메뉴 건너뛰기




Volumn 21, Issue 8, 2011, Pages 808-817

Purification, and biochemical and biophysical characterization of cellobiohydrolase I from trichoderma harzianum IOC 3844

Author keywords

Catalytic core domain; Cellobiohydrolase i; Identification; Purification; Trichoderma harzianum 3844

Indexed keywords

4 NITROPHENYL BETA DEXTRO CELLOBIOSIDE; CELLOBIOHYDROLASE I; CELLULOSE; CELLULOSE 1,4 BETA CELLOBIOSIDASE; MICROCRYSTALLINE CELLULOSE; PAPAIN; SEPHADEX; TRYPTOPHAN; UNCLASSIFIED DRUG; WATER;

EID: 80052277424     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1010.10037     Document Type: Article
Times cited : (23)

References (58)
  • 1
    • 78649697569 scopus 로고    scopus 로고
    • Purification and characterization of a novel thermoactive cellulase from thermophilic actinomycetes isolated from soil sample of Egypt
    • Aboul-Enein, F. A., E. Serour, and T. Hussein. 2010. Purification and characterization of a novel thermoactive cellulase from thermophilic actinomycetes isolated from soil sample of Egypt. Int. J. Acad. Res. 2: 81-86.
    • (2010) Int. J. Acad. Res , vol.2 , pp. 81-86
    • Aboul-Enein, F.A.1    Serour, E.2    Hussein, T.3
  • 3
    • 77649287391 scopus 로고    scopus 로고
    • Access to cellulose limits the efficiency of enzymatic hydrolysis: The role of amorphogenesis
    • Arantes, V. and J. N. Saddler. 2010. Access to cellulose limits the efficiency of enzymatic hydrolysis: The role of amorphogenesis. Biotech. Biofuels 3: 1-11.
    • (2010) Biotech. Biofuels , vol.3 , pp. 1-11
    • Arantes, V.1    Saddler, J.N.2
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Bailey, S. 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50: 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr , vol.50 , pp. 760-763
    • Bailey, S.1
  • 5
    • 24944544681 scopus 로고    scopus 로고
    • Purification and characterization of cellulase from the wild-type and two improved mutants of Pseudomonas fluorescens
    • Bakare, M. K., I. O. Adewale, A. Ajayi, A. I. Okoh, and O. O. Shonukan. 2005. Purification and characterization of cellulase from the wild-type and two improved mutants of Pseudomonas fluorescens. African J. Biotechnol. 4: 898-904.
    • (2005) African J. Biotechnol , vol.4 , pp. 898-904
    • Bakare, M.K.1    Adewale, I.O.2    Ajayi, A.3    Okoh, A.I.4    Shonukan, O.O.5
  • 6
  • 8
    • 0034609290 scopus 로고    scopus 로고
    • Characterization of Trichoderma reesei cellobiohydrolase CeI7A secreted from Pichia pastoris using two different promoters
    • Boer, H., T. T. Teeri, and A. Koivula. 2000. Characterization of Trichoderma reesei cellobiohydrolase CeI7A secreted from Pichia pastoris using two different promoters. Biotech. Bioeng. 69: 486-494.
    • (2000) Biotech. Bioeng , vol.69 , pp. 486-494
    • Boer, H.1    Teeri, T.T.2    Koivula, A.3
  • 9
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. Rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0027351945 scopus 로고
    • Structural models of primary-cell walls in flowering plants: Consistency of molecular structure with the physical properties of the wall during growth
    • Carpita, N. C. and D. M. Gibeaut. 1993. Structural models of primary-cell walls in flowering plants: Consistency of molecular structure with the physical properties of the wall during growth. Plant J. 3: 1-30.
    • (1993) Plant J , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 12
    • 84858973274 scopus 로고    scopus 로고
    • High-yield endoglucanase production by Trichoderma harzianum IOC-3844 cultivated in pretreated sugarcane mill byproduct
    • doi:10.4061/2010/854526
    • Castro, A., M. C. Ferreira, J. Cd. Cruz, K. C. R. Pedro, D. F. Carvalho, S. G. F. Leite, and N. Pereira Jr. 2010. High-yield endoglucanase production by Trichoderma harzianum IOC-3844 cultivated in pretreated sugarcane mill byproduct. Enzyme Res. doi:10.4061/2010/854526.
    • (2010) Enzyme Res
    • Castro, A.1    Ferreira, M.C.2    Cd Cruz, J.3    Pedro, K.C.R.4    Carvalho, D.F.5    Leite, S.G.F.6    Pereira Jr., N.7
  • 15
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies, G. and B. Henrissat. 1995. Structures and mechanisms of glycosyl hydrolases. Structure 3: 853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 16
    • 0021426650 scopus 로고
    • An assay for selective determination of exo-1,4,-beta-glucanase in a mixture of cellulolytic enzymes
    • Deshpande, M. V., K. E. Eriksson, and L. G. Pettersson. 1984. An assay for selective determination of exo-1,4,-beta-glucanase in a mixture of cellulolytic enzymes. Anal. Biochem. 138: 481-487.
    • (1984) Anal. Biochem , vol.138 , pp. 481-487
    • Deshpande, M.V.1    Eriksson, K.E.2    Pettersson, L.G.3
  • 17
    • 0027968302 scopus 로고
    • The 3-dimensional crystal-structure of the catalytic core of cellobiohydrolase-I from Trichoderma reesei
    • Divne, C., J. Stahlberg, T. Reinikainen, L. Ruohonen, G. Petterson, J. K. C. Knowles, et al. 1994. The 3-dimensional crystal-structure of the catalytic core of cellobiohydrolase-I from Trichoderma reesei. Science 265: 524-528.
    • (1994) Science , vol.265 , pp. 524-528
    • Divne, C.1    Stahlberg, J.2    Reinikainen, T.3    Ruohonen, L.4    Petterson, G.5    Knowles, J.K.C.6
  • 18
    • 0345676498 scopus 로고    scopus 로고
    • High-resolution crystal structures reveal how a cellulose chain is bound in the 50 angstrom long tunnel of cellobiohydrolase I from Trichoderma reesei
    • Divne, C., J. Stahlberg, T. T. Teeri, and J. T. Alwyn. 1998. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 angstrom long tunnel of cellobiohydrolase I from Trichoderma reesei. J. Molec. Biol. 275: 309-325.
    • (1998) J. Molec. Biol , vol.275 , pp. 309-325
    • Divne, C.1    Stahlberg, J.2    Teeri, T.T.3    Alwyn, J.T.4
  • 19
    • 0034581178 scopus 로고    scopus 로고
    • Use of fluorescence spectroscopy as thermodynamics tool
    • Eftink, M. R. 2000. Use of fluorescence spectroscopy as thermodynamics tool. Energ. Biol. Macromolec. 323: 459-473.
    • (2000) Energ. Biol. Macromolec , vol.323 , pp. 459-473
    • Eftink, M.R.1
  • 20
    • 75649147383 scopus 로고    scopus 로고
    • The molecular weight of protein in solution can be determined for a single SAXS measurement on a relative scale
    • Fischer, H., M. Oliveira Neto, H. B. Napolitano, I. Polikarpov, and A. Craievich. 2010. The molecular weight of protein in solution can be determined for a single SAXS measurement on a relative scale. J. Appl. Crystallogr. 43: 101-109.
    • (2010) J. Appl. Crystallogr , vol.43 , pp. 101-109
    • Fischer, H.1    Oliveira Neto, M.2    Napolitano, H.B.3    Polikarpov, I.4    Craievich, A.5
  • 21
    • 0028214830 scopus 로고
    • Cellulose morphology and enzymatic reactivity: A modified solute exclusion technique
    • Gama, F. M., J. A. Teixeira, and M. Mota. 1994. Cellulose morphology and enzymatic reactivity: A modified solute exclusion technique. Biotechnol. Bioeng. 43: 381-387.
    • (1994) Biotechnol. Bioeng , vol.43 , pp. 381-387
    • Gama, F.M.1    Teixeira, J.A.2    Mota, M.3
  • 22
    • 9944253283 scopus 로고    scopus 로고
    • Purification, cloning and characterisation of two forms of thermostable and highly active cellobiohydrolase I (Cel7A) produced by the industrial strain of Chrysosporium lucknowense
    • Gusakov, A. V., A. P. Sinitsyn, T. N. Salanovich, F. E. Bukhtojarov, A. V. Markov, B. B. Ustinov, et al. 2005. Purification, cloning and characterisation of two forms of thermostable and highly active cellobiohydrolase I (Cel7A) produced by the industrial strain of Chrysosporium lucknowense. Enzyme Microbial Technol. 36: 57-69.
    • (2005) Enzyme Microbial Technol , vol.36 , pp. 57-69
    • Gusakov, A.V.1    Sinitsyn, A.P.2    Salanovich, T.N.3    Bukhtojarov, F.E.4    Markov, A.V.5    Ustinov, B.B.6
  • 24
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino-acid-sequence similarities
    • Henrissat, B. 1991. A classification of glycosyl hydrolases based on amino-acid-sequence similarities. Biochem. J. 280: 309-316.
    • (1991) Biochem. J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 25
    • 34249773227 scopus 로고
    • Cellulases and their interaction with cellulose
    • Henrissat, B. 1994. Cellulases and their interaction with cellulose. Cellulose 1: 169-196.
    • (1994) Cellulose , vol.1 , pp. 169-196
    • Henrissat, B.1
  • 26
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino-acid-sequence similarities
    • Henrissat, B. and A. Bairoch. 1993. New families in the classification of glycosyl hydrolases based on amino-acid-sequence similarities. Biochem. J. 293: 781-788.
    • (1993) Biochem. J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 28
    • 0027651651 scopus 로고
    • Activity studies of 8 purified cellulases: Specificity, synergism, and binding domain effects
    • Irwin, D. C., M. Spezio, L. P. Walker, D. B. Wilson. 1993. Activity studies of 8 purified cellulases: Specificity, synergism, and binding domain effects. Biotechnol. Bioeng. 42: 1002-1013.
    • (1993) Biotechnol. Bioeng , vol.42 , pp. 1002-1013
    • Irwin, D.C.1    Spezio, M.2    Walker, L.P.3    Wilson, D.B.4
  • 29
    • 77955645816 scopus 로고    scopus 로고
    • Practical screening of purified cellobiohydrolases and endoglucanases with alpha-cellulose and specification of hydrodynamics
    • Jager, G., Z. J. Wu, K. Garschhammer, P. Engel, T. Klement, R. Rinaldi, et al. 2010. Practical screening of purified cellobiohydrolases and endoglucanases with alpha-cellulose and specification of hydrodynamics. Biotechnol. Biofuels 3: 18.
    • (2010) Biotechnol. Biofuels , vol.3 , pp. 18
    • Jager, G.1    Wu, Z.J.2    Garschhammer, K.3    Engel, P.4    Klement, T.5    Rinaldi, R.6
  • 30
  • 31
    • 0024962351 scopus 로고
    • Determination of the 3-dimensional solutions structure of the C-terminal domain of cellobiohydrolase-I from Trichoderma reesei: A study using nuclear magnetic ressonance and hybrid distance geometry dynamical simulated annealing
    • Kraulis, P. J., G. M. Clore, M. Nilges, T. A. Jones, G. Pettersson, J. Knowles, and A. M. Gronenborn. 1989. Determination of the 3-dimensional solutions structure of the C-terminal domain of cellobiohydrolase-I from Trichoderma reesei: A study using nuclear magnetic ressonance and hybrid distance geometry dynamical simulated annealing. Biochemistry 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    Gronenborn, A.M.7
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structrural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structrural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-691.
    • (1970) Nature , vol.227 , pp. 680-691
    • Laemmli, U.K.1
  • 34
    • 0000010402 scopus 로고
    • Production of cellulases
    • Mandels, M. and J. Weber. 1969. Production of cellulases. Adv. Chem. Series 95: 391-398.
    • (1969) Adv. Chem. Series , vol.95 , pp. 391-398
    • Mandels, M.1    Weber, J.2
  • 35
    • 0033199811 scopus 로고    scopus 로고
    • Substrate and enzyme characteristics that limit cellulose hydrolysis
    • Mansfield, S. D., C. Mooney, and J. N. Saddler. 1999. Substrate and enzyme characteristics that limit cellulose hydrolysis. Biotechnol. Progress 15: 804-816.
    • (1999) Biotechnol. Progress , vol.15 , pp. 804-816
    • Mansfield, S.D.1    Mooney, C.2    Saddler, J.N.3
  • 37
    • 0035861979 scopus 로고    scopus 로고
    • Family 7 cellobiohydrolases from Phanerochaete chrysosporium: Crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 angstrom resolution and homology models of the isozymes
    • Munoz, I. G., W. Ubhayasekera, H. Henriksson, I. Szabo, G. Pettersson, G. Johansson, et al. 2001. Family 7 cellobiohydrolases from Phanerochaete chrysosporium: Crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 angstrom resolution and homology models of the isozymes. J. Molecul. Biol. 314: 1097-1111.
    • (2001) J. Molecul. 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
  • 38
    • 0031980657 scopus 로고    scopus 로고
    • Survey and analysis of commercial cellulase preparations suitable for biomass conversion to ethanol
    • Nieves, R. A., C. I. Ehrman, W. S. Adney, R. T. Elander, and M. E. Himmel. 1998. Survey and analysis of commercial cellulase preparations suitable for biomass conversion to ethanol. World J. Microbiol. Biotechnol. 14: 301-304.
    • (1998) World J. Microbiol. Biotechnol , vol.14 , pp. 301-304
    • Nieves, R.A.1    Ehrman, C.I.2    Adney, W.S.3    Elander, R.T.4    Himmel, M.E.5
  • 39
    • 17444397116 scopus 로고    scopus 로고
    • Porter: A new, accurate server for protein secondary structure prediction
    • Pollastri, G. and A. McLysaght. 2005. Porter: A new, accurate server for protein secondary structure prediction. Bioinformatics 21: 1719-1720.
    • (2005) Bioinformatics , vol.21 , pp. 1719-1720
    • Pollastri, G.1    McLysaght, A.2
  • 40
    • 33847270801 scopus 로고    scopus 로고
    • Ethanol as an alternative fuel from agricultural, industrial and urban residues
    • Prasad, S., A. Singh, and H. C. Joshi. 2007. Ethanol as an alternative fuel from agricultural, industrial and urban residues. Resour. Conserv. Recycl. 50: 1-39.
    • (2007) Resour. Conserv. Recycl , vol.50 , pp. 1-39
    • Prasad, S.1    Singh, A.2    Joshi, H.C.3
  • 41
    • 0034620514 scopus 로고    scopus 로고
    • Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A
    • Raghothama, S., P. J. Simpson, L. Szabo, T. Nagy, H. Gilbert, and M. P. Williamson. 2000. Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A. Biochemistry 39: 978-984.
    • (2000) Biochemistry , vol.39 , pp. 978-984
    • Raghothama, S.1    Simpson, P.J.2    Szabo, L.3    Nagy, T.4    Gilbert, H.5    Williamson, M.P.6
  • 42
    • 78650826171 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable cellobiohydrolase from Fomitopsis pinicola
    • Shin, K., Y. H. Kim, M. Jeya, J. K. Lee, and Y. S. Kim. 2010. Purification and characterization of a thermostable cellobiohydrolase from Fomitopsis pinicola. J. Microbiol. Biotechnol. 20: 1681-1688.
    • (2010) J. Microbiol. Biotechnol , vol.20 , pp. 1681-1688
    • Shin, K.1    Kim, Y.H.2    Jeya, M.3    Lee, J.K.4    Kim, Y.S.5
  • 43
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N. and R. W. Woody. 2000. Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287: 252-260.
    • (2000) Anal. Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 44
    • 0030606294 scopus 로고    scopus 로고
    • Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei
    • Stahlberg, J., C. Divne, A. Koivula, K. Piens, M. Claeyssens, T. T. Teeri, et al. 1996. Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei. J. Molec. Biol. 264: 337-349.
    • (1996) J. Molec. Biol , vol.264 , pp. 337-349
    • Stahlberg, J.1    Divne, C.2    Koivula, A.3    Piens, K.4    Claeyssens, M.5    Teeri, T.T.6
  • 45
    • 14744278342 scopus 로고
    • A new model for enzymatic hydrolysis of cellulose based on the 2-domains structure of cellobiohydrolase-I
    • Stahlberg, J., G. Johansson, and G. Pettersson. 1991. A new model for enzymatic hydrolysis of cellulose based on the 2-domains structure of cellobiohydrolase-I. Biotechnology 9: 286-290.
    • (1991) Biotechnology , vol.9 , pp. 286-290
    • Stahlberg, J.1    Johansson, G.2    Pettersson, G.3
  • 46
    • 1942486976 scopus 로고    scopus 로고
    • Factors influencing glycosylation of Trichoderma reesei cellulases. I: Postsecretorial changes of the O-and N-glycosylation pattern of Cel7A
    • Stals, I., K. Sandra, S. Geysens, R. Contreras, J. Van Beeumen, M. Claeyssens, et al. 2004. Factors influencing glycosylation of Trichoderma reesei cellulases. I: Postsecretorial changes of the O-and N-glycosylation pattern of Cel7A. Glycobiology 14: 713-724.
    • (2004) Glycobiology , vol.14 , pp. 713-724
    • Stals, I.1    Sandra, K.2    Geysens, S.3    Contreras, R.4    van Beeumen, J.5    Claeyssens, M.6
  • 47
    • 0028261414 scopus 로고
    • Deglycosylation of asparagine-linked glycans: Purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum
    • Tarentino, A. L. and T. H. Plummer Jr. 1994. Deglycosylation of asparagine-linked glycans: Purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum. Methods Enz. 230: 44-57.
    • (1994) Methods Enz , vol.230 , pp. 44-57
    • Tarentino, A.L.1    Plummer Jr., T.H.2
  • 48
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: New insight into the function of cellobiohydrolases
    • Teeri, T. T. 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
  • 50
    • 33845985596 scopus 로고    scopus 로고
    • Degradation of cellulose and hemicelluloses by the brown rot fungus Piptoporus betulinus: Production of extracellular enzymes and characterization of the major cellulases
    • Valaskova, V. and P. Baldrian. 2006. Degradation of cellulose and hemicelluloses by the brown rot fungus Piptoporus betulinus: Production of extracellular enzymes and characterization of the major cellulases. Microbiology 152: 3613-3622.
    • (2006) Microbiology , vol.152 , pp. 3613-3622
    • Valaskova, V.1    Baldrian, P.2
  • 51
    • 0142106377 scopus 로고    scopus 로고
    • Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Ce17A. A comparison with Phanerochaete chrysosporium Cel7D
    • von Ossowski, I., J. Stahlberg, A. Koivula, K. Piens, D. Becker, H. Boer, et al. 2003. Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Ce17A. A comparison with Phanerochaete chrysosporium Cel7D. J. Molec. Biol. 333: 817-829.
    • (2003) J. Molec. Biol , vol.333 , pp. 817-829
    • von Ossowski, I.1    Stahlberg, J.2    Koivula, A.3    Piens, K.4    Becker, D.5    Boer, H.6
  • 52
    • 17644439305 scopus 로고    scopus 로고
    • Comparison of domains function between cellobiohydrolase I and endoglucanase I from Trichoderma pseudokoningii S-38 by limited proteolysis
    • Wang, L. S., J. Liu, Y. Z. Zhang, Y. Zhao, and P. J. Gao. 2003. Comparison of domains function between cellobiohydrolase I and endoglucanase I from Trichoderma pseudokoningii S-38 by limited proteolysis. J. Molec. Catal. B Enzymatic 24: 27-38.
    • (2003) J. Molec. Catal. B Enzymatic , vol.24 , pp. 27-38
    • Wang, L.S.1    Liu, J.2    Zhang, Y.Z.3    Zhao, Y.4    Gao, P.J.5
  • 53
    • 0035543093 scopus 로고    scopus 로고
    • The depth of chemical time and the power of enzymes as catalysts
    • Wolfenden, R. and M. J. Snider. 2001. The depth of chemical time and the power of enzymes as catalysts. Accounts Chem. Res. 34: 938-945.
    • (2001) Accounts Chem. Res , vol.34 , pp. 938-945
    • Wolfenden, R.1    Snider, M.J.2
  • 54
    • 77957034698 scopus 로고
    • Methods for measuring cellulase activities
    • Wood, T. M. and K. M. Bhat. 1988. Methods for measuring cellulase activities. Methods Enz. 160: 87-112.
    • (1988) Methods Enz , vol.160 , pp. 87-112
    • Wood, T.M.1    Bhat, K.M.2
  • 55
    • 34249869832 scopus 로고    scopus 로고
    • Ab initio modeling of small proteins by iterative TASSER simulations
    • Wu, S. T., J. Skolnick, and Y. Zhang. 2007. Ab initio modeling of small proteins by iterative TASSER simulations. BMC Biol. 5: 17.
    • (2007) BMC Biol , vol.5 , pp. 17
    • Wu, S.T.1    Skolnick, J.2    Zhang, Y.3
  • 56
    • 33746121105 scopus 로고    scopus 로고
    • Outlook for cellulase improvement: Screening and selection strategies
    • Zhang, Y. H. P., M. E. Himmel, and J. R. Mielenz. 2006. Outlook for cellulase improvement: Screening and selection strategies. Biotechnol. Adv. 24: 452-481.
    • (2006) Biotechnol. Adv , vol.24 , pp. 452-481
    • Zhang, Y.H.P.1    Himmel, M.E.2    Mielenz, J.R.3
  • 57
    • 10844286172 scopus 로고    scopus 로고
    • Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems
    • Zhang, Y. H. P. and L. R. Lynd. 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.P.1    Lynd, L.R.2
  • 58
    • 44449092955 scopus 로고    scopus 로고
    • Identification and purification of the main components of cellulases from a mutant strain of Trichoderma viride T 100-14
    • Zhou, J., Y. H. Wang, J. Chu, Y. P. Zhuang, S. L. Zhang, and P. Yin. 2008. Identification and purification of the main components of cellulases from a mutant strain of Trichoderma viride T 100-14. Bioresour. Technol. 99: 6826-6833.
    • (2008) Bioresour. Technol , vol.99 , pp. 6826-6833
    • Zhou, J.1    Wang, Y.H.2    Chu, J.3    Zhuang, Y.P.4    Zhang, S.L.5    Yin, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.