메뉴 건너뛰기




Volumn 79, Issue 14, 2013, Pages 4220-4229

Insights into exo- and endoglucanase activities of family 6 glycoside hydrolases from Podospora anserina

Author keywords

[No Author keywords available]

Indexed keywords

AMORPHOUS CELLULOSE; BIOMASS DEGRADATIONS; CARBOXYMETHYLCELLULOSE; CATALYTIC EFFICIENCIES; GLYCOSIDE HYDROLASES; HYDROXYETHYL CELLULOSE; STRUCTURAL MODELING; TRICHODERMA REESEI;

EID: 84879805279     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00327-13     Document Type: Article
Times cited : (46)

References (61)
  • 1
    • 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 KM, Siika-Aho M, Teeri TT, Kirk TK. 1996. The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size. Appl. Environ. Microbiol. 62:2883-2887.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2883-2887
    • Kleman-leyer, K.M.1    Siika-aho, M.2    Teeri, T.T.3    Kirk, T.K.4
  • 2
    • 0028353231 scopus 로고
    • Cellulose hydrolysis by the cellulases from Trichoderma reesei: a new model for synergistic interaction.
    • Nidetzky B, Steiner W, Hayn M, Claeyssens M. 1994. Cellulose hydrolysis by the cellulases from Trichoderma reesei: a new model for synergistic interaction. Biochem. J. 298(Part 3):705-710.
    • (1994) Biochem. J. , vol.298 , Issue.3 , pp. 705-710
    • Nidetzky, B.1    Steiner, W.2    Hayn, M.3    Claeyssens, M.4
  • 3
    • 0033485705 scopus 로고    scopus 로고
    • Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I.
    • Valjamae P, Sild V, Nutt A, Pettersson G, Johansson G. 1999. Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I. Eur. J. Biochem. 266:327-334.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 327-334
    • Valjamae, P.1    Sild, V.2    Nutt, A.3    Pettersson, G.4    Johansson, G.5
  • 4
    • 84966185447 scopus 로고
    • Synergism of cellulases from Trichoderma reesei in the degradation of cellulose.
    • Henrissat B, Driguez H, Viet C, Schülein M. 1985. Synergism of cellulases from Trichoderma reesei in the degradation of cellulose. Biotechnology 3:722-726.
    • (1985) Biotechnology , vol.3 , pp. 722-726
    • Henrissat, B.1    Driguez, H.2    Viet, C.3    Schülein, M.4
  • 9
    • 0025182502 scopus 로고
    • Threedimensional structure of cellobiohydrolase II from Trichoderma reesei.
    • Rouvinen J, Bergfors T, Teeri T, Knowles JKC, Jones TA. 1990. Threedimensional 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.C.4    Jones, T.A.5
  • 12
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics.
    • doi:10.1093/nar/gkn663.
    • Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B. 2009. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res. 37:D233-D238. doi:10.1093/nar/gkn663.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 233-238
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5    Henrissat, B.6
  • 13
    • 9744263969 scopus 로고    scopus 로고
    • Three-dimensional structure of a thermostable native cellobiohydrolase, CBHIB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii.
    • Grassick A, Murray PG, Thompson R, Collins CM, Byrnes L, Birrane G, Higgins TM, Tuohy MG. 2004. Three-dimensional structure of a thermostable native cellobiohydrolase, CBHIB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii. Eur. J. Biochem. 271:4495-4506.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 4495-4506
    • Grassick, A.1    Murray, P.G.2    Thompson, R.3    Collins, C.M.4    Byrnes, L.5    Birrane, G.6    Higgins, T.M.7    Tuohy, M.G.8
  • 14
    • 0035861979 scopus 로고    scopus 로고
    • Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 Å resolution and homology models of the isozymes.
    • Munoz IG, Ubhayasekera W, Henriksson H, Szabo I, Pettersson G, Johansson G, Mowbray SL, Stahlberg J. 2001. Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 Å resolution and homology models of the isozymes. J. Mol. Biol. 314:1097-1111.
    • (2001) J. Mol. Biol. , vol.314 , pp. 1097-1111
    • Munoz, I.G.1    Ubhayasekera, W.2    Henriksson, H.3    Szabo, I.4    Pettersson, G.5    Johansson, G.6    Mowbray, S.L.7    Stahlberg, J.8
  • 15
    • 48249145161 scopus 로고    scopus 로고
    • Crystal structures of Melanocarpus albomyces cellobiohydrolase Ce17B in complex with cello-oligomers show high flexibility in the substrate binding.
    • Parkkinen T, Koivula A, Vehmaanpera J, Rouvinen J. 2008. Crystal structures of Melanocarpus albomyces cellobiohydrolase Ce17B in complex with cello-oligomers show high flexibility in the substrate binding. Protein Sci. 17:1383-1394.
    • (2008) Protein Sci. , vol.17 , pp. 1383-1394
    • Parkkinen, T.1    Koivula, A.2    Vehmaanpera, J.3    Rouvinen, J.4
  • 16
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: new insight into the function of cellobiohydrolases.
    • Teeri TT. 1997. Crystalline cellulose degradation: new insight into the function of cellobiohydrolases. Trends Biotechnol. 15:160-167.
    • (1997) Trends Biotechnol. , vol.15 , pp. 160-167
    • Teeri, T.T.1
  • 19
    • 10844286172 scopus 로고    scopus 로고
    • Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems.
    • Zhang YH, Lynd LR. 2004. Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems. Biotechnol. Bioeng. 88:797-824.
    • (2004) Biotechnol. Bioeng. , vol.88 , pp. 797-824
    • Zhang, Y.H.1    Lynd, L.R.2
  • 20
    • 0018980751 scopus 로고
    • Stability of the cellulase of Trichoderma reesei under use conditions.
    • Reese ET, Mandels M. 1980. Stability of the cellulase of Trichoderma reesei under use conditions. Biotechnol. Bioeng. 22:323-335.
    • (1980) Biotechnol. Bioeng. , vol.22 , pp. 323-335
    • Reese, E.T.1    Mandels, M.2
  • 22
    • 37149003390 scopus 로고    scopus 로고
    • Evaluation of minimal Trichoderma reesei cellulase mixtures on differently pretreated barley straw substrates.
    • Rosgaard L, Pedersen S, Langston J, Akerhielm D, Cherry JR, Meyer AS. 2007. Evaluation of minimal Trichoderma reesei cellulase mixtures on differently pretreated barley straw substrates. Biotechnol. Prog. 23:1270- 1276.
    • (2007) Biotechnol. Prog. , vol.23 , pp. 1270-1276
    • Rosgaard, L.1    Pedersen, S.2    Langston, J.3    Akerhielm, D.4    Cherry, J.R.5    Meyer, A.S.6
  • 23
    • 0027131591 scopus 로고
    • High frequency one-step gene replacement in Trichoderma reesei. II. Effects of deletions of individual cellulase genes.
    • Suominen PL, Mantyla AL, Karhunen T, Hakola S, Nevalainen H. 1993. High frequency one-step gene replacement in Trichoderma reesei. II. Effects of deletions of individual cellulase genes. Mol. Gen. Genet. 241:523- 530.
    • (1993) Mol. Gen. Genet. , vol.241
    • Suominen, P.L.1    Mantyla, A.L.2    Karhunen, T.3    Hakola, S.4    Nevalainen, H.5
  • 24
    • 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, Schulein M, Henrissat B, Chanzy H. 2000. 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. Appl. Environ. Microbiol. 66:1444-1452.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1444-1452
    • Boisset, C.1    Fraschini, C.2    Schulein, M.3    Henrissat, B.4    Chanzy, H.5
  • 25
    • 0034657160 scopus 로고    scopus 로고
    • Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 Å resolution.
    • Davies GJ, Brzozowski AM, Dauter M, Varrot A, Schulein M. 2000. Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 Å resolution. Biochem. J. 348:201-207.
    • (2000) Biochem. J. , vol.348 , pp. 201-207
    • Davies, G.J.1    Brzozowski, A.M.2    Dauter, M.3    Varrot, A.4    Schulein, M.5
  • 26
    • 0038396111 scopus 로고    scopus 로고
    • Enzymatic properties of cellulases from Humicola insolens.
    • Schulein M. 1997. Enzymatic properties of cellulases from Humicola insolens. J. Biotechnol. 57:71-81.
    • (1997) J. Biotechnol. , vol.57 , pp. 71-81
    • Schulein, M.1
  • 27
    • 79251613225 scopus 로고    scopus 로고
    • Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass.
    • Couturier M, Haon M, Coutinho PM, Henrissat B, Lesage-Meessen L, Berrin JG. 2011. Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass. Appl. Environ. Microbiol. 77:237-246.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 237-246
    • Couturier, M.1    Haon, M.2    Coutinho, P.M.3    Henrissat, B.4    Lesage-meessen, L.5    Berrin, J.G.6
  • 28
    • 77955506096 scopus 로고    scopus 로고
    • Automated assay for screening the enzymatic release of reducing sugars from micronized biomass.
    • doi:10 .1186/1475-2859-9-58.
    • Navarro D, Couturier M, da Silva GGD, Berrin JG, Rouau X, Asther M, Bignon C. 2010. Automated assay for screening the enzymatic release of reducing sugars from micronized biomass. Microb. Cell Fact. 9:58. doi:10 .1186/1475-2859-9-58.
    • (2010) Microb. Cell Fact. , vol.9 , pp. 58
    • Navarro, D.1    Couturier, M.2    da Silva, G.G.D.3    Berrin, J.G.4    Rouau, X.5    Asther, M.6    Bignon, C.7
  • 29
    • 79954997148 scopus 로고    scopus 로고
    • Effect of pretreatment and enzymatic hydrolysis of wheat straw on cell wall composition, hydrophobicity and cellulase adsorption.
    • Heiss-Blanquet S, Zheng D, Ferreira NL, Lapierre C, Baumberger S. 2011. Effect of pretreatment and enzymatic hydrolysis of wheat straw on cell wall composition, hydrophobicity and cellulase adsorption. Bioresour. Technol. 102:5938-5946.
    • (2011) Bioresour. Technol. , vol.102 , pp. 5938-5946
    • Heiss-blanquet, S.1    Zheng, D.2    Ferreira, N.L.3    Lapierre, C.4    Baumberger, S.5
  • 30
    • 70350493135 scopus 로고    scopus 로고
    • Processivity, synergism, and substrate specificity of Thermobifida fusca Cel6B.
    • Vuong TV, Wilson DB. 2009. Processivity, synergism, and substrate specificity of Thermobifida fusca Cel6B. Appl. Environ. Microbiol. 75: 6655-6661.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 6655-6661
    • Vuong, T.V.1    Wilson, D.B.2
  • 32
    • 76549203762 scopus 로고
    • A submicrodetermination of glucose.
    • Park JT, Johnson MJ. 1949. A submicrodetermination of glucose. J. Biol. Chem. 181:149-151.
    • (1949) J. Biol. Chem. , vol.181 , pp. 149-151
    • Park, J.T.1    Johnson, M.J.2
  • 33
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server.
    • Kelley LA, Sternberg MJE. 2009. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4:363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 35
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugarbinding subsites in glycosyl hydrolases.
    • Davies GJ, Wilson KS, Henrissat B. 1997. Nomenclature for sugarbinding subsites in glycosyl hydrolases. Biochem. J. 321:557-559.
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 37
    • 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. 1998. Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei: adsorption, sugar production pattern, and synergism of the enzymes. Biotechnol. Bioeng. 59:621-634.
    • (1998) Biotechnol. Bioeng. , vol.59 , pp. 621-634
    • Medve, J.1    Karlsson, J.2    Lee, D.3    Tjerneld, F.4
  • 38
    • 0033556286 scopus 로고    scopus 로고
    • Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 Å resolution.
    • Varrot A, Hastrup S, Schulein M, Davies GJ. 1999. Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 Å resolution. Biochem. J. 337:297-304.
    • (1999) Biochem. J. , vol.337 , pp. 297-304
    • Varrot, A.1    Hastrup, S.2    Schulein, M.3    Davies, G.J.4
  • 39
    • 84871874790 scopus 로고    scopus 로고
    • Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina.
    • Bey M, Zhou S, Poidevin L, Henrissat B, Coutinho PM, Berrin JG, Sigoillot JC. 2013. Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina. Appl. Environ. Microbiol. 79:488-496.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 488-496
    • Bey, M.1    Zhou, S.2    Poidevin, L.3    Henrissat, B.4    Coutinho, P.M.5    Berrin, J.G.6    Sigoillot, J.C.7
  • 40
    • 33746614259 scopus 로고    scopus 로고
    • Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls.
    • Bauer S, Vasu P, Persson S, Mort AJ, Somerville CR. 2006. Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls. Proc. Natl. Acad. Sci. U. S. A. 103:11417-11422.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 11417-11422
    • Bauer, S.1    Vasu, P.2    Persson, S.3    Mort, A.J.4    Somerville, C.R.5
  • 41
    • 33846392320 scopus 로고    scopus 로고
    • Cloning, functional expres- sion and characterization of Aspergillus sulphureus beta-mannanase in Pichia pastoris.
    • Chen X, Cao Y, Ding Y, Lu W, Li D. 2007. Cloning, functional expres- sion and characterization of Aspergillus sulphureus beta-mannanase in Pichia pastoris. J. Biotechnol. 128:452-461.
    • (2007) J. Biotechnol. , vol.128 , pp. 452-461
    • Chen, X.1    Cao, Y.2    Ding, Y.3    Lu, W.4    Li, D.5
  • 42
    • 67649631523 scopus 로고    scopus 로고
    • Expression of endo-1,4-beta-xylanase from Trichoderma reesei in Pichia pastoris and functional characterization of the produced enzyme.
    • doi:10.1186/1472-6750-9-56.
    • He J, Yu B, Zhang KY, Ding XM, Chen DW. 2009. Expression of endo-1,4-beta-xylanase from Trichoderma reesei in Pichia pastoris and functional characterization of the produced enzyme. BMC Biotechnol. 9:56. doi:10.1186/1472-6750-9-56.
    • (2009) BMC Biotechnol. , vol.9 , pp. 56
    • He, J.1    Yu, B.2    Zhang, K.Y.3    Ding, X.M.4    Chen, D.W.5
  • 43
    • 84859511736 scopus 로고    scopus 로고
    • From in silico to in vitro: modelling and production of Trichoderma reesei endoglucanase 1 and its mutant in Pichia pastoris.
    • Akcapinar GB, Gul O, Sezerman UO. 2012. From in silico to in vitro: modelling and production of Trichoderma reesei endoglucanase 1 and its mutant in Pichia pastoris. J. Biotechnol. 159:61-68.
    • (2012) J. Biotechnol. , vol.159 , pp. 61-68
    • Akcapinar, G.B.1    Gul, O.2    Sezerman, U.O.3
  • 44
    • 84455173789 scopus 로고    scopus 로고
    • Heterologous expression of Pycnoporus cinnabarinus cellobiose dehydrogenase in Pichia pastoris and involvement in saccharification processes.
    • doi:10.1186/1475-2859-10-113.
    • Bey M, Berrin JG, Poidevin L, Sigoillot JC. 2011. Heterologous expression of Pycnoporus cinnabarinus cellobiose dehydrogenase in Pichia pastoris and involvement in saccharification processes. Microb. Cell Fact. 10: 113. doi:10.1186/1475-2859-10-113.
    • (2011) Microb. Cell Fact. , vol.10 , pp. 113
    • Bey, M.1    Berrin, J.G.2    Poidevin, L.3    Sigoillot, J.C.4
  • 45
    • 0034609290 scopus 로고    scopus 로고
    • Characterization of Trichoderma reesei cellobiohydrolase CeI7A secreted from Pichia pastoris using two different promoters.
    • Boer H, Teeri TT, Koivula A. 2000. Characterization of Trichoderma reesei cellobiohydrolase CeI7A secreted from Pichia pastoris using two different promoters. Biotechnol. Bioeng. 69:486-494.
    • (2000) Biotechnol. Bioeng. , vol.69 , pp. 486-494
    • Boer, H.1    Teeri, T.T.2    Koivula, A.3
  • 46
    • 84879812605 scopus 로고    scopus 로고
    • Comparison of the heterologous expression of Trichoderma reesei endoglucanase II and cellobiohydrolase II in the yeasts Pichia pastoris and Yarrowia lipolytica.
    • Boonvitthya N, Bozonnet S, Burapatana V, O'Donohue MJ, Chulalaksananukul W. 2013. Comparison of the heterologous expression of Trichoderma reesei endoglucanase II and cellobiohydrolase II in the yeasts Pichia pastoris and Yarrowia lipolytica. Mol. Biotechnol. 54:158-169.
    • (2013) Mol. Biotechnol. , vol.54 , pp. 158-169
    • Boonvitthya, N.1    Bozonnet, S.2    Burapatana, V.3    O'donohue, M.J.4    Chulalaksananukul, W.5
  • 49
    • 84857391934 scopus 로고    scopus 로고
    • Optimization of a synthetic mixture composed of major Trichoderma reesei enzymes for the hydrolysis of steam-exploded wheat straw.
    • doi:10.1186/1754-6834-5-9.
    • Billard H, Faraj A, Ferreira NL, Menir S, Heiss-Blanquet S. 2012. Optimization of a synthetic mixture composed of major Trichoderma reesei enzymes for the hydrolysis of steam-exploded wheat straw. Biotechnol. Biofuels 5:9. doi:10.1186/1754-6834-5-9.
    • (2012) Biotechnol. Biofuels , vol.5 , pp. 9
    • Billard, H.1    Faraj, A.2    Ferreira, N.L.3    Menir, S.4    Heiss-blanquet, S.5
  • 50
    • 0031918884 scopus 로고    scopus 로고
    • Efficient secretion of Trichoderma reesei cellobiohydrolase II in Schizosaccharomyces pombe and characterization of its products.
    • Okada H, Sekiya T, Yokoyama K, Tohda H, Kumagai H, Morikawa Y. 1998. Efficient secretion of Trichoderma reesei cellobiohydrolase II in Schizosaccharomyces pombe and characterization of its products. Appl. Microbiol. Biotechnol. 49:301-308.
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 301-308
    • Okada, H.1    Sekiya, T.2    Yokoyama, K.3    Tohda, H.4    Kumagai, H.5    Morikawa, Y.6
  • 52
    • 0023104178 scopus 로고
    • Detection and characterization of the specific and nonspecific endoglucanases of Trichoderma reesei- evidence demonstrating endoglucanase activity by cellobiohydrolase- II.
    • Kyriacou A, Mackenzie CR, Neufeld RJ. 1987. Detection and characterization of the specific and nonspecific endoglucanases of Trichoderma reesei- evidence demonstrating endoglucanase activity by cellobiohydrolase- II. Enzyme Microb. Technol. 9:25-32.
    • (1987) Enzyme Microb. Technol. , vol.9 , pp. 25-32
    • Kyriacou, A.1    Mackenzie, C.R.2    Neufeld, R.J.3
  • 53
    • 0027298768 scopus 로고
    • Trichoderma reesei has no true exo-cellulase-all intact and truncated cellulases produce new reducing end groups on cellulose.
    • Stahlberg J, Johansson G, Pettersson G. 1993. Trichoderma reesei has no true exo-cellulase-all intact and truncated cellulases produce new reducing end groups on cellulose. Biochim. Biophys. Acta 1157:107- 113.
    • (1993) Biochim. Biophys. Acta , vol.1157
    • Stahlberg, J.1    Johansson, G.2    Pettersson, G.3
  • 54
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases.
    • Henrissat B, Davies G. 1997. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7:637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 55
    • 0028765765 scopus 로고
    • Adsorption and synergism of cellobiohydrolase-I and cellobiohydrolase-II of Trichoderma reesei during hydrolysis of microcrystalline cellulose.
    • Medve J, Stahlberg J, Tjerneld F. 1994. Adsorption and synergism of cellobiohydrolase-I and cellobiohydrolase-II of Trichoderma reesei during hydrolysis of microcrystalline cellulose. Biotechnol. Bioeng. 44:1064- 1073.
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 1064-1073
    • Medve, J.1    Stahlberg, J.2    Tjerneld, F.3
  • 56
    • 0028021533 scopus 로고
    • The Cel3 gene of Agaricus bisporus codes for a modular cellulase and is transcriptionally regulated by the carbon source.
    • Chow CM, Yague E, Raguz S, Wood DA, Thurston CF. 1994. The Cel3 gene of Agaricus bisporus codes for a modular cellulase and is transcriptionally regulated by the carbon source. Appl. Environ. Microbiol. 60: 2779-2785.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2779-2785
    • Chow, C.M.1    Yague, E.2    Raguz, S.3    Wood, D.A.4    Thurston, C.F.5
  • 57
    • 69949099255 scopus 로고    scopus 로고
    • Processive endoglucanases mediate degradation of cellulose by Saccharophagus degradans.
    • Watson BJ, Zhang HT, Longmire AG, Moon YH, Hutcheson SW. 2009. Processive endoglucanases mediate degradation of cellulose by Saccharophagus degradans. J. Bacteriol. 191:5697-5705.
    • (2009) J. Bacteriol. , vol.191 , pp. 5697-5705
    • Watson, B.J.1    Zhang, H.T.2    Longmire, A.G.3    Moon, Y.H.4    Hutcheson, S.W.5
  • 58
    • 0029896866 scopus 로고    scopus 로고
    • Characterization of CenC, an enzyme from Cellulomonas fimi with both endoand exoglucanase activities.
    • Tomme P, Kwan E, Gilkes NR, Kilburn DG, Warren RAJ. 1996. Characterization of CenC, an enzyme from Cellulomonas fimi with both endoand exoglucanase activities. J. Bacteriol. 178:4216-4223.
    • (1996) J. Bacteriol. , vol.178 , pp. 4216-4223
    • Tomme, P.1    Kwan, E.2    Gilkes, N.R.3    Kilburn, D.G.4    Warren, R.A.J.5
  • 59
    • 0032571552 scopus 로고    scopus 로고
    • A scheme for designating enzymes that hydrolyse the polysaccharides in the cell walls of plants.
    • Henrissat B, Teeri TT, Warren RA. 1998. A scheme for designating enzymes that hydrolyse the polysaccharides in the cell walls of plants. FEBS Lett. 425:352-354.
    • (1998) FEBS Lett. , vol.425 , pp. 352-354
    • Henrissat, B.1    Teeri, T.T.2    Warren, R.A.3
  • 60
    • 0033199581 scopus 로고    scopus 로고
    • Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Cel6A from Trichoderma reesei
    • Zou JY, Kleywegt GJ, Stahlberg J, Driguez H, Nerinckx W, Claeyssens M, Koivula A, Teeri TT, Jones TA. 1999. Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Cel6A from Trichoderma reesei. Structure 7:1035-1045.
    • (1999) Structure , vol.7 , pp. 1035-1045
    • Zou, J.Y.1    Kleywegt, G.J.2    Stahlberg, J.3    Driguez, H.4    Nerinckx, W.5    Claeyssens, M.6    Koivula, A.7    Teeri, T.T.8    Jones, T.A.9
  • 61
    • 0031024813 scopus 로고    scopus 로고
    • A bifunctionalized fluorogenic tetrasaccharide as a substrate to study cellulases.
    • Armand S, Drouillard S, Schulein M, Henrissat B, Driguez H. 1997. A bifunctionalized fluorogenic tetrasaccharide as a substrate to study cellulases. J. Biol. Chem. 272:2709-2713.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2709-2713
    • Armand, S.1    Drouillard, S.2    Schulein, M.3    Henrissat, B.4    Driguez, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.