메뉴 건너뛰기




Volumn , Issue , 2007, Pages 35-50

Cellulases for biomass conversion

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84863205916     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/1-4020-5377-0_3     Document Type: Chapter
Times cited : (10)

References (72)
  • 1
    • 0001188346 scopus 로고
    • Structural and functional domains of cellobiohydrolase i from T. reesei - A small-angle x-ray-scattering study of the intact enzyme and its core
    • Abuja, P.M., Schmuck, M., Pilz, I., Tomme, P., Claeyssens, M. (1988a) Structural and functional domains of cellobiohydrolase I from T. reesei - a Small-Angle X-Ray-Scattering Study of the Intact Enzyme and Its Core. Eur. Biophys. J. 15, 339-342.
    • (1988) Eur. Biophys. J. , vol.15 , pp. 339-342
    • Abuja, P.M.1    Schmuck, M.2    Pilz, I.3    Tomme, P.4    Claeyssens, M.5
  • 2
    • 0024286212 scopus 로고
    • Domain structure of cellobiohydrolase II as studied by small angle X-ray scattering: Close resemblance to cellobiohydrolase i
    • Abuja, P.M., Pilz, I., Claeyssens, M. and Tomme, P. (1988b) Domain structure of cellobiohydrolase II as studied by small angle X-ray scattering: close resemblance to cellobiohydrolase I. Biochem. Biophys. Res. Commun. 156, 180-185.
    • (1988) Biochem. Biophys. Res. Commun. , vol.156 , pp. 180-185
    • Abuja, P.M.1    Pilz, I.2    Claeyssens, M.3    Tomme, P.4
  • 4
    • 0000407469 scopus 로고
    • Ueber einige sclerotinien und sclerotienkrankheiten
    • de Bary, A. (1886) Ueber einige sclerotinien und sclerotienkrankheiten. Bot. Zeit. XLIV: 377.
    • (1886) Bot. Zeit. , vol.44 , pp. 377
    • De Bary, A.1
  • 5
    • 0027984011 scopus 로고
    • The cellulosome - A treasure-trove for biotechnology
    • Bayer, E.A., Morag, E. and Lamed, R. (1994) The cellulosome - a treasure-trove for biotechnology. Trends in Biotechnology 12, 378-386.
    • (1994) Trends in Biotechnology , vol.12 , pp. 378-386
    • Bayer, E.A.1    Morag, E.2    Lamed, R.3
  • 6
    • 4243392868 scopus 로고    scopus 로고
    • Emerging phylogenetics of cellulosome structure
    • Gilbert, H.J., Davies, G, Henrissat, B., Svensson, B. (Eds), The Royal Society of Chemistry, Cambridge
    • Bayer, E.A., Ding, S.-Y., Mechaly, A., Shoham, Y. and Lamed, R. (1999) Emerging phylogenetics of cellulosome structure, In Recent Advances In Carbohydrate Bioengineering, Gilbert, H.J., Davies, G, Henrissat, B., Svensson, B. (Eds), The Royal Society of Chemistry, Cambridge, p. 189-201.
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 189-201
    • Bayer, E.A.1    Ding, S.-Y.2    Mechaly, A.3    Shoham, Y.4    Lamed, R.5
  • 7
    • 4143139469 scopus 로고    scopus 로고
    • The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides
    • Bayer, E.A., Belaich, J.P., Shoham, Y. and Lamed, R. (2004) The cellulosomes: multienzyme machines for degradation of plant cell wall polysaccharides. Annual Review of Microbiology 58, 521-554.
    • (2004) Annual Review of Microbiology , vol.58 , pp. 521-554
    • Bayer, E.A.1    Belaich, J.P.2    Shoham, Y.3    Lamed, R.4
  • 8
    • 0345701247 scopus 로고    scopus 로고
    • Structure and ligand binding of carbohydrate-binding module csCBM6-3 reveals similarities with fucose-specific lectins and "galactose- binding" domains
    • Boraston, A.B., Notenboom, V., Warren, R.A., Kilburn, D.G., Rose, D. R. and Davies, G. (2003) Structure and ligand binding of carbohydrate-binding module csCBM6-3 reveals similarities with fucose-specific lectins and "galactose-binding" domains. J. Mol. Biol. 327(3):659-669.
    • (2003) J. Mol. Biol. , vol.327 , Issue.3 , pp. 659-669
    • Boraston, A.B.1    Notenboom, V.2    Warren, R.A.3    Kilburn, D.G.4    Rose, D.R.5    Davies, G.6
  • 9
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • Boraston, A.B., Bolam, D.N., Gilbert, H.J. and Davies, G.J. (2004) Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem. J. 382, 769-781.
    • (2004) Biochem. J. , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 10
    • 0042794279 scopus 로고
    • Engineering aspects of the enzymatic conversion of waste cellulose to glucose
    • Brandt, D., Hontz, L. and Mandels, M. (1973) Engineering aspects of the enzymatic conversion of waste cellulose to glucose. AIChE Symposium Series 69, 127.
    • (1973) AIChE Symposium Series , vol.69 , pp. 127
    • Brandt, D.1    Hontz, L.2    Mandels, M.3
  • 11
    • 0000473844 scopus 로고
    • Researches on the germination of some of the Graminae
    • Brown, H.T., and Morris, G.H. (1890). Researches on the germination of some of the Graminae. J. Chem. Soc. Lond. 57, 458-528.
    • (1890) J. Chem. Soc. Lond. , vol.57 , pp. 458-528
    • Brown, H.T.1    Morris, G.H.2
  • 12
    • 0024402815 scopus 로고
    • Fungal Cellulase Systems: Comparison of the specificities of the cellobiohydrolases isolated from Penicillium pinophilum and Trichoderma reesei
    • Claeyssens, M., Tilbeurgh, H.V., Tomme, P., Wood, T.M. and McCrae, S. I. (1989) Fungal Cellulase Systems: Comparison of the specificities of the cellobiohydrolases isolated from Penicillium pinophilum and Trichoderma reesei. Biochem. J. 261, 819-826.
    • (1989) Biochem. J. , vol.261 , pp. 819-826
    • Claeyssens, M.1    Tilbeurgh, H.V.2    Tomme, P.3    Wood, T.M.4    McCrae, S.I.5
  • 13
    • 0011993364 scopus 로고
    • Kubicek, C. P., Eveleigh, D. E., Esterbauer, H., Steiner, W. and Kubicek-Pranz, E.M. (Eds.), London, the Royal Society of Chemistry
    • Claeyssens, M. and Tomme, P. (1990) In Kubicek, C. P., Eveleigh, D. E., Esterbauer, H., Steiner, W. and Kubicek-Pranz, E.M. (Eds.), Trichoderma reesei Cellulases: Biochemistry, Genetics, Physiology and Application, London, the Royal Society of Chemistry, pp. 1-11.
    • (1990) Trichoderma Reesei Cellulases: Biochemistry, Genetics, Physiology and Application , pp. 1-11
    • Claeyssens, M.1    Tomme, P.2
  • 14
    • 0345285388 scopus 로고
    • Cross-synergistic interactions between components of the cellulase systems of Talaromyces emersonii, Fusarium solani, Penicillium funiculosum, and Trichoderma koningii
    • Coughlan, M.P., Moloney, A.P., McCrae, S.I. and Wood, T.M. (1987) Cross-synergistic interactions between components of the cellulase systems of Talaromyces emersonii, Fusarium solani, Penicillium funiculosum, and Trichoderma koningii. Biochem. Soc. Transactions 15, 263-264.
    • (1987) Biochem. Soc. Transactions , vol.15 , pp. 263-264
    • Coughlan, M.P.1    Moloney, A.P.2    McCrae, S.I.3    Wood, T.M.4
  • 15
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • Gilbert, H.J., Davies, G., Henrissat, B. and B. Svensson (eds.), The Royal Society of Chemistry, Cambridge
    • Coutinho, P.M. and Henrissat, B. (1999) Carbohydrate-active enzymes: an integrated database approach. In Recent Advances in Carbohydrate Bioengineering, Gilbert, H.J., Davies, G., Henrissat, B. and B. Svensson (eds.), The Royal Society of Chemistry, Cambridge, pp. 3-12.
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 17
    • 0028774532 scopus 로고
    • Favoured structural motifs in globular proteins
    • Efimov, A.V. (1994) Favoured structural motifs in globular proteins. Structure 2, 999-1002.
    • (1994) Structure , vol.2 , pp. 999-1002
    • Efimov, A.V.1
  • 18
    • 0345285391 scopus 로고
    • Enzyme mechanisms involved in the degradation of wood components
    • Bailey, M., Enari T.M. and Linko, M. (Eds.), Helsinki, SITRA
    • Eriksson, K.E. (1975) Enzyme mechanisms involved in the degradation of wood components. In Bailey, M., Enari T.M. and Linko, M. (Eds.), Symposium on Enzymatic Hydrolysis of Cellulose. Helsinki, SITRA, p. 263.
    • (1975) Symposium on Enzymatic Hydrolysis of Cellulose , pp. 263
    • Eriksson, K.E.1
  • 20
    • 84954875039 scopus 로고
    • The 1,4-α-glucan cellobiohydrolases of T. reesei QM 9414. A new type of cellulolytic synergism
    • Fägerstam, L. G. and Pettersson, L. G. (1980) The 1,4-α-glucan cellobiohydrolases of T. reesei QM 9414. A new type of cellulolytic synergism. FEBS Lett. 119, 97.
    • (1980) FEBS Lett. , vol.119 , pp. 97
    • Fägerstam, L.G.1    Pettersson, L.G.2
  • 21
    • 0035877619 scopus 로고    scopus 로고
    • Design and production of active cellulosome chimeras: Selective incorporation of dockerincontaining enzymes into defined functional complexes
    • Fierobe, H.P., Mechaly, A., Tardif, C., Belaich, A., Lamed, R., Shoham, Y., Belaich, J.P. and Bayer, E.A. (2001) Design and production of active cellulosome chimeras: selective incorporation of dockerincontaining enzymes into defined functional complexes. J. Biol. Chem. 276, 21257-21261.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21257-21261
    • Fierobe, H.P.1    Mechaly, A.2    Tardif, C.3    Belaich, A.4    Lamed, R.5    Shoham, Y.6    Belaich, J.P.7    Bayer, E.A.8
  • 22
    • 0027517063 scopus 로고
    • Nucleotide-sequences of the celB gene encoding endo- 1,4-beta-glucanase- 2, Orf1 and Orf2 forming a putative cellulase gene-cluster of Clostridium josui
    • Fujino, T., Karita, S. and Ohmiya, K. (1993) Nucleotide-sequences of the celB gene encoding endo- 1,4-beta-glucanase-2, Orf1 and Orf2 forming a putative cellulase gene-cluster of Clostridium josui. J. Ferment. and Bioeng. 76(4):243-250.
    • (1993) J. Ferment. and Bioeng. , vol.76 , Issue.4 , pp. 243-250
    • Fujino, T.1    Karita, S.2    Ohmiya, K.3
  • 23
    • 0027285934 scopus 로고
    • Sequencing of a Clostridium thermocellum gene (cipA) encoding the cellulosomal S(L)-protein reveals an unusual degree of internal homology
    • Gerngross, U.T., Romaniec, M.P. M., Kobayashi, T., Huskisson, N.S. and Demain, A.L. (1993) Sequencing of a Clostridium thermocellum gene (cipA) encoding the cellulosomal S(L)-protein reveals an unusual degree of internal homology. Mol. Microbiol. 8(2):325-334.
    • (1993) Mol. Microbiol. , vol.8 , Issue.2 , pp. 325-334
    • Gerngross, U.T.1    Romaniec, M.P.M.2    Kobayashi, T.3    Huskisson, N.S.4    Demain, A.L.5
  • 24
    • 0003077412 scopus 로고
    • Evidence for multiple components in microbial cellulases
    • Gilligan, W. and Reese, E.T. (1954) Evidence for multiple components in microbial cellulases. Can. J. Microbiol. 1, 90.
    • (1954) Can. J. Microbiol. , vol.1 , pp. 90
    • Gilligan, W.1    Reese, E.T.2
  • 26
    • 0014705573 scopus 로고
    • The formation of short fibres from native cellulose by components of Trichoderma koningii cellulase
    • Halliwell, G. and Riaz, M. (1970) The formation of short fibres from native cellulose by components of Trichoderma koningii cellulase. Biochem. J. 116, 35-42.
    • (1970) Biochem. J. , vol.116 , pp. 35-42
    • Halliwell, G.1    Riaz, M.2
  • 27
    • 0028280706 scopus 로고
    • Four helix bundle diversity in globular proteins
    • Harris, N.L., Presnell, S.R. and Cohen, F.E. (1994) Four helix bundle diversity in globular proteins. J. Mol. Biol. 236, 1356-1368.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1356-1368
    • Harris, N.L.1    Presnell, S.R.2    Cohen, F.E.3
  • 28
    • 0027651651 scopus 로고
    • Activity studies of eight purified cellulases: Specificity, synergism, and binding domain effects
    • Irwin, D.C., Spezio, M., Walker, L.P. and Wilson, D.B. (1993) Activity studies of eight purified cellulases: specificity, synergism, and binding domain effects. Biotech. Bioeng. 42, 1002-1013.
    • (1993) Biotech. Bioeng. , vol.42 , pp. 1002-1013
    • Irwin, D.C.1    Spezio, M.2    Walker, L.P.3    Wilson, D.B.4
  • 30
    • 0036157410 scopus 로고    scopus 로고
    • Cell-surface-anchoring role of N-terminal surface layer homology domains of Clostridium cellulovorans enge
    • Kosugi, A., Murashima, K., Tamaru, Y. and Doi R.H. (2002) Cell-surface-anchoring role of N-terminal surface layer homology domains of Clostridium cellulovorans enge. J. Bacteriol. 184(4): 884-888.
    • (2002) J. Bacteriol. , vol.184 , Issue.4 , pp. 884-888
    • Kosugi, A.1    Murashima, K.2    Tamaru, Y.3    Doi, R.H.4
  • 31
    • 0024962351 scopus 로고
    • Determination of the three-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, J., Clore, G.M., Nilges, M., Jones, T.A., Pettersson, G., Knowles, J. and Gronenborn, A.M. (1989) Determination of the three-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 28, 7241-7257.
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 32
    • 0021016163 scopus 로고
    • Characterization of a cellulose-binding, cellulase-containing complex in Clostridium thermocellum
    • Lamed, R., Setter, E. and Bayer, E.A. (1983) Characterization of a cellulose-binding, cellulase-containing complex in Clostridium thermocellum. J. Bacteriol. 156, 828-836.
    • (1983) J. Bacteriol. , vol.156 , pp. 828-836
    • Lamed, R.1    Setter, E.2    Bayer, E.A.3
  • 33
    • 0003020155 scopus 로고
    • The cellulosome of Clostridium thermocellum
    • Lamed, R. and Bayer, E.A. (1988) The cellulosome of Clostridium thermocellum. Adv. Appl. Microbiol. 33, 1-46.
    • (1988) Adv. Appl. Microbiol. , vol.33 , pp. 1-46
    • Lamed, R.1    Bayer, E.A.2
  • 34
    • 0017309766 scopus 로고
    • Structural patterns in globular proteins
    • Levitt, M. and Chothia, C. (1976) Structural patterns in globular proteins. Nature 261, 552-557.
    • (1976) Nature , vol.261 , pp. 552-557
    • Levitt, M.1    Chothia, C.2
  • 35
    • 0013792042 scopus 로고
    • Individual roles of cellulase components derived from Trichoderma viride
    • Li, H., Flora, R.M. and King, K.W. (1965) Individual roles of cellulase components derived from Trichoderma viride. Arch. Biochem. Biophys. 111, 439-447.
    • (1965) Arch. Biochem. Biophys. , vol.111 , pp. 439-447
    • Li, H.1    Flora, R.M.2    King, K.W.3
  • 36
    • 0002516819 scopus 로고
    • Fungal cellulases and the microbial decomposition of cellulosic fabric
    • Mandels, M. and Reese E.T. (1964) Fungal cellulases and the microbial decomposition of cellulosic fabric. Develop. Indust. Microbiol. 5, 5-20.
    • (1964) Develop. Indust. Microbiol. , vol.5 , pp. 5-20
    • Mandels, M.1    Reese, E.T.2
  • 37
    • 0014984701 scopus 로고
    • Enhanced cellulase production by a mutant of Trichoderma viride
    • Mandels, M., Weber, J. and Parizek, R. (1971) Enhanced cellulase production by a mutant of Trichoderma viride. Appl. Microbiol. 21, 152.
    • (1971) Appl. Microbiol. , vol.21 , pp. 152
    • Mandels, M.1    Weber, J.2    Parizek, R.3
  • 38
    • 0019217567 scopus 로고
    • Synergistic hydrolysis of cellulose by components of the extracellular cellulase system of Talaromyces emersonii
    • McHale, A. and Coughlan, M.P. (1980) Synergistic hydrolysis of cellulose by components of the extracellular cellulase system of Talaromyces emersonii. FEBS Lett. 117, 319.
    • (1980) FEBS Lett. , vol.117 , pp. 319
    • McHale, A.1    Coughlan, M.P.2
  • 39
    • 0008509725 scopus 로고    scopus 로고
    • Cohesin-dockerin interaction in cellulosome assembly. A single hydroxyl group of a dockerin domain distinguishes between nonrecognition and high affinity recognition
    • Mechaly, A., Fierobe, H.P., Belaich, A., Belaich, J.P., Lamed, R., Shoham, Y. and Bayer, E.A. (2001) Cohesin-dockerin interaction in cellulosome assembly. A single hydroxyl group of a dockerin domain distinguishes between nonrecognition and high affinity recognition. J. Biol. Chem. 276(22):19678-19678.
    • (2001) J. Biol. Chem. , vol.276 , Issue.22 , pp. 19678-19678
    • Mechaly, A.1    Fierobe, H.P.2    Belaich, A.3    Belaich, J.P.4    Lamed, R.5    Shoham, Y.6    Bayer, E.A.7
  • 42
    • 0345285394 scopus 로고
    • The germination of some of the gramineae
    • Morris, B. (1890) The germination of some of the gramineae. J. Chem. Soc. Lond. 57, 497.
    • (1890) J. Chem. Soc. Lond. , vol.57 , pp. 497
    • Morris, B.1
  • 43
    • 0009597090 scopus 로고
    • Cellulose-enzymes
    • Newcombe, F.C. (1899) Cellulose-Enzymes. Annal. Bot. XIII, No. XLIX:49-81.
    • (1899) Annal. Bot. , vol.13 , Issue.44 , pp. 49-81
    • Newcombe, F.C.1
  • 44
    • 0035967536 scopus 로고    scopus 로고
    • Crystal structures of the family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10A in native and ligand-bound forms
    • Notenboom, V., Boraston, A.B., Kilburn, D.G. and Rose, D.R. (2001) Crystal structures of the family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10A in native and ligand-bound forms. Biochemistry 40(21):6248-6256.
    • (2001) Biochemistry , vol.40 , Issue.21 , pp. 6248-6256
    • Notenboom, V.1    Boraston, A.B.2    Kilburn, D.G.3    Rose, D.R.4
  • 45
    • 0027918137 scopus 로고
    • Alpha plus beta folds revisited: Some favoured motifs
    • Orengo, C.A. and Thornton, J.M. (1993) Alpha plus beta folds revisited: some favoured motifs. Structure 1, 105-120.
    • (1993) Structure , vol.1 , pp. 105-120
    • Orengo, C.A.1    Thornton, J.M.2
  • 46
    • 0028593509 scopus 로고
    • Protein superfamilles and domain superfolds
    • Orengo, C.A., Jones, D.T. and Thornton, J.M. (1994) Protein superfamilles and domain superfolds. Nature 372, 631-634.
    • (1994) Nature , vol.372 , pp. 631-634
    • Orengo, C.A.1    Jones, D.T.2    Thornton, J.M.3
  • 47
    • 0344422440 scopus 로고
    • The mechanism of enzymatic hydrolysis of cellulose
    • Bailey, M., Enari, T.M. and Linko, M. (eds), Helsinki, Finland, SITRA
    • Petterson, L. G. (1975) The mechanism of enzymatic hydrolysis of cellulose. In Bailey, M., Enari, T.M. and Linko, M. (eds), Symposium on Enzymatic Hydrolysis of Cellulose. Helsinki, Finland, SITRA, pp. 255.
    • (1975) Symposium on Enzymatic Hydrolysis of Cellulose , pp. 255
    • Petterson, L.G.1
  • 49
    • 76549243087 scopus 로고
    • The biological degradation of soluble cellulose derivatives and its relationship to the mechanism of cellulose hydrolysis
    • Reese, E.T., Siu, R.G.H. and Levinson, H.S. (1950) The biological degradation of soluble cellulose derivatives and its relationship to the mechanism of cellulose hydrolysis. J. Bacteriol. 59, 485.
    • (1950) J. Bacteriol. , vol.59 , pp. 485
    • Reese, E.T.1    Siu, R.G.H.2    Levinson, H.S.3
  • 51
    • 0035487187 scopus 로고    scopus 로고
    • Endb, A multidomain family 44 cellulase from Ruminococcus flavefaciens 17, binds to cellulose via a novel cellulose-binding module and to another R-flavefaciens protein via a dockerin domain
    • Rincon, M. T., McCrae, S.I., Kirby, J., Scott, K.P. and Flint, H.J. (2001) Endb, A multidomain family 44 cellulase from Ruminococcus flavefaciens 17, binds to cellulose via a novel cellulose-binding module and to another R-flavefaciens protein via a dockerin domain. Appl. Environ. Microbiol. 67(10): 4426-4431.
    • (2001) Appl. Environ. Microbiol. , vol.67 , Issue.10 , pp. 4426-4431
    • Rincon, M.T.1    McCrae, S.I.2    Kirby, J.3    Scott, K.P.4    Flint, H.J.5
  • 52
    • 0025182502 scopus 로고
    • Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei
    • Rouvinen, J., Bergfors, T., Teeri, T, Knowles, J. K. and Jones, T. A. (1990) Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. Science 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
  • 53
    • 0030759920 scopus 로고    scopus 로고
    • Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca
    • Sakon, J., Irwin, D., Wilson, D.B. and Karplus, A. (1997) Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca. Nature Struct. Biol. 4(10):810-818.
    • (1997) Nature Struct. Biol. , vol.4 , Issue.10 , pp. 810-818
    • Sakon, J.1    Irwin, D.2    Wilson, D.B.3    Karplus, A.4
  • 54
    • 0026772722 scopus 로고
    • Involvement of separate domains of the cellulosomal protein-S1 of Clostridium thermocellum in binding to cellulose and in anchoring of catalytic subunits to the cellulosome
    • Salamitou, S., Tokatlidis, K., Beguin, P. and Aubert J.P. (1992) Involvement of separate domains of the cellulosomal protein-S1 of Clostridium thermocellum in binding to cellulose and in anchoring of catalytic subunits to the cellulosome. Febs Letters 304(1):89-92.
    • (1992) Febs Letters , vol.304 , Issue.1 , pp. 89-92
    • Salamitou, S.1    Tokatlidis, K.2    Beguin, P.3    Aubert, J.P.4
  • 55
    • 84892217471 scopus 로고
    • The purification and properties of the C1-component of the cellulase complex
    • Hajny, G. J. and Reese, E. T. (eds)
    • Selby, K. (1969) The purification and properties of the C1-component of the cellulase complex. In Hajny, G. J. and Reese, E. T. (eds), Cellulases and Their Applications. Advances in Chemistry Series 95, 34-50.
    • (1969) Cellulases and Their Applications. Advances in Chemistry Series , vol.95 , pp. 34-50
    • Selby, K.1
  • 56
    • 0027932706 scopus 로고
    • Thermodynamics of ligand binding to the starch-binding domain of glucoamylase from Aspergillus niger
    • Sigurskjold, B.W., Svensson, G.B. and Driguez, H (1994) Thermodynamics of ligand binding to the starch-binding domain of glucoamylase from Aspergillus niger. Eur. J. Biochem. 225(1):133-41.
    • (1994) Eur. J. Biochem. , vol.225 , Issue.1 , pp. 133-141
    • Sigurskjold, B.W.1    Svensson, G.B.2    Driguez, H.3
  • 57
    • 0034731387 scopus 로고    scopus 로고
    • The structural basis for the ligand specificity of family 2 carbohydrate-binding modules
    • Simpson, P.J., Xie, H.-F., Bolam, D.N., Gilbert, H.J. and Williamson, M.P. (2000) The structural basis for the ligand specificity of family 2 carbohydrate-binding modules. J. Biol. Chem. 275(52):41137-42.
    • (2000) J. Biol. Chem. , vol.275 , Issue.52 , pp. 41137-41142
    • Simpson, P.J.1    Xie, H.-F.2    Bolam, D.N.3    Gilbert, H.J.4    Williamson, M.P.5
  • 58
    • 0026529913 scopus 로고
    • Primary sequence-analysis of Clostridium cellulovorans cellulose binding protein-A
    • Shoseyov, O., Takagi, M., Goldstein, M.A. and Doi, R.H. (1992) Primary sequence-analysis of Clostridium cellulovorans cellulose binding protein-A. Proc. Nat. Acad. Sci. USA 89(8):3483-3487.
    • (1992) Proc. Nat. Acad. Sci. USA , vol.89 , Issue.8 , pp. 3483-3487
    • Shoseyov, O.1    Takagi, M.2    Goldstein, M.A.3    Doi, R.H.4
  • 59
    • 0030604713 scopus 로고    scopus 로고
    • Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy
    • Sorimachi, K., Jacks, A.J., Le Gal-Coeffect, M.-F., Williamson, G., Archer, D.B. and Willamson, M.P. (1996) Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 259(5):970-87.
    • (1996) J. Mol. Biol. , vol.259 , Issue.5 , pp. 970-987
    • Sorimachi, K.1    Jacks, A.J.2    Le Gal-Coeffect, M.-F.3    Williamson, G.4    Archer, D.B.5    Willamson, M.P.6
  • 60
    • 0031570348 scopus 로고    scopus 로고
    • Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin
    • Sorimachi, K., Le Gal-Coeffect, M. F., Williamson, G., Archer, D.B. and Williamson M.P. (1997) Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin. Structure 5(5):647-61.
    • (1997) Structure , vol.5 , Issue.5 , pp. 647-661
    • Sorimachi, K.1    Le Gal-Coeffect, M.F.2    Williamson, G.3    Archer, D.B.4    Williamson, M.P.5
  • 63
    • 0014601940 scopus 로고
    • The cellulase of Fusarium solani, resolution of the enzyme complex
    • Wood, T.M. (1969) The cellulase of Fusarium solani, resolution of the enzyme complex. Biochem. J. 115, 457.
    • (1969) Biochem. J. , vol.115 , pp. 457
    • Wood, T.M.1
  • 64
    • 0344887351 scopus 로고
    • Cellulase of Trichoderma koningii
    • Wood, T.M. (1988) Cellulase of Trichoderma koningii. Methods Enzymol. 160, 221-234.
    • (1988) Methods Enzymol. , vol.160 , pp. 221-234
    • Wood, T.M.1
  • 65
    • 0017519909 scopus 로고
    • Cellulase from Fusarium solani purification and properties of the C-1 component
    • Wood, T.M. and McCrae, S.I. (1977) Cellulase from Fusarium solani purification and properties of the C-1 component. Carbohydr. Res. 57, 117-133.
    • (1977) Carbohydr. Res. , vol.57 , pp. 117-133
    • Wood, T.M.1    McCrae, S.I.2
  • 68
    • 0009639701 scopus 로고    scopus 로고
    • Conversion of Hardwood Biomass to Ethanol Via Dilute Acid Cocurrent Prehydrolysis and Enzymatic SSCF - Process Design and Economics
    • 6-04 Fort Collins, CO, May 2-6
    • Wooley R. and Ruth M. (1999) Conversion Of Hardwood Biomass To Ethanol Via Dilute Acid Cocurrent Prehydrolysis And Enzymatic SSCF - Process Design And Economics: Proceedings for the 21st Symposium on Biotechnology for Fuels and Chemicals, 6-04 Fort Collins, CO, May 2-6.
    • (1999) Proceedings for the 21st Symposium on Biotechnology for Fuels and Chemicals
    • Wooley, R.1    Ruth, M.2
  • 71
    • 1142298547 scopus 로고    scopus 로고
    • Architecture of the Bacteroides cellulosolvens cellulosome: Description of a cell surface-anchoring scaffoldin and a family 48 cellulase
    • Xu, Q., Bayer, E.A., Goldman, M., Kenig, R., Shoham, Y. and Lamed, R. (2004a) Architecture of the Bacteroides cellulosolvens cellulosome: description of a cell surface-anchoring scaffoldin and a family 48 cellulase. J. Bacteriol. 186, 968-977.
    • (2004) J. Bacteriol. , vol.186 , pp. 968-977
    • Xu, Q.1    Bayer, E.A.2    Goldman, M.3    Kenig, R.4    Shoham, Y.5    Lamed, R.6
  • 72
    • 4344636766 scopus 로고    scopus 로고
    • A novel Acetivibrio cellulolyticus anchoring scaffoldin that bears divergent cohesins
    • Xu, Q., Barak, Y., Kenig, R., Shoham, Y., Bayer, E.A. and Lamed, R. (2004b) A novel Acetivibrio cellulolyticus anchoring scaffoldin that bears divergent cohesins. J. Bacteriol. 186, 5782-5789.
    • (2004) J. Bacteriol. , vol.186 , pp. 5782-5789
    • Xu, Q.1    Barak, Y.2    Kenig, R.3    Shoham, Y.4    Bayer, E.A.5    Lamed, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.