose Iβ: The enzyme-substrate complex
    • Zhong L., Matthews J.F., Hansen P.I., Crowley M.F., Cleary J.M., Walker R.C., et al. Computational simulations of the Trichoderma reesei cellobiohydrolase I acting on microcrystalline cellulose Iβ: The enzyme-substrate complex. Carbohydrate Research 2009, 344:1984-1992.
    • (2009) Carbohydrate Research , vol.344 , pp. 1984-1992
    • Zhong, L.1    Matthews, J.F.2    Hansen, P.I.3    Crowley, M.F.4    Cleary, J.M.5    Walker, R.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.