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Volumn 11, Issue 7, 2012, Pages

Quantitative secretomic analysis of Trichoderma reesei strains reveals enzymatic composition for lignocellulosic biomass degradation

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBATE PEROXIDASE; CELLULASE; CHITINASE; GLYCOSIDASE; HEMICELLULOSE; LIGNIN; LIGNOCELLULOSE; PHOSPHATASE; PROTEINASE; SUPEROXIDE DISMUTASE; CARRIER PROTEIN; FUNGAL PROTEIN; PEPTIDE HYDROLASE;

EID: 84862229138     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.012419     Document Type: Article
Times cited : (127)

References (69)
  • 1
    • 0036159062 scopus 로고    scopus 로고
    • Hydrolysis of lignocellulosic materials for ethanol production: A review
    • DOI 10.1016/S0960-8524(01)00212-7, PII S0960852401002127
    • Sun, Y., and Cheng, J. Y. (2002) Hydrolysis of lignocellulosic materials for ethanol production: A review. Bioresource Technol. 83, 1-11 (Pubitemid 34126398)
    • (2002) Bioresource Technology , vol.83 , Issue.1 , pp. 1-11
    • Sun, Y.1    Cheng, J.2
  • 2
    • 43049115291 scopus 로고    scopus 로고
    • Trends in biotechnological production of fuel ethanol from different feedstocks
    • Sanchez, O. J., and Cardona, C. A. (2008) Trends in biotechnological production of fuel ethanol from different feedstocks. Bioresource Technol. 99, 5270-5295
    • (2008) Bioresource Technol. , vol.99 , pp. 5270-5295
    • Sanchez, O.J.1    Cardona, C.A.2
  • 5
    • 77955445449 scopus 로고    scopus 로고
    • Quantitative iTRAQ secretome analysis of Aspergillus niger reveals novel hydrolytic enzymes
    • Adav, S. S., Li, A. A., Manavalan, A., Punt, P., and Sze, S. K. (2010) Quantitative iTRAQ secretome analysis of Aspergillus niger reveals novel hydrolytic enzymes. J. Proteome Res. 9, 3932-3940
    • (2010) J. Proteome Res. , vol.9 , pp. 3932-3940
    • Adav, S.S.1    Li, A.A.2    Manavalan, A.3    Punt, P.4    Sze, S.K.5
  • 6
    • 80052037383 scopus 로고    scopus 로고
    • ITRAQ-based quantitative proteomic analysis of Thermobifida fusca reveals metabolic pathways of cellulose utilization
    • Adav, S. S., Ng, C. S., and Sze, S. K. (2011) iTRAQ-based quantitative proteomic analysis of Thermobifida fusca reveals metabolic pathways of cellulose utilization. J. Proteomics. 74, 2112-2122
    • (2011) J. Proteomics. , vol.74 , pp. 2112-2122
    • Adav, S.S.1    Ng, C.S.2    Sze, S.K.3
  • 7
    • 82455171991 scopus 로고    scopus 로고
    • ITRAQ-based quantitative secretome analysis of Phanerochaete chrysosporium
    • Manavalan, A., Adav, S. S., and Sze, S. K. (2011) iTRAQ-based quantitative secretome analysis of Phanerochaete chrysosporium. J. Proteomics. 75, 642-654
    • (2011) J. Proteomics. , vol.75 , pp. 642-654
    • Manavalan, A.1    Adav, S.S.2    Sze, S.K.3
  • 8
    • 0001646214 scopus 로고    scopus 로고
    • Applications of Trichoderma reesei enzymes in the pulp and paper industry
    • Harman, G. E., and Kubicek, C. P., eds, Taylor and Francis, London
    • Buchert, J., Oksanen, T., Pere, J., Siika-Aho, M., Suurnäkki, A., and Viirkari, L. (1998) Applications of Trichoderma reesei enzymes in the pulp and paper industry. In Trichoderma and Gliocladium (Harman, G. E., and Kubicek, C. P., eds), pp. 343-363, Taylor and Francis, London
    • (1998) Trichoderma and Gliocladium , pp. 343-363
    • Buchert, J.1    Oksanen, T.2    Pere, J.3    Siika-Aho, M.4    Suurnäkki, A.5    Viirkari, L.6
  • 9
    • 0001098948 scopus 로고    scopus 로고
    • Application of Trichoderma enzymes in the textile industry
    • Harman, G. E., and Kubicek, C. P., eds, Taylor and Francis, London
    • Galante, Y. M., De Conti, A., and Monteverdi, R. (1998) Application of Trichoderma enzymes in the textile industry. In Trichoderma and Gliocladium (Harman, G. E., and Kubicek, C. P., eds), pp. 311-326, Taylor and Francis, London
    • (1998) Trichoderma and Gliocladium , pp. 311-326
    • Galante, Y.M.1    De Conti, A.2    Monteverdi, R.3
  • 10
    • 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
  • 11
    • 0031602223 scopus 로고    scopus 로고
    • Characterization of mycelial morphology using image analysis
    • Paul, G. C., and Thomas, C. R. (1998) Characterization of mycelial morphology using image analysis. Adv. Biochem. Eng. Biotechnol. 60, 1-59
    • (1998) Adv. Biochem. Eng. Biotechnol. , vol.60 , pp. 1-59
    • Paul, G.C.1    Thomas, C.R.2
  • 12
    • 0038632044 scopus 로고    scopus 로고
    • Influence of morphology on the near-infrared spectra of mycelial biomass and its implications in bioprocess monitoring
    • DOI 10.1002/bit.10621
    • Vaidyanathan, S., White, S., Harvey, L. M., and McNeil, B. (2003) Influence of morphology on the near-infrared spectra of mycelial biomass and its implications in bioprocess monitoring. Biotechnol. Bioeng. 82, 715-724 (Pubitemid 36576236)
    • (2003) Biotechnology and Bioengineering , vol.82 , Issue.6 , pp. 715-724
    • Vaidyanathan, S.1    White, S.2    Harvey, L.M.3    McNeil, B.4
  • 13
    • 0034002738 scopus 로고    scopus 로고
    • The influence of culture conditions on mycelial structure and cellulase production by Trichoderma reesei Rut C-30
    • DOI 10.1016/S0141-0229(99)00166-0, PII S0141022999001660
    • Domingues, F. C., Queiroz, J. A., Cabral, J. M., and Fonseca, L. P. (2000) The influence of culture conditions on mycelial structure and cellulase production by Trichoderma reesei Rut C-30. Enzyme Microb. Tech. 26, 394-401 (Pubitemid 30122407)
    • (2000) Enzyme and Microbial Technology , vol.26 , Issue.5-6 , pp. 394-401
    • Domingues, F.C.1    Queiroz, J.A.2    Cabral, J.M.S.3    Fonseca, L.P.4
  • 14
    • 0032031899 scopus 로고    scopus 로고
    • Influence of morphology on product formation in Aspergillus awamori during submerged fermentations
    • DOI 10.1021/bp980014x
    • Johansen, C. L., Coolen, L., and Hunik, J. H. (1998) Influence of morphology on product formation in Aspergillus awamori during submerged fermentations. Biotechnol. Progr. 14, 233-240 (Pubitemid 28202607)
    • (1998) Biotechnology Progress , vol.14 , Issue.2 , pp. 233-240
    • Johansen, C.L.1    Coolen, L.2    Hunik, J.H.3
  • 15
    • 0037509011 scopus 로고    scopus 로고
    • The relationship between pellet size and production of Mn(II) peroxidase by Phanerochaete chrysosporium in submerged culture
    • DOI 10.1016/S0141-0229(97)00065-3, PII S0141022997000653
    • Jimenez-Tobon, G. A., Penninckx, M. J., and Lejeune, R. (1997) The relationship between pellet size and production of Mn(II) peroxidase by Phanerochaete chrysosporium in submerged culture. Enzyme Microb. Tech. 21, 537-542 (Pubitemid 27489051)
    • (1997) Enzyme and Microbial Technology , vol.21 , Issue.7 , pp. 537-542
    • Jimenez-Tobon, G.A.1    Penninckx, M.J.2    Lejeune, R.3
  • 16
    • 80053899949 scopus 로고    scopus 로고
    • Proteomics analysis of pH and strains dependent protein secretion of Trichoderma reesei
    • Adav, S. S., Ravindran, A., Chao, L. T., Tan, L., Singh, S., and Sze, S. K. (2011) Proteomics analysis of pH and strains dependent protein secretion of Trichoderma reesei. J. Proteome Res. 10, 4579-4596
    • (2011) J. Proteome Res. , vol.10 , pp. 4579-4596
    • Adav, S.S.1    Ravindran, A.2    Chao, L.T.3    Tan, L.4    Singh, S.5    Sze, S.K.6
  • 17
    • 0025602002 scopus 로고
    • Cellobiose metabolism and cellobiohydrolase-I biosynthesis by Trichoderma reesei
    • Fritscher, C., Messner, R., and Kubicek, C. P. (1990) Cellobiose metabolism and cellobiohydrolase-I biosynthesis by Trichoderma reesei. Exp. Mycol. 14, 405-415
    • (1990) Exp. Mycol. , vol.14 , pp. 405-415
    • Fritscher, C.1    Messner, R.2    Kubicek, C.P.3
  • 19
    • 0029045457 scopus 로고
    • The Bgl1 gene of Trichoderma reesei QM-9414 encodes an extracellular, cellulose-inducible β-glucosidase involved in cellulase induction by Sophorose
    • Mach, R. L., Seiboth, B., Myasnikov, A., Gonzalez, R., Strauss, J., Harkki, A. M., and Kubicek, C. P. (1995) The Bgl1 gene of Trichoderma reesei QM-9414 encodes an extracellular, cellulose-inducible β-glucosidase involved in cellulase induction by Sophorose. Mol. Microbiol. 16, 687-697
    • (1995) Mol. Microbiol. , vol.16 , pp. 687-697
    • Mach, R.L.1    Seiboth, B.2    Myasnikov, A.3    Gonzalez, R.4    Strauss, J.5    Harkki, A.M.6    Kubicek, C.P.7
  • 20
    • 0031295876 scopus 로고    scopus 로고
    • Cellulose degrading enzymes and their potential industrial applications
    • DOI 10.1016/S0734-9750(97)00006-2, PII S0734975097000062
    • Bhat, M. K., and Bhat, S. (1997) Cellulose degrading enzymes and their potential industrial applications. Biotechnol. Adv. 15, 583-620 (Pubitemid 29369840)
    • (1997) Biotechnology Advances , vol.15 , Issue.3-4 , pp. 583-620
    • Bhat, M.K.1    Bhat, S.2
  • 21
    • 0001956748 scopus 로고    scopus 로고
    • Regulation of production of plant polysaccharide degrading enzymes by Trichoderma
    • Harman, G. E., and Kubicek, C. P., eds, Taylor & Francis Ltd., Bristol, UK
    • Kubicek, C. P., and Penttila, M. E. (1998) Regulation of production of plant polysaccharide degrading enzymes by Trichoderma. In Trichoderma and Gliocladium (Harman, G. E., and Kubicek, C. P., eds), pp. 49-67, Taylor & Francis Ltd., Bristol, UK
    • (1998) Trichoderma and Gliocladium , pp. 49-67
    • Kubicek, C.P.1    Penttila, M.E.2
  • 22
    • 77955407242 scopus 로고    scopus 로고
    • Synthetic enzyme mixtures for biomass deconstruction: Production and optimization of a core set
    • Banerjee, G., Car, S., Scott-Craig, J. S., Borrusch, M. S., Aslam, N., and Walton, J. D. (2010) Synthetic enzyme mixtures for biomass deconstruction: Production and optimization of a core set. Biotechnol. Bioeng. 106, 707-720
    • (2010) Biotechnol. Bioeng. , vol.106 , pp. 707-720
    • Banerjee, G.1    Car, S.2    Scott-Craig, J.S.3    Borrusch, M.S.4    Aslam, N.5    Walton, J.D.6
  • 23
    • 77957734512 scopus 로고    scopus 로고
    • Rapid optimization of enzyme mixtures for deconstruction of diverse pretreatment/biomass feedstock combinations
    • art. no. 22
    • Banerjee, G., Car, S., Scott-Craig, J. S., Borrusch, M. S., and Walton, J. D. (2010) Rapid optimization of enzyme mixtures for deconstruction of diverse pretreatment/biomass feedstock combinations. Biotechnol. Biofuels 3, art. no. 22
    • (2010) Biotechnol. Biofuels , vol.3
    • Banerjee, G.1    Car, S.2    Scott-Craig, J.S.3    Borrusch, M.S.4    Walton, J.D.5
  • 25
    • 0003131715 scopus 로고
    • Biochemical aspects of the production of microbial hemicellulases
    • Coughlam, M. P., and Hazlewood, G. P., eds Potland Press, London
    • Biely, P. (1993) Biochemical aspects of the production of microbial hemicellulases. In Hemicellulose and hemicellulases (Coughlam, M. P., and Hazlewood, G. P., eds) pp. 127-143, Potland Press, London
    • (1993) Hemicellulose and Hemicellulases , pp. 127-143
    • Biely, P.1
  • 26
    • 0000961468 scopus 로고
    • Production of acetyl xylan esterase by Trichoderma reesei and Schizophyllum commune
    • Biely, P., Mackenzie, C. R., and Schneider, H. (1988) Production of acetyl xylan esterase by Trichoderma reesei and Schizophyllum commune. Can. J. Microbiol. 34, 767-772
    • (1988) Can. J. Microbiol. , vol.34 , pp. 767-772
    • Biely, P.1    Mackenzie, C.R.2    Schneider, H.3
  • 27
    • 77954316235 scopus 로고    scopus 로고
    • Cellulases, xylanases, β-glucosidase and ferulic acid esterase produced by Trichoderma and Aspergillus act synergistically in the hydrolysis of sugarcane bagasse
    • Gottschalk, L. M., Oliveira, R. A., and Bon, E. P. (2010) Cellulases, xylanases, β-glucosidase and ferulic acid esterase produced by Trichoderma and Aspergillus act synergistically in the hydrolysis of sugarcane bagasse. Biochem. Eng. J. 51, 72-78
    • (2010) Biochem. Eng. J. , vol.51 , pp. 72-78
    • Gottschalk, L.M.1    Oliveira, R.A.2    Bon, E.P.3
  • 28
    • 24944461039 scopus 로고    scopus 로고
    • Characterization of cellulases and hemicellulases produced by Trichoderma reesei on various carbon sources
    • DOI 10.1016/j.procbio.2005.03.057, PII S1359511305002035
    • Juhasz, T., Szengyel, Z., Reczey, K., Siika-Aho, M., and Viikari, L. (2005) Characterization of cellulases and hemicellulases produced by Trichoderma reesei on various carbon sources. Process Biochem. 40, 3519-3525 (Pubitemid 41327364)
    • (2005) Process Biochemistry , vol.40 , Issue.11 , pp. 3519-3525
    • Juhasz, T.1    Szengyel, Z.2    Reczey, K.3    Siika-Aho, M.4    Viikari, L.5
  • 29
    • 77954595049 scopus 로고    scopus 로고
    • Quantitative iTRAQ Secretome analysis of cellulolytic Thermobifida fusca
    • Adav, S. S., Ng, C. S., Arulmani, M., and Sze, S. K. (2010) Quantitative iTRAQ Secretome analysis of cellulolytic Thermobifida fusca. J. Proteome Res. 9, 3016-3024
    • (2010) J. Proteome Res. , vol.9 , pp. 3016-3024
    • Adav, S.S.1    Ng, C.S.2    Arulmani, M.3    Sze, S.K.4
  • 30
    • 77954368187 scopus 로고    scopus 로고
    • Novel application of electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) in shotgun proteomics: Comprehensive profiling of rat kidney proteome
    • Hao, P., Guo, T., Li, X., Adav, S. S., Yang, J., Wei, M., and Sze, S. K. (2010) Novel application of electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) in shotgun proteomics: Comprehensive profiling of rat kidney proteome. J. Proteome Res. 9, 3520-3526
    • (2010) J. Proteome Res. , vol.9 , pp. 3520-3526
    • Hao, P.1    Guo, T.2    Li, X.3    Adav, S.S.4    Yang, J.5    Wei, M.6    Sze, S.K.7
  • 31
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • Bendtsen J. D., Nielsen H., von Heijne G., and Brunak, S. (2004) Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 340, 783-795 (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 32
    • 77956818710 scopus 로고    scopus 로고
    • Cellotriose and cellotetraose as inducers of the genes encoding cellobiohydrolases in the basidiomycete Phanerochaete chrysosporium
    • Suzuki, H., Igarashi, K., and Samejima, M. (2010) Cellotriose and cellotetraose as inducers of the genes encoding cellobiohydrolases in the basidiomycete Phanerochaete chrysosporium. Appl. Environ. Microbiol. 76, 6164-6170
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 6164-6170
    • Suzuki, H.1    Igarashi, K.2    Samejima, M.3
  • 33
    • 77954676864 scopus 로고    scopus 로고
    • Array comparative genomic hybridization analysis of Trichoderma reesei strains with enhanced cellulase production properties
    • Vitikainen, M., Arvas, M., Pakula, T., Oja, M., Penttilä, M., and Saloheimo, M. (2010) Array comparative genomic hybridization analysis of Trichoderma reesei strains with enhanced cellulase production properties. BMC Genomics 11, 441
    • (2010) BMC Genomics , vol.11 , pp. 441
    • Vitikainen, M.1    Arvas, M.2    Pakula, T.3    Oja, M.4    Penttilä, M.5    Saloheimo, M.6
  • 35
    • 0030036051 scopus 로고    scopus 로고
    • The glucose repressor gene cre1 of Trichoderma: Isolation and expression of a full-length and a truncated mutant form
    • Ilmén, M., Thrane, C., and Penttilä, M. (1996) The glucose repressor gene cre1 of Trichoderma: Isolation and expression of a full-length and a truncated mutant form. Mol. Gen. Genet. 251, 451-460
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 451-460
    • Ilmén, M.1    Thrane, C.2    Penttilä, M.3
  • 36
    • 48249114001 scopus 로고    scopus 로고
    • The Hypocrea jecorina (Trichoderma reesei) hypercellulolytic mutant RUT C30 lacks a 85 kb (29 gene-encoding) region of the wild-type genome
    • Seidl, V., Gamauf, C., Druzhinina, I. S., Seiboth, B., Hartl, L., and Kubicek, C. P. (2008) The Hypocrea jecorina (Trichoderma reesei) hypercellulolytic mutant RUT C30 lacks a 85 kb (29 gene-encoding) region of the wild-type genome. BMC Genomics 9, 327
    • (2008) BMC Genomics , vol.9 , pp. 327
    • Seidl, V.1    Gamauf, C.2    Druzhinina, I.S.3    Seiboth, B.4    Hartl, L.5    Kubicek, C.P.6
  • 37
    • 20444391995 scopus 로고    scopus 로고
    • Cloning and characterization of the glucosidase II alpha subunit gene of Trichoderma reesei: A frameshift mutation results in the aberrant glycosylation profile of the hypercellulolytic strain Rut-C30
    • DOI 10.1128/AEM.71.6.2910-2924.2005
    • Geysens, S., Pakula, T., Uusitalo, J., Dewerte, I., Penttilä, M., and Contreras, R. (2005) Cloning and characterization of the glucosidase II α subunit gene of Trichoderma reesei: A frameshift mutation results in the aberrant glycosylation profile of the hypercellulolytic strain Rut-C30. Appl. Environ. Microbiol. 71, 2910-2924 (Pubitemid 40807194)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.6 , pp. 2910-2924
    • Geysens, S.1    Pakula, T.2    Uusitalo, J.3    Dewerte, I.4    Penttila, M.5    Contreras, R.6
  • 47
    • 0023264566 scopus 로고
    • 2 production by Phanerochaete chrysosporium
    • 2 production by Phanerochaete chrysosporium. J. Bacteriol. 169, 2195-2201
    • (1987) J. Bacteriol. , vol.169 , pp. 2195-2201
    • Kersten, P.J.1    Kirk, T.K.2
  • 48
    • 0025246775 scopus 로고
    • Glyoxal oxidase of Phanerochaete chrysosporium: Its characterization and activation by lignin peroxidase
    • Kersten, P. J. (1990) Glyoxal oxidase of Phanerochaete chrysosporium: Its characterization and activation by lignin peroxidase. Proc. Natl. Acad. Sci. U.S.A. 87, 2936-2940
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 2936-2940
    • Kersten, P.J.1
  • 49
    • 0343990851 scopus 로고    scopus 로고
    • Cell wall alterations in loblolly pine wood decayed by the white-rot fungus, Ceriporiopsis subvermispora
    • DOI 10.1016/S0168-1656(97)01674-X, PII S016816569701674X
    • Blanchette, R. A., Krueger, E. W., Haight, J. E., Akhtar, M., and Akin, D. E. (1997) Cell wall alterations in loblolly pine wood decayed by the white-rot fungus, Ceriporiopsis subvermispora. J. Biotechnol. 53, 203-213 (Pubitemid 27286438)
    • (1997) Journal of Biotechnology , vol.53 , Issue.2-3 , pp. 203-213
    • Blanchette, R.A.1    Krueger, E.W.2    Haight, J.E.3    Akhtar, M.4    Akin, D.E.5
  • 50
    • 0342327383 scopus 로고    scopus 로고
    • Sugar oxidoreductases and veratryl alcohol oxidase as related to lignin degradation
    • DOI 10.1016/S0168-1656(97)01680-5, PII S0168165697016805
    • Ander, P., and Marzullo, L. (1997) Sugar oxidoreductases and veratryl alcohol oxidase as related to lignin degradation. J. Biotechnol. 53, 115-131 (Pubitemid 27286435)
    • (1997) Journal of Biotechnology , vol.53 , Issue.2-3 , pp. 115-131
    • Ander, P.1    Marzullo, L.2
  • 52
    • 28944455667 scopus 로고    scopus 로고
    • The secretome of Pleurotus sapidus
    • DOI 10.1002/pmic.200500015
    • Zorn, H., Peters, T., Nimtz, M., and Berger, R. G. (2005) The secretome of Pleurotus sapidus. Proteomics 5, 4832-4838 (Pubitemid 43016903)
    • (2005) Proteomics , vol.5 , Issue.18 , pp. 4832-4838
    • Zorn, H.1    Peters, T.2    Nimtz, M.3    Berger, R.G.4
  • 53
    • 33646570211 scopus 로고    scopus 로고
    • Proteomic analysis of extracellular proteins from Aspergillus oryzae grown under submerged and solid-state culture conditions
    • DOI 10.1128/AEM.72.5.3448-3457.2006
    • Oda, K., Kakizono, D., Yamada, O., Iefuji, H., Akita, O., and Iwashita, K. (2006) Proteomic analysis of extracellular proteins from Aspergillus oryzae grown under submerged and solid-state culture conditions. Appl. Environ. Microbiol. 72, 3448-3457 (Pubitemid 43727998)
    • (2006) Applied and Environmental Microbiology , vol.72 , Issue.5 , pp. 3448-3457
    • Oda, K.1    Kakizono, D.2    Yamada, O.3    Iefuji, H.4    Akita, O.5    Iwashita, K.6
  • 54
    • 0842348166 scopus 로고    scopus 로고
    • Proteomic analysis of rutin-induced secreted proteins from Aspergillus flavus
    • DOI 10.1016/j.fgb.2003.11.014
    • Medina, M. L., Kiernan, U. A., and Francisco, W. A. (2004) Proteomic analysis of rutin-induced secreted proteins from Aspergillus flavus. Fungal Genet. Biol. 41, 327-335 (Pubitemid 38169452)
    • (2004) Fungal Genetics and Biology , vol.41 , Issue.3 , pp. 327-335
    • Medina, M.L.1    Kiernan, U.A.2    Francisco, W.A.3
  • 55
    • 34748923122 scopus 로고    scopus 로고
    • Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum
    • DOI 10.1002/pmic.200700184
    • Paper, J. M., Scott-Craig, J. S., Adhikari, N. D., Cuomo, C. A., and Walton, J. D. (2007) Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum. Proteomics 7, 3171-3183 (Pubitemid 47477959)
    • (2007) Proteomics , vol.7 , Issue.17 , pp. 3171-3183
    • Paper, J.M.1    Scott-Craig, J.S.2    Adhikari, N.D.3    Cuomo, C.A.4    Walton, J.D.5
  • 56
    • 84874663198 scopus 로고    scopus 로고
    • Fungal genome initiative. Broad Institute of Harvard and MIT (http://www.broad.mit.edu).
    • Fungal Genome Initiative
  • 60
    • 0028765765 scopus 로고
    • Adsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline cellulose
    • DOI 10.1002/bit.260440907
    • Medve, J., Ståhlberg, J., and Tjerneld, F. (1994) Adsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline cellulose. Biotechnol. Bioeng. 44, 1064-1073 (Pubitemid 24331656)
    • (1994) Biotechnology and Bioengineering , vol.44 , Issue.9 , pp. 1064-1073
    • Medve, J.1    Stahlberg, J.2    Tjerneld, F.3
  • 61
    • 84996102559 scopus 로고
    • Reversibility and competition in the adsorption of Trichoderma reesei cellulase components
    • Kyriacou, A., Neufeld, R. J., and Mackenzie, C. R. (1989) Reversibility and competition in the adsorption of Trichoderma reesei cellulase components. Biotechnol. Bioeng. 33, 631-637
    • (1989) Biotechnol. Bioeng. , vol.33 , pp. 631-637
    • Kyriacou, A.1    Neufeld, R.J.2    Mackenzie, C.R.3
  • 62
    • 0034124523 scopus 로고    scopus 로고
    • Cell wall and membraneassociated exo-β-D-glucanases from developing maize seedlings
    • Kim, J. B., Olek, A. T., and Carpita, N. C. (2000) Cell wall and membraneassociated exo-β-D-glucanases from developing maize seedlings. Plant Physiol. 123, 471-486
    • (2000) Plant Physiol. , vol.123 , pp. 471-486
    • Kim, J.B.1    Olek, A.T.2    Carpita, N.C.3
  • 64
    • 42149108423 scopus 로고    scopus 로고
    • Bioconversion of lignocellulosic biomass: Biochemical and molecular perspectives
    • Kumar, R., Singh, S., and Singh, O. V. (2008) Bioconversion of lignocellulosic biomass: Biochemical and molecular perspectives. J. Indust. Microbiol. Biotechnol. 35, 377-391
    • (2008) J. Indust. Microbiol. Biotechnol. , vol.35 , pp. 377-391
    • Kumar, R.1    Singh, S.2    Singh, O.V.3
  • 66
    • 0031735449 scopus 로고    scopus 로고
    • Plant cell wall proteins
    • Cassab, G. I. (1998) Plant cell wall proteins. Annu. Rev. Plant Phys. 49, 281-309
    • (1998) Annu. Rev. Plant Phys. , vol.49 , pp. 281-309
    • Cassab, G.I.1
  • 68
    • 34250372161 scopus 로고    scopus 로고
    • A barley xyloglucan xyloglucosyl transferase covalently links xyloglucan, cellulosic substrates, and (1,3;1,4)-β-D-glucans
    • DOI 10.1074/jbc.M611487200
    • Hrmova, M., Farkas, V., Lahnstein, J., and Fincher, G. B. (2007) A barley xyloglucan xyloglucosyl transferase covalently links xyloglucan, cellulosic substrates, and (1,3;1,4)-β-D-glucans. J. Biol. Chem. 282, 12951-12962 (Pubitemid 47100602)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 12951-12962
    • Hrmova, M.1    Farkas, V.2    Lahnstein, J.3    Fincher, G.B.4
  • 69
    • 0000146858 scopus 로고
    • Mixed linkage β-glucan, protein-content, and kernel weight in avena species
    • Miller, S. S., Wood, P. J., Pietrzak, L. N., and Fulcher, R. G. (1993) Mixed linkage β-glucan, protein-content, and kernel weight in avena species. Cereal Chem. 70, 231-233
    • (1993) Cereal Chem. , vol.70 , pp. 231-233
    • Miller, S.S.1    Wood, P.J.2    Pietrzak, L.N.3    Fulcher, R.G.4


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