메뉴 건너뛰기




Volumn , Issue 550, 2004, Pages 3-96

Trichoderma reesei strains for production of cellulases for the textile industry

Author keywords

Biofinishing; Biostoning; Cellulase; Cloning; Homologous and heterologous gene expression; Melanocarpus albomyces; Textile industry; Trichoderma reesei

Indexed keywords


EID: 84884721967     PISSN: 12350621     EISSN: 14550849     Source Type: Book Series    
DOI: None     Document Type: Review
Times cited : (4)

References (209)
  • 1
    • 0025777266 scopus 로고
    • Monoclonal antibodies against core and cellulose-binding domains of Trichoderma reesei cellobiohydrolase I and II and endoglucanase I
    • Aho, S., Olkkonen, V., Jalava, T., Paloheimo, M., Bühler, R., Niku-Paavola, M.-L., Bamford, D. and Korhola, M. 1991. Monoclonal antibodies against core and cellulose-binding domains of Trichoderma reesei cellobiohydrolase I and II and endoglucanase I. Eur. J. Biochem. 200:643-649.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 643-649
    • Aho, S.1    Olkkonen, V.2    Jalava, T.3    Paloheimo, M.4    Bühler, R.5    Niku-Paavola, M.-L.6    Bamford, D.7    Korhola, M.8
  • 3
    • 0031307441 scopus 로고    scopus 로고
    • The molecular biology of secreted enzyme production by fungi
    • Archer, D. and Peberdy, J. 1997. The molecular biology of secreted enzyme production by fungi. Crit. Rev. Biotechnol. 17:273-306. (Pubitemid 127716529)
    • (1997) Critical Reviews in Biotechnology , vol.17 , Issue.4 , pp. 273-306
    • Archer, D.B.1    Peberdy, J.F.2
  • 4
    • 0037250343 scopus 로고    scopus 로고
    • Characterization of novel transcription factors ACEI and ACEII involved in regulation of cellulase and xylanase genes in Trichoderma reesei
    • Academic dissertation. Espoo: app.
    • Aro, N. 2003. Characterization of novel transcription factors ACEI and ACEII involved in regulation of cellulase and xylanase genes in Trichoderma reesei. Academic dissertation. Espoo: VTT Publications 488. 83 p. + app. 25 p. http://www.vtt.fi/inf/pdf/publications/2003/P488.pdf
    • (2003) VTT Publications , vol.488
    • Aro, N.1
  • 5
    • 0035968258 scopus 로고    scopus 로고
    • ACEII, a novel transcriptional activator involved in regulation of cellulase and xylanase genes of Trichoderma reesei
    • Aro, N., Saloheimo, A., Ilmén, M. and Penttilä, M. 2001. ACEII, a novel transcriptional activator involved in regulation of cellulase and xylanase genes of Trichoderma reesei. J. Biol. Chem. 276:24309-24314.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24309-24314
    • Aro, N.1    Saloheimo, A.2    Ilmén, M.3    Penttilä, M.4
  • 6
    • 0037226849 scopus 로고    scopus 로고
    • ACEI of Trichoderma reesei is a repressor of cellulase and xylanase expression
    • DOI 10.1128/AEM.69.1.56-65.2003
    • Aro, N., Ilmén, M., Saloheimo, A. and Penttilä, M. 2003. ACEI of Trichoderma reesei is a repressor of cellulase and xylanase expression. Appl. Environ. Microbiol. 69:56-65. (Pubitemid 36077457)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.1 , pp. 56-65
    • Aro, N.1    Ilmen, M.2    Saloheimo, A.3    Penttila, M.4
  • 7
    • 0034255675 scopus 로고    scopus 로고
    • Effects of agitation level on the adsorption, desorption, and activities on cotton fabrics of full length and core domains of EGV (Humicola insolens) and CenA (Cellulomonas fimi)
    • DOI 10.1016/S0141-0229(00)00205-2, PII S0141022900002052
    • Azevedo, H., Bishop, D. and Cavaco-Paulo, A. 2000. Effects of agitation level on the adsorption, desorption, and activities on cotton fabric of full length and core domains of EGV (Humicola insolens) and CenA (Cellulomonas fimi). Enzyme Microb. Technol. 27:325-329. (Pubitemid 30427208)
    • (2000) Enzyme and Microbial Technology , vol.27 , Issue.3-5 , pp. 325-329
    • Azevedo, H.1    Bishop, D.2    Cavaco-Paulo, A.3
  • 8
    • 0019554715 scopus 로고
    • INDUCTION, ISOLATION AND TESTING OF STALE TRICHODERMA REESEI MUTANTS WITH IMPROVED PRODUCTION OF SOLUBILIZING CELLULASE
    • DOI 10.1016/0141-0229(81)90076-4
    • Bailey, M. and Nevalainen, H. 1981. Induction, isolation and testing of stable Trichoderma reesei mutants with improved production of solubiling cellulase. Enzyme Microb. Technol. 3:153-157. (Pubitemid 11495110)
    • (1981) Enzyme and Microbial Technology , vol.3 , Issue.2 , pp. 153-157
    • Bailey, M.J.1    Nevalainen, K.M.H.2
  • 9
    • 14744272350 scopus 로고
    • Cloning and amplification of the gene encoding an extracellular β-glucosidase from Trichoderma reesei: Evidence for improved rates of saccharification of cellulosic substrates
    • Barnett, C., Berka, R. and Fowler, T. 1991. Cloning and amplification of the gene encoding an extracellular β-glucosidase from Trichoderma reesei: evidence for improved rates of saccharification of cellulosic substrates. Bio/Technology 9:562-567.
    • (1991) Bio/Technology , vol.9 , pp. 562-567
    • Barnett, C.1    Berka, R.2    Fowler, T.3
  • 10
    • 0030065736 scopus 로고    scopus 로고
    • Identification of two functionally different classes of exocellulases
    • DOI 10.1021/bi9520388
    • Barr, B., Hsieh, Y.-L., Ganem, B. and Wilson, D. 1996. Identification of two functionally different classes of exocellulases. Biochemistry 35:586-592. (Pubitemid 26032711)
    • (1996) Biochemistry , vol.35 , Issue.2 , pp. 586-592
    • Barr, B.K.1    Hsieh, Y.-L.2    Ganem, B.3    Wilson, D.B.4
  • 11
    • 84884710555 scopus 로고    scopus 로고
    • Bacillus cellulase and its applications
    • Pat. EP 0 739 982 A1
    • van Beckhoven, R., Lenting, H., Maurer, K.-H. and Weiss, A. 1996. Bacillus cellulase and its applications. Pat. EP 0 739 982 A1.
    • (1996)
    • Van Beckhoven, R.1    Lenting, H.2    Maurer, K.-H.3    Weiss, A.4
  • 12
    • 0035940050 scopus 로고    scopus 로고
    • Biostoning of denims by Penicillium occitanis (Pol6) cellulases
    • DOI 10.1016/S0168-1656(01)00309-1, PII S0168165601003091
    • Belghith, H., Ellouz-Chaabouni, S. and Gargouri, A. 2001. Biostoning of denims by Penicillium occitanis (Pol6) cellulases. J. Biotechnol. 89:257-262. (Pubitemid 32739064)
    • (2001) Journal of Biotechnology , vol.89 , Issue.2-3 , pp. 257-262
    • Belghith, H.1    Ellouz-Chaabouni, S.2    Gargouri, A.3
  • 13
    • 0036595947 scopus 로고    scopus 로고
    • Expression of xylanase enzymes from thermophilic microorganisms in fungal hosts
    • DOI 10.1007/s00792-001-0252-5
    • Bergquist, P., Te'o, V., Gibbs, M., Cziferszky, A., de Faria, F., Azevedo, M. and Nevalainen, H. 2002. Expression of xylanase enzymes from thermophilic microorganisms in fungal hosts. Extremophiles 6:177-184. (Pubitemid 41490466)
    • (2002) Extremophiles , vol.6 , Issue.3 , pp. 177-184
    • Bergquist, P.1    Te'o, V.2    Gibbs, M.3    Cziferszky, A.4    De Faria, F.P.5    Azevedo, M.6    Nevalainen, H.7
  • 14
    • 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. 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
  • 15
    • 0002797974 scopus 로고    scopus 로고
    • An ultrastructural study of the interaction of a fungal endoglucanase from Humicola insolens with cotton fibres
    • Boisset, C., Chanzy, H., Schülein, M. and Henrissat, B. 1997. A untrastructural study of the interaction of a fungal endoglucanase from Humicola insolens with cotton fibres. Cellulose 4:7-20. (Pubitemid 127508288)
    • (1997) Cellulose , vol.4 , Issue.1 , pp. 7-20
    • Boisset, C.1    Chanzy, H.2    Schulein, M.3    Henrissat, B.4
  • 16
    • 0035443118 scopus 로고    scopus 로고
    • Glycoside hydrolases and glycosyltransferases: Families and functional modules
    • DOI 10.1016/S0959-440X(00)00253-0
    • Bourne, Y. and Henrissat, B. 2001. Glycoside hydrolases and glycosyltransferases: families and functional modules. Curr. Opin. Struct. Biol. 11:593-600. (Pubitemid 32972023)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.5 , pp. 593-600
    • Bourne, Y.1    Henrissat, B.2
  • 18
    • 79951699104 scopus 로고    scopus 로고
    • High molecular weight Trichoderma cellulase
    • Pat. WO 98/15619, PCT/US97/18402
    • Bower, B., Clarkson, K., Collier, K., Kellis, J., Kelly, M. and Larenas, E. 1998a. High molecular weight Trichoderma cellulase. Pat. WO 98/15619, PCT/US97/18402.
    • (1998)
    • Bower, B.1    Clarkson, K.2    Collier, K.3    Kellis, J.4    Kelly, M.5    Larenas, E.6
  • 19
    • 74349124047 scopus 로고    scopus 로고
    • Hyperexpression and glycosylation of Trichoderma reesei EGIII
    • Claeyssens, M., Nerinckx, W. and Piens, K. (eds.) Carbohydrates from Trichoderma reesei and other microorganisms. The Royal Society of Chemistry. Cambridge, UK
    • Bower, B., Kodama, K., Swanson, B., Fowler, T., Meerman, H., Collier, K., Mitchinson, C. and Ward, M. 1998b. Hyperexpression and glycosylation of Trichoderma reesei EGIII. In: Claeyssens, M., Nerinckx, W. and Piens, K. (eds.) Carbohydrates from Trichoderma reesei and other microorganisms. Structures, biochemistry, genetics and applications. The Royal Society of Chemistry. Cambridge, UK. Pp. 328-334.
    • (1998) Structures, Biochemistry, Genetics and Applications , pp. 328-334
    • Bower, B.1    Kodama, K.2    Swanson, B.3    Fowler, T.4    Meerman, H.5    Collier, K.6    Mitchinson, C.7    Ward, M.8
  • 20
    • 0009867423 scopus 로고    scopus 로고
    • New cellulase processes for the textile industry
    • EU-project report
    • Buchert, J. and Heikinheimo, L. 1998. New cellulase processes for the textile industry. EU-project report. Carbohydr. Eur. 22:32-34.
    • (1998) Carbohydr. Eur. , vol.22 , pp. 32-34
    • Buchert, J.1    Heikinheimo, L.2
  • 22
    • 0025942151 scopus 로고
    • Double-antibody sandwich enzyme-linked immunosorbent assay for quantification of endoglucanase I of Trichoderma reesei
    • Bühler, R. 1991. Double-antibody sandwich enzyme-linked immunosorbent assay for quantification of endoglucanase I of Trichoderma reesei. Appl. Environ. Microbiol. 57:3317-3321.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 3317-3321
    • Bühler, R.1
  • 24
    • 84998186751 scopus 로고    scopus 로고
    • Improving dimensional stability of cotton fabrics with cellulase enzymes
    • Cavaco-Paulo, A. 2001. Improving dimensional stability of cotton fabrics with cellulase enzymes. Textile Res. J. 71:842-843.
    • (2001) Textile Res. J. , vol.71 , pp. 842-843
    • Cavaco-Paulo, A.1
  • 25
    • 84942082550 scopus 로고    scopus 로고
    • Catalysis and processing
    • Cavaco-Paulo, A. and Gübitz, G. (eds.) Woodhead Publishing Ltd., England
    • Cavaco-Paulo, A. and Gübitz, G. 2003. Catalysis and processing. In: Cavaco-Paulo, A. and Gübitz, G. (eds.) Textile processing with enzymes. Woodhead Publishing Ltd., England. Pp. 86-119.
    • (2003) Textile Processing with Enzymes , pp. 86-119
    • Cavaco-Paulo, A.1    Gübitz, G.2
  • 26
    • 0031803075 scopus 로고    scopus 로고
    • Hydrolysis of cotton cellulose by engineered cellulases from Trichoderma reesei
    • Cavaco-Paulo, A., Almeida, L. and Bishop, D. 1998a. Hydrolysis of cotton cellulose by engineered cellulases from Trichoderma reesei. Textile Res. J. 68:273-280.
    • (1998) Textile Res. J. , vol.68 , pp. 273-280
    • Cavaco-Paulo, A.1    Almeida, L.2    Bishop, D.3
  • 28
    • 0037134512 scopus 로고    scopus 로고
    • Elucidation of the metabolic rate of glucose in the filamentous fungus Trichoderma reesei using EST analysis and cDNA microarray
    • Chambergo, F., Bonaccorsi, E., Ferreira, A., Ramos, A., Ribamar, Ferreira J., Abrahao-Neto, J., Simon Farah, J. and El-Dorry, H. 2002. Elucidation of the metabolic rate of glucose in the filamentous fungus Trichoderma reesei using EST analysis and cDNA microarray. J. Biol. Chem. 277:13983-11388.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13983-111388
    • Chambergo, F.1    Bonaccorsi, E.2    Ferreira, A.3    Ramos, A.4    Ribamar, F.J.5    Abrahao-Neto, J.6    Simon Farah, J.7    El-Dorry, H.8
  • 29
    • 84884721402 scopus 로고
    • Cellulase induction in Myriococcum albomyces
    • Chung, D.H. 1971. Cellulase induction in Myriococcum albomyces. Han'guk Sikp'um Kwahakhoechi 3:1-5.
    • (1971) Han'guk Sikp'um Kwahakhoechi , vol.3 , pp. 1-5
    • Chung, D.H.1
  • 30
    • 84884716153 scopus 로고    scopus 로고
    • CIRFS, The International Rayon and Synthetic fibres Committee. 2002, Year Book
    • CIRFS, The International Rayon and Synthetic fibres Committee. 2002, Year Book.
  • 31
    • 84884713448 scopus 로고
    • Methods for treating cotton-containing fabrics with cellulase low in cellobiohydrolases
    • Pat. WO 92/17574
    • Clarkson, K., Larenas, E. and Weiss, G. 1992a. Methods for treating cotton-containing fabrics with cellulase low in cellobiohydrolases. Pat. WO 92/17574.
    • (1992)
    • Clarkson, K.1    Larenas, E.2    Weiss, G.3
  • 32
    • 84884707158 scopus 로고
    • Methods for treating cotton-containing fabrics with cellulase free of exo-cellobiohydrolase, and the treated fabrics
    • Pat. WO 92/17572
    • Clarkson, K., Larenas, E. and Weiss, G. 1992b. Methods for treating cotton-containing fabrics with cellulase free of exo-cellobiohydrolase, and the treated fabrics. Pat. WO 92/17572.
    • (1992)
    • Clarkson, K.1    Larenas, E.2    Weiss, G.3
  • 33
    • 84884713448 scopus 로고
    • Methods for treating cotton-containing fabrics with cellulase
    • Pat. WO 92/06183
    • Clarkson, K., Larenas, E. and Weiss, G. 1992c. Methods for treating cotton-containing fabrics with cellulase. Pat. WO 92/06183.
    • (1992)
    • Clarkson, K.1    Larenas, E.2    Weiss, G.3
  • 34
    • 0442320929 scopus 로고
    • Methods for treating cotton-containing fabrics with CBHI enriched cellulase
    • Pat. WO 93/22428
    • Clarkson, K., Collier, K., Lad, P. and Weiss, G. 1993. Methods for treating cotton-containing fabrics with CBHI enriched cellulase. Pat. WO 93/22428.
    • (1993)
    • Clarkson, K.1    Collier, K.2    Lad, P.3    Weiss, G.4
  • 35
    • 84884723834 scopus 로고
    • Methods for stonewashing fabrics using endoglucanases
    • Pat. WO 94/07983
    • Clarkson, K., Larenas, E., Weiss, G. and Bower, B. 1994a. Methods for stonewashing fabrics using endoglucanases. Pat. WO 94/07983.
    • (1994)
    • Clarkson, K.1    Larenas, E.2    Weiss, G.3    Bower, B.4
  • 36
    • 84884725104 scopus 로고
    • Method for reducing lint generation during treatment of cotton-containing and non-cotton-containing cellulosic fabric
    • Pat. WO 94/23113
    • Clarkson, K., Larenas, E. and Weiss, G. 1994b. Method for reducing lint generation during treatment of cotton-containing and non-cotton-containing cellulosic fabric. Pat. WO 94/23113.
    • (1994)
    • Clarkson, K.1    Larenas, E.2    Weiss, G.3
  • 38
    • 0035571505 scopus 로고    scopus 로고
    • The secretion pathway in filamentous fungi: A biotechnological view
    • DOI 10.1006/fgbi.2001.1276
    • Conesa, A., Punt, P., van Luijk, N. and van den Hondel, C. 2001. The secretion pathway in filamentous fungi: A biotechnological view. Fungal Genet. Biol. 33:155-171. (Pubitemid 34229801)
    • (2001) Fungal Genetics and Biology , vol.33 , Issue.3 , pp. 155-171
    • Conesa, A.1    Punt, P.J.2    Van Luijk, N.3    Van Den, H.C.A.M.J.J.4
  • 39
    • 0035940074 scopus 로고    scopus 로고
    • Cellulase finishing of woven, cotton fabrics in jet and winch machines
    • DOI 10.1016/S0168-1656(01)00307-8, PII S0168165601003078
    • Cortez, J., Ellis, J. and Bishop, D. 2001. Cellulase finishing of woven, cotton fabrics in jet and winch machines. J. Biotechnol. 89:239-245. (Pubitemid 32739062)
    • (2001) Journal of Biotechnology , vol.89 , Issue.2-3 , pp. 239-245
    • Cortez, J.M.1    Ellis, J.2    Bishop, D.P.3
  • 40
    • 0036687083 scopus 로고    scopus 로고
    • Using cellulases to improve the dimensional stability of cellulosic fabrics
    • Cortez, J., Ellis, J. and Bishop, D. 2002. Using cellulases to improve the dimensional stability of cellulosic fabric. Textile Res. J. 72:673-680. (Pubitemid 34961542)
    • (2002) Textile Research Journal , vol.72 , Issue.8 , pp. 673-680
    • Cortez, J.M.1    Ellis, J.2    Bishop, D.P.3
  • 41
    • 0028217921 scopus 로고
    • A novel method for efficient expression cloning of fungal enzyme genes
    • DOI 10.1007/BF00301060
    • Dalboge, H. and Heldt-Hansen, H.P. 1994. A novel method for efficient expression cloning of fungal enzyme genes. Mol. Gen. Genet. 243:253-260. (Pubitemid 24151984)
    • (1994) Molecular and General Genetics , vol.243 , Issue.3 , pp. 253-260
    • Dalboge, H.1    Heldt-Hansen, H.P.2
  • 42
    • 0028822343 scopus 로고
    • Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9-angstöm resolution
    • Davies, G., Tolley, S., Henrissat, B., Hjort, C. and Schülein, M. 1995. Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9-angstöm resolution. Biochemistry 34:16210-16220.
    • (1995) Biochemistry , vol.34 , pp. 16210-16220
    • Davies, G.1    Tolley, S.2    Henrissat, B.3    Hjort, C.4    Schülein, M.5
  • 43
    • 0027968302 scopus 로고
    • The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei
    • Divne, C., Ståhlberg, J., Reinikainen, T., Ruohonen, L., Pettersson, G., Knowles, J., Teeri, T. and Jones, A. 1994. The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science 265:524-528. (Pubitemid 24264997)
    • (1994) Science , vol.265 , Issue.5171 , pp. 524-528
    • Divne, C.1    Stahlberg, J.2    Reinikainen, T.3    Ruohonen, L.4    Pettersson, G.5    Knowles, J.K.C.6    Teeri, T.T.7    Jones, T.A.8
  • 44
    • 0024035173 scopus 로고
    • Genetic improvement of Trichoderma reesei for large scale cellulase production
    • Durand, H., Clanet, M. and Tiraby, G. 1988a. Genetic improvement of Trichoderma reesei for large scale cellulase production. Enzyme Microb. Technol. 10:341-345.
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 341-345
    • Durand, H.1    Clanet, M.2    Tiraby, G.3
  • 45
    • 0000129443 scopus 로고
    • Classical and molecular genetics applied to Trichoderma reesei for the selection of improved cellulolytic industrial strains
    • Aubert, J., Benguin, P. and Millet, J. (eds). Academic Press, New York
    • Durand, H., Baron, M., Calmels, T and Tiraby, G. 1988b. Classical and molecular genetics applied to Trichoderma reesei for the selection of improved cellulolytic industrial strains. In: Aubert, J., Benguin, P. and Millet, J. (eds). Biochemistry and Genetics of cellulose degradation. Academic Press, New York. Pp. 135-151.
    • (1988) Biochemistry and Genetics of Cellulose Degradation , pp. 135-151
    • Durand, H.1    Baron, M.2    Calmels, T.3    Tiraby, G.4
  • 46
    • 0025929094 scopus 로고
    • Production of cellulases by Myriococcum albomyces
    • El-Gindy, A. 1991. Production of cellulases by Myriococcum albomyces. Zentralblatt für Mikrobiologie 146:193-196.
    • (1991) Zentralblatt für Mikrobiologie , vol.146 , pp. 193-196
    • El-Gindy, A.1
  • 47
    • 0036151166 scopus 로고    scopus 로고
    • Expression and processing of a major xylanase (XYN2) from the thermophilic fungus Humicola grisea var. thermoidea in Trichoderma reesei
    • DOI 10.1046/j.1472-765x.2002.01057.x
    • de Faria, F., Te'o, V., Berquist, P., Azevedo, M. and Nevalainen, H. 2002. Expression and processing of a major xylanase (XYN2) from the thermophilic fungus Humicola grisea var. thermoidea in Trichoderma reesei. Lett. Appl. Microbiol. 34:119-123. (Pubitemid 34094029)
    • (2002) Letters in Applied Microbiology , vol.34 , Issue.2 , pp. 119-123
    • De Faria, F.P.1    Te'O, V.S.J.2    Bergquist, P.L.3    Azevedo, M.O.4    Nevalainen, K.M.H.5
  • 48
    • 84884711691 scopus 로고    scopus 로고
    • Compositions and methods for treating cellulose containing fabrics using truncated cellulase enzyme compositions
    • Pat. US 6,294,366
    • Farrington, G., Anderson, P., Bergquist, P., Daniels, R., Moreland, D., Morgan H. and Williams, D. 2001. Compositions and methods for treating cellulose containing fabrics using truncated cellulase enzyme compositions. Pat. US 6,294,366.
    • (2001)
    • Farrington, G.1    Anderson, P.2    Bergquist, P.3    Daniels, R.4    Moreland, D.5    Morgan, H.6    Williams, D.7
  • 50
    • 84884722824 scopus 로고    scopus 로고
    • Method and compositions for treating cellulose containing fabrics using truncated cellulase enzyme compositions
    • Pat. US 6,268,196
    • Fowler, T., Clarkson, K., Ward, M., Collier, K. and Larenas, E. 2001. Method and compositions for treating cellulose containing fabrics using truncated cellulase enzyme compositions. Pat. US 6,268,196.
    • (2001)
    • Fowler, T.1    Clarkson, K.2    Ward, M.3    Collier, K.4    Larenas, E.5
  • 53
    • 0031054007 scopus 로고    scopus 로고
    • Efficient production of secreted proteins by Aspergillus: Progress, limitations and prospects
    • DOI 10.1007/s002530050880
    • Gouka, R., Punt, P. and van den Hondel. 1997. Efficient production of secreted proteins by Aspergillus: progress, limitations and prospects. Appl. Microbiol. Biotechnol. 47:1-11. (Pubitemid 27077292)
    • (1997) Applied Microbiology and Biotechnology , vol.47 , Issue.1 , pp. 1-11
    • Gouka, R.J.1    Punt, P.J.2    Van Den, H.C.A.M.J.J.3
  • 54
    • 0001051337 scopus 로고
    • The cellulase system of Trichoderma. The relationship between purified extracellular enzymes from unduced or cellulose-grown cells
    • Gritzali, M. and Brown, R.D.Jr. 1979. The cellulase system of Trichoderma. The relationship between purified extracellular enzymes from unduced or cellulose-grown cells. Adv. Chem. Ser. 81:237-260.
    • (1979) Adv. Chem. Ser. , vol.81 , pp. 237-260
    • Gritzali, M.1    Brown Jr., R.D.2
  • 57
    • 0033790321 scopus 로고    scopus 로고
    • A comparative study of different cellulase preparations in the enzymatic treatments of cotton fabrics
    • Gusakov, A., Berlin, A., Popova, N., Okunev, O., Sinitsyna, O. and Sinitsyn, A. 2000a. A comparative study of different cellulase preparations in the enzymatic treatments of cotton fabrics. Appl. Biochem. Biotechnol. 88:119-126.
    • (2000) Appl. Biochem. Biotechnol. , vol.88 , pp. 119-126
    • Gusakov, A.1    Berlin, A.2    Popova, N.3    Okunev, O.4    Sinitsyna, O.5    Sinitsyn, A.6
  • 58
    • 0034669395 scopus 로고    scopus 로고
    • Surface hydrophobic amino acid residues in cellulase molecules as a structural factor responsible for their high denim-washing performance
    • Gusakov, A., Sinitsyn, A., Berlin, A., Markov, A. and Ankudimova, N. 2000b. Surface hydrophobic amino acid residues in cellulase molecules as a structural factor responsible for their high denim-washing performance. Enzyme Microb. Technol. 27:664-671.
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 664-671
    • Gusakov, A.1    Sinitsyn, A.2    Berlin, A.3    Markov, A.4    Ankudimova, N.5
  • 60
    • 0034074839 scopus 로고    scopus 로고
    • Rapid transformation of high cellulase-producing mutant strains of Trichoderma reesei by microprojectile bombardment
    • Hazell, B., Te'o, V., Bradner, J., Bergquist, P. and Nevalainen, H. 2000. Rapid transformation of high secreting mutant strains of Trichoderma reesei by microprojectile bombardment. Lett. Appl. Microbiol. 30:282-286. (Pubitemid 30209781)
    • (2000) Letters in Applied Microbiology , vol.30 , Issue.4 , pp. 282-286
    • Hazell, B.W.1    Te'o, V.S.J.2    Bradner, J.R.3    Bergquist, P.L.4    Nevalainen, K.M.H.5
  • 61
    • 0035424387 scopus 로고    scopus 로고
    • Synergistic effects of Trichoderma reesei cellulases on the properties of knitted cotton fabric
    • Heikinheimo, L. and Buchert, J. 2001. Synergistic effects of Trichoderma reesei cellulases on the properties of knitted cotton fabric. Textile Res. J. 71:672-677. (Pubitemid 32722879)
    • (2001) Textile Research Journal , vol.71 , Issue.8 , pp. 672-677
    • Heikinheimo, L.1    Buchert, J.2
  • 64
    • 0142027913 scopus 로고    scopus 로고
    • Effect of purified Trichoderma reesei cellulases on formation of cotton powder from cotton fabric
    • Heikinheimo, L., Miettinen-Oinonen, A., Cavaco-Paulo, A. and Buchert, J. Effect of purified Trichoderma reesei cellulases on formation of cotton powder from cotton fabric. J. Appl. Polymer Sci. 90:917-1922.
    • J. Appl. Polymer Sci. , vol.90 , pp. 917-1922
    • Heikinheimo, L.1    Miettinen-Oinonen, A.2    Cavaco-Paulo, A.3    Buchert, J.4
  • 65
    • 0000590673 scopus 로고
    • Hydrolysis of barley (1→3), (1→4)-β-D-glucan by a cellobiohydrolase II preparation from Trichoderma reesei
    • Henriksson, K., Teleman, A., Suortti, T., Reinikainen, T., Jaskari, J., Teleman, O. and Poutanen, K. 1995. Hydrolysis of barley (1→3), (1→4)-β-D-glucan by a cellobiohydrolase II preparation from Trichoderma reesei. Carbohydr. Polym. 26:109-119.
    • (1995) Carbohydr. Polym. , vol.26 , pp. 109-119
    • Henriksson, K.1    Teleman, A.2    Suortti, T.3    Reinikainen, T.4    Jaskari, J.5    Teleman, O.6    Poutanen, K.7
  • 66
    • 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
  • 67
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and Bairoch, A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293:781-788. (Pubitemid 23244564)
    • (1993) Biochemical Journal , vol.293 , Issue.3 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 68
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases [1]
    • Henrissat, B. and Bairoch, A. 1996. Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316:695-696. (Pubitemid 26182174)
    • (1996) Biochemical Journal , vol.316 , Issue.2 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 69
    • 0032571552 scopus 로고    scopus 로고
    • A scheme for designating enzymes that hydrolyse the polysaccharides in the cell walls of plants
    • DOI 10.1016/S0014-5793(98)00265-8, PII S0014579398002658
    • Henrissat, B., Teeri, T. and Warren, R. 1998. A scheme for designating enzymes that hydrolyse the polysaccharides in the cell walls of plants. FEBS Letters 425:352-354. (Pubitemid 28178920)
    • (1998) FEBS Letters , vol.425 , Issue.2 , pp. 352-354
    • Henrissat, B.1    Teeri, T.T.2    Warren, R.A.J.3
  • 70
    • 0033179622 scopus 로고    scopus 로고
    • Cellulase for commodity products from cellulosic biomass
    • DOI 10.1016/S0958-1669(99)80065-2
    • Himmel, M., Ruth, M. and Wyman, C. 1999. Cellulase for commodity products from cellulosic biomass. Curr. Opin. Biotechnol. 10:358-364. (Pubitemid 29373950)
    • (1999) Current Opinion in Biotechnology , vol.10 , Issue.4 , pp. 358-364
    • Himmel, M.E.1    Ruth, M.F.2    Wyman, C.E.3
  • 71
    • 0036008521 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of a family 45 endoglucanase from the thermophilic fungus Melanocarpus albomyces
    • DOI 10.1107/S0907444901020236
    • Hirvonen, M. and Papageorgiou, A. 2002. Crystallization and preliminary crystallographic analysis of a family 45 endoglucanase from the thermophilic fungus Melanocarpus albomyces. Acta Cryst. D58:336-338. (Pubitemid 34179215)
    • (2002) Acta Crystallographica Section D: Biological Crystallography , vol.58 , Issue.2 , pp. 336-338
    • Hirvonen, M.1    Papageorgiou, A.C.2
  • 72
    • 0030036051 scopus 로고    scopus 로고
    • The glucose repressor gene cre1 of Trichoderma: Isolation and expression of a full-length and a tuncated 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 tuncated 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
  • 73
    • 0030944352 scopus 로고    scopus 로고
    • Regulation of cellulase gene expression in the filamentous fungus Trichoderma reesei
    • Ilmén, M., Saloheimo, A., Onnela, M.-L. and Penttilä, M. 1997. Regulation of cellulase gene expression in the filamentous fungus Trichoderma reesei. Appl. Environ. Microbiol. 63:1298-1306. (Pubitemid 27174831)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.4 , pp. 1298-1306
    • Ilmen, M.1    Saloheimo, A.2    Onnela, M.-L.3    Penttila, M.E.4
  • 74
    • 0036968875 scopus 로고    scopus 로고
    • Recent studies of protein secretion by filamentous fungi
    • DOI 10.1016/S1389-1723(02)80191-8
    • Iwashita, K. 2002. Recent studied of protein secretion by filamentous fungi. J. Biosci. Bioeng. 94:530-535. (Pubitemid 36132551)
    • (2002) Journal of Bioscience and Bioengineering , vol.94 , Issue.6 , pp. 530-535
    • Iwashita, K.1
  • 75
    • 0027367915 scopus 로고
    • Transformation of Trichoderma reesei with the Hormoconis resinae glucoamylase P (gamP) gene: Production of a heterologous glucoamylase by Trichoderma reesei
    • Joutsjoki, V., Torkkeli, T. and Nevalainen, H. 1993. Transformation of Trichoderma reesei with the Hormoconis resinae glucoamylase P (gamP) gene: production of a heterologous glucoamylase by Trichoderma reesei. Curr. Genet. 24:223-228. (Pubitemid 23294053)
    • (1993) Current Genetics , vol.24 , Issue.3 , pp. 223-228
    • Joutsjoki, V.V.1    Torkkeli, T.K.2    Nevalainen, K.M.H.3
  • 76
    • 0027138808 scopus 로고
    • High frequency one-step gene replacement in Trichoderma reesei. I. Endoglucanase I overproduction
    • DOI 10.1007/BF00279893
    • Karhunen, T., Mäntylä, A., Nevalainen, H. and Suominen, P. 1993. High frequency one-step replacement in Trichoderma reesei. I. Endoglucanase I overproduction. Mol. Gen. Genet. 241:515-522. (Pubitemid 24003870)
    • (1993) Molecular and General Genetics , vol.241 , Issue.5-6 , pp. 515-522
    • Karhunen, T.1    Mantyla, A.2    Nevalainen, K.M.H.3    Suominen, P.L.4
  • 78
    • 0036310984 scopus 로고    scopus 로고
    • Purification and characterisation of a novel laccase from the ascomycete Melanocarpus albomyces
    • DOI 10.1007/s00253-002-1012-x
    • Kiiskinen, L.-L., Viikari, L. and Kruus, K. 2002. Purification and characterization of a novel laccase from the ascomycete Melanocarpus albomyces. Appl. Microbiol. Biotechnol. 59:198-204. (Pubitemid 34756959)
    • (2002) Applied Microbiology and Biotechnology , vol.59 , Issue.2-3 , pp. 198-204
    • Kiiskinen, L.-L.1    Viikari, L.2    Kruus, K.3
  • 79
    • 4844228512 scopus 로고    scopus 로고
    • Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme
    • DOI 10.1099/mic.0.27147-0
    • Kiiskinen, L.-L., Kruus, K., Bailey, M., Ylösmäki, E., Siika-aho, M. and Saloheimo, M. 2004. Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme. Microbiology 150:3065-3074. (Pubitemid 39317807)
    • (2004) Microbiology , vol.150 , Issue.9 , pp. 3065-3074
    • Kiiskinen, L.-L.1    Kruus, K.2    Bailey, M.3    Ylosmaki, E.4    Siika-aho, M.5    Saloheimo, M.6
  • 81
  • 82
    • 0029743877 scopus 로고    scopus 로고
    • The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size
    • Kleman-Leyer, K., Siika-aho, M., Teeri, T. and Kirk, K. 1996. The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synegistically to solubilize native cotton cellulose but not to decrease its molecular size. Appl. Environ. Microbiol. 62:2883-2887. (Pubitemid 26260095)
    • (1996) Applied and Environmental Microbiology , vol.62 , Issue.8 , pp. 2883-2887
    • Kleman-Leyer, K.M.1    Siika-Aho, M.2    Teeri, T.T.3    Kent, K.T.4
  • 83
    • 0025112195 scopus 로고
    • Optimizing processing conditions in enzymatic stonewashing
    • September: 24-28
    • Kochavi, D., Videbaek, T. and Cedroni, D. 1990. Optimizing processing conditions in enzymatic stonewashing. American Dyestuff Reporter September: 24-28.
    • (1990) American Dyestuff Reporter
    • Kochavi, D.1    Videbaek, T.2    Cedroni, D.3
  • 85
    • 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, P., Clore, G., Nilges, M., Jones, A., Pettersson, G., Knowles, J. and Gronenborn, A. 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, P.1    Clore, G.2    Nilges, M.3    Jones, A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.7
  • 86
    • 0033020387 scopus 로고    scopus 로고
    • Overexpression of the Saccharomyces cerevisiae mannosylphosphodolichol synthase-encoding gene in Trichoderma reesei results in an increased level of protein secretion and abnormal ultrastructure
    • Kruszewska, J., Butterweck, A., Kurzatkowski, W., Migdalski, A., Kubicek, C. and Palamarczyk, G. 1999. Overexpression of the Saccharomyces cerevisiae mannosylphosphodolichol synthase-encoding gene in Trichoderma reesei results in an increased level of protein secretion and abnormal ultrastructure. Appl. Environ. Microbiol. 65:2382-2387.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2382-2387
    • Kruszewska, J.1    Butterweck, A.2    Kurzatkowski, W.3    Migdalski, A.4    Kubicek, C.5    Palamarczyk, G.6
  • 88
    • 0000358186 scopus 로고
    • O-linked - but not N-linked - glycosylation is necessary for endolucanase I and II secretion by Trichoderma reesei
    • Kubicek, C., Panda, T., Schreferl-Kunar, G., Gruber, F. and Messner, R. 1987. O-linked - but not N-linked - glycosylation is necessary for endolucanase I and II secretion by Trichoderma reesei. Can. J. Microbiol. 33:698-703.
    • (1987) Can. J. Microbiol. , vol.33 , pp. 698-703
    • Kubicek, C.1    Panda, T.2    Schreferl-Kunar, G.3    Gruber, F.4    Messner, R.5
  • 89
    • 0027551663 scopus 로고
    • The Trichoderma cellulase regulatory puzzle: From the interior life of a secretory fungus
    • DOI 10.1016/0141-0229(93)90030-6
    • Kubicek, C., Messner, R., Gruber, F., Mach, R. and Kubicek-Pranz, E. 1993. The Trichoderma cellulase regulatory puzzle: from the interior life of a secretory fungus. Enzyme Microb. Technol. 15:90-99. (Pubitemid 23045759)
    • (1993) Enzyme and Microbial Technology , vol.15 , Issue.2 , pp. 90-99
    • Kubicek, C.P.1    Messner, R.2    Gruber, F.3    Mach, R.L.4    Kubicek-Pranz, E.M.5
  • 90
    • 0025816748 scopus 로고
    • Transformation of Trichoderma reesei with the cellobiohydrolase II gene as a means for obtaining strains with increase cellulase production and specific activity
    • Kubicek-Pranz, E., Gruber, F. and Kubicek, C. 1991. Transformation of Trichoderma reesei with the cellobiohydrolase II gene as a means for obtaining strains with increase cellulase production and specific activity. J. Biotech. 20:83-94.
    • (1991) J. Biotech. , vol.20 , pp. 83-94
    • Kubicek-Pranz, E.1    Gruber, F.2    Kubicek, C.3
  • 91
    • 0029839467 scopus 로고    scopus 로고
    • Molecular evidence that the asexual industrial fungus Trichoderma reesei is a clonal derivative of the ascomycete Hypocrea jecorina
    • Kuhls, K., Lieckfeldt, E., Samuels, G., Kovacs, W., Meyer, W., Petrini, O., Gams, W., Börner, T. and Kubicek, C. 1996. Molecular evidence that the asexual industrial fungus Trichoderma reesei is a clonal derivative of the ascomycete Hypocrea jecorina. Proc. Natl. Acad. Sci. 93:7755-7760.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 7755-7760
    • Kuhls, K.1    Lieckfeldt, E.2    Samuels, G.3    Kovacs, W.4    Meyer, W.5    Petrini, O.6    Gams, W.7    Börner, T.8    Kubicek, C.9
  • 92
    • 0031121058 scopus 로고    scopus 로고
    • Optimizing the use of cellulase enzymes in finishing cellulosic fabrics
    • Kumar, A., Yoon, M.-Y. and Purtell, C. 1997. Optimizing the use of cellulase enzymes in finishing cellulosic fabrics. Textile Chemist and Colorist 29:37-42. (Pubitemid 127772198)
    • (1997) Textile Chemist and Colorist , vol.29 , Issue.4 , pp. 37-42
    • Kumar, A.1    Yoon, M.-Y.2    Purtell, C.3
  • 93
    • 53549133473 scopus 로고    scopus 로고
    • Polypeptides having cellobiohydrolase I activity and polynucleotides encoding same
    • Pat. WO 03/000941
    • Lange, L., Wu, W., Aubert, D., Landvik, S., Schnorr, K. and Clausen, I. 2003. Polypeptides having cellobiohydrolase I activity and polynucleotides encoding same. Pat. WO 03/000941.
    • (2003)
    • Lange, L.1    Wu, W.2    Aubert, D.3    Landvik, S.4    Schnorr, K.5    Clausen, I.6
  • 94
    • 0035940077 scopus 로고    scopus 로고
    • Guidelines to come to minimized tensile strength loss upon cellulase application
    • DOI 10.1016/S0168-1656(01)00301-7, PII S0168165601003017
    • Lenting, H. and Warmoeskerken, M. 2001. Guidelines to come to minimized tensile strength loss upon cellulase application. J. Biotechnol. 89:227-232. (Pubitemid 32739060)
    • (2001) Journal of Biotechnology , vol.89 , Issue.2-3 , pp. 227-232
    • Lenting, H.B.M.1    Warmoeskerken, M.M.C.G.2
  • 95
    • 0035406437 scopus 로고    scopus 로고
    • Proteins associated with the cell envelope of Trichoderma reesei: A proteomic approach
    • Lim, D., Hains, P., Walsh, B., Bergquist, P. and Nevalainen, H. 2001. Proteins associated with the cell envelope of Trichoderma reesei: A proteomic approach. Proteomics 1:899-910. (Pubitemid 33587415)
    • (2001) Proteomics , vol.1 , Issue.7 , pp. 899-910
    • Dongbin, L.1    Hains, P.2    Walsh, B.3    Bergquist, P.4    Nevalainen, H.5
  • 96
    • 0343247806 scopus 로고    scopus 로고
    • The roles and function of cellulose-binding domains
    • DOI 10.1016/S0168-1656(97)00087-4, PII S0168165697000874
    • Linder, M. and Teeri, T. 1997. The roles and function of cellulose-binding domains. J. Biotechnol. 57:15-28. (Pubitemid 27397467)
    • (1997) Journal of Biotechnology , vol.57 , Issue.1-3 , pp. 15-28
    • Linder, M.1    Teeri, T.T.2
  • 98
  • 99
    • 84884713680 scopus 로고    scopus 로고
    • A method of obtaining a cellulosic textile fabric with reduced tendency to pilling formation
    • Pat. WO 96/17994
    • Lund, H. and Pedersen, H. 1996. A method of obtaining a cellulosic textile fabric with reduced tendency to pilling formation. Pat. WO 96/17994.
    • (1996)
    • Lund, H.1    Pedersen, H.2
  • 100
    • 84884715763 scopus 로고    scopus 로고
    • A process for combined desizing and "stone-washing" of dyed denim
    • Pat. WO 97/18286
    • Lund, H. 1997. A process for combined desizing and "stone- washing" of dyed denim. Pat. WO 97/18286.
    • (1997)
    • Lund, H.1
  • 102
    • 27144505347 scopus 로고    scopus 로고
    • Genetic transformation of Trichoderma and Gliocladium
    • Kubicek, C. and Harman, G. (eds.)
    • Mach, R. and Zeilinger, S. 1998. Genetic transformation of Trichoderma and Gliocladium. In: Kubicek, C. and Harman, G. (eds.) Trichoderma & Gliocladium, Basic biology, taxonomy and genetics, Vol. 1. Pp. 225-242.
    • (1998) Trichoderma & Gliocladium, Basic Biology, Taxonomy and Genetics , vol.1 , pp. 225-242
    • Mach, R.1    Zeilinger, S.2
  • 103
    • 0037255672 scopus 로고    scopus 로고
    • Regulation of gene expression in industrial fungi: Trichoderma
    • Mach, R. and Zeilinger, S. 2003. Regulation of gene expression in industrial fungi: Trichoderma. Appl. Microbiol. Biotechnol. 60:515-522. (Pubitemid 36169525)
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.5 , pp. 515-522
    • Mach, R.L.1    Zeilinger, S.2
  • 104
    • 0032532639 scopus 로고    scopus 로고
    • Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 Å resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate
    • Mackenzie, L., Sulzenbacher, G., Divne, C., Jones, A., Wöldike, H., Schülein, M., Withers, S. and Davies, G. 1998. Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 Å resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate. Biochem. J. 335:409-416.
    • (1998) Biochem. J. , vol.335 , pp. 409-416
    • Mackenzie, L.1    Sulzenbacher, G.2    Divne, C.3    Jones, A.4    Wöldike, H.5    Schülein, M.6    Withers, S.7    Davies, G.8
  • 105
    • 0022401295 scopus 로고
    • Isolation and culture of a thermophilic fungus, Melanocarpus albomyces, and factors influencing the production and activity of xylanase
    • Maheshwari, R. and Kamalam, P. 1985. Isolation and culture of a thermophilic fungus, Melanocarpus albomyces, and factors influencing the production and activity of xylanase. J. Gen. Microbiol. 131:3017-3027. (Pubitemid 16202276)
    • (1985) Journal of General Microbiology , vol.131 , Issue.11 , pp. 3017-3027
    • Maheshwari, R.1    Kamalam, P.T.2
  • 107
    • 0017268658 scopus 로고
    • Measurement of saccharifying cellulase
    • Gaden, E.L., Mandels, M.H., Reese, E.T. and Spano, L.A. (eds.) John Wiley and Sons, New York
    • Mandels, M., Andreotti, R. and Roche, C. 1976. Measurement of saccharifying cellulase. In: Gaden, E.L., Mandels, M.H., Reese, E.T. and Spano, L.A. (eds.) Biotechnology and Bioengineering Symposium No 6. John Wiley and Sons, New York. Pp. 21-33.
    • (1976) Biotechnology and Bioengineering Symposium , Issue.6 , pp. 21-33
    • Mandels, M.1    Andreotti, R.2    Roche, C.3
  • 109
    • 0031695160 scopus 로고    scopus 로고
    • Solution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello-oligosaccharides
    • DOI 10.1046/j.1432-1327.1998.2560279.x
    • Mattinen, M.-J., Linder, M., Drakenberg, T. and Annila, A. 1998. Solution structure of the cellobiose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello-oligosaccharides. Eur. J. Biochem. 256:279-286. (Pubitemid 28404789)
    • (1998) European Journal of Biochemistry , vol.256 , Issue.2 , pp. 279-286
    • Mattinen, M.-L.1    Linder, M.2    Drakenberg, T.3    Annila, A.4
  • 110
    • 0000753948 scopus 로고    scopus 로고
    • Development of new cellulases
    • van Ee, J., Misset, O. and Baas, E. (eds.) Marcel Dekker, Inc., New York
    • Maurer, K.-H. 1997. Development of new cellulases. In: van Ee, J., Misset, O. and Baas, E. (eds.) Enzymes in detergency. Marcel Dekker, Inc., New York. Pp. 175-202.
    • (1997) Enzymes in Detergency , pp. 175-202
    • Maurer, K.-H.1
  • 112
    • 0031549642 scopus 로고    scopus 로고
    • Overexpression of the Aspergillus niger pH 2.5 acid phosphatase gene in a heterologous host Trichoderma reesei
    • DOI 10.1016/S0168-1656(97)00121-1, PII S0168165697001211
    • Miettinen-Oinonen, A., Torkkeli, T., Paloheimo, M. and Nevalainen H. 1997. Overexpression of the Aspergillus niger pH 2.5 acid phosphatase gene in a heterologous host Trichoderma reesei. J. Biotechnol. 58:13-20. (Pubitemid 27397460)
    • (1997) Journal of Biotechnology , vol.58 , Issue.1 , pp. 13-20
    • Miettinen-Oinonen, A.1    Torkkeli, T.2    Paloheimo, M.3    Helena, N.4
  • 114
    • 0004147654 scopus 로고    scopus 로고
    • Natural-cellulose fibres
    • The Textile Institute, Manchester
    • Morton, W. and Hearle, J. 1997. Natural-cellulose fibres. In: Physical properties of textile fibers. The Textile Institute, Manchester. Pp. 38-47.
    • (1997) Physical Properties of Textile Fibers , pp. 38-47
    • Morton, W.1    Hearle, J.2
  • 119
    • 0028787878 scopus 로고
    • Production of Trichoderma reesei cellulases on glucose-containing media
    • Nakari-Setälä, T. and Penttilä, M. 1995. Production of Trichoderma reesei cellulases on glucose-containing media. Appl. Environ. Microbiol. 61:3650-3655.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3650-3655
    • Nakari-Setälä, T.1    Penttilä, M.2
  • 120
    • 84884717199 scopus 로고
    • New Trichoderma promoters for production of hydrolytic enzymes on glucose medium
    • Suominen, P. and Reinikainen, T. (eds.) Foundation for Biotechnical and Industrial Fermentation Research, Espoo, Finland
    • Nakari-Setälä, T., Onnela, M.-L., Ilmén, M. and Penttilä, M. 1993. New Trichoderma promoters for production of hydrolytic enzymes on glucose medium. In: Suominen, P. and Reinikainen, T. (eds.) Proceedings of the 2nd TRICEL Symposium on Trichoderma reesei cellulases and other hydrolases. Foundation for Biotechnical and Industrial Fermentation Research, Espoo, Finland. Pp. 239-246.
    • (1993) Proceedings of the 2nd TRICEL Symposium on Trichoderma Reesei Cellulases and Other Hydrolases , pp. 239-246
    • Nakari-Setälä, T.1    Onnela, M.-L.2    Ilmén, M.3    Penttilä, M.4
  • 122
    • 77957053413 scopus 로고    scopus 로고
    • Strain improvement in filamentous fungi - An overview
    • Kchachatourians, G., Arora, D. (eds.) Elsevier, Amsterdam
    • Nevalainen, H. 2001. Strain improvement in filamentous fungi - an overview. In: Kchachatourians, G., Arora, D. (eds.) Applied mycology and biotechnology, Agriculture and food production. Elsevier, Amsterdam, Vol. 1. Pp. 289-304.
    • (2001) Applied Mycology and Biotechnology, Agriculture and Food Production , vol.1 , pp. 289-304
    • Nevalainen, H.1
  • 124
    • 0028113146 scopus 로고
    • On the safety of Trichoderma reesei
    • DOI 10.1016/0168-1656(94)90126-0
    • Nevalainen, H., Suominen, P. and Taimisto, K. 1994. On the safety of Trichoderma reesei. J. Biotechnol. 37:193-200. (Pubitemid 24355163)
    • (1994) Journal of Biotechnology , vol.37 , Issue.3 , pp. 193-200
    • Nevalainen, H.1
  • 126
    • 29544447668 scopus 로고    scopus 로고
    • Application of genetic engineering for strain improvement in filamentous fungi
    • Arora, D. (ed.). Marcel Dekker, Inc.
    • Nevalainen, H., Te'o, V. and Penttilä, M. 2004. Application of genetic engineering for strain improvement in filamentous fungi. In: Arora, D. (ed.). Handbook of fungal biotechnology. Marcel Dekker, Inc. Pp. 193-208.
    • (2004) Handbook of Fungal Biotechnology , pp. 193-208
    • Nevalainen, H.1    Te'O, V.2    Penttilä, M.3
  • 127
    • 84942087397 scopus 로고    scopus 로고
    • Process engineering and industrial enzyme applications
    • Cavaco-Paulo, A. and Gübitz, G. (eds.) Woodhead Publishing Ltd., England
    • Nierstrasz, V. and Warmoeskerken, M. 2003. Process engineering and industrial enzyme applications. In: Cavaco-Paulo, A. and Gübitz, G. (eds.) Textile processing with enzymes, Woodhead Publishing Ltd., England. Pp. 120-157.
    • (2003) Textile Processing with Enzymes , pp. 120-157
    • Nierstrasz, V.1    Warmoeskerken, M.2
  • 128
    • 0035187264 scopus 로고    scopus 로고
    • L-Sorbose induces cellulase gene transcription in the cellulolytic fungus Trichoderma reesei
    • DOI 10.1007/s002940000165
    • Nogawa, M., Goto, M., Okada, H. and Morikawa, Y. 2001. L-sorbose induces cellulase gene transcription in the cellulolytic fungus Trichoderma reesei. Curr. Genet. 38:329-334. (Pubitemid 32058725)
    • (2001) Current Genetics , vol.38 , Issue.6 , pp. 329-334
    • Nogawa, M.1    Goto, M.2    Okada, H.3    Morikawa, Y.4
  • 130
    • 0031890507 scopus 로고    scopus 로고
    • Molecular characterization and heterologous expression of the gene encoding a low-molecular-mass endoglucanase from Trichoderma reesei QM9414
    • Okada, H., Tada, K., Sekiya, T., Yokoyama, K., Takahashi, A., Tohda, H., Kumagai, H. and Morikawa, Y. 1998. Molecular characterization and heterologous expression of the gene encoding a low-molecular-mass endoglucanase from Trichoderma reesei QM9414. Appl. Environ. Microbiol. 64:555-563. (Pubitemid 28079821)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.2 , pp. 555-563
    • Okada, H.1    Tada, K.2    Sekiya, T.3    Yokoyama, K.4    Takahashi, A.5    Tohda, H.6    Kumagai, H.7    Morikawa, Y.8
  • 131
    • 84884715819 scopus 로고
    • Compositions and methods to vary color density
    • Pat. WO 90/02790
    • Oslon, L. and Stanley, P. 1990. Compositions and methods to vary color density. Pat. WO 90/02790.
    • (1990)
    • Oslon, L.1    Stanley, P.2
  • 132
    • 84884718705 scopus 로고    scopus 로고
    • Alkaline cellulases
    • Pat. US 5,912,157
    • Osten von der, C. and Schuelein, M. 1999. Alkaline cellulases. Pat. US 5,912,157.
    • (1999)
    • Osten Von Der, C.1    Schuelein, M.2
  • 133
    • 0000994306 scopus 로고    scopus 로고
    • Cellulose: The structure slowly unravels
    • O'Sullivan, A. 1997. Cellulose: the structure slowly unravels. Cellulose 4:173-207. (Pubitemid 127508792)
    • (1997) Cellulose , vol.4 , Issue.3 , pp. 173-207
    • O'Sullivan, A.C.1
  • 135
    • 0000526137 scopus 로고
    • Enzyme production by Trichoderma using the cbh1 promoter
    • Suominen, P. and Reinikainen, T. (eds.) Foundation for Biotechnical and Industrial Fermentation Research, Helsinki
    • Paloheimo, M., Miettinen-Oinonen, A., Torkkeli, T., Nevalainen, H. and Suominen, P. 1993. Enzyme production by Trichoderma using the cbh1 promoter. In: Suominen, P. and Reinikainen, T. (eds.) Proceedings of the TRICEL 93 symposium workshop, Espoo, Finland. Foundation for Biotechnical and Industrial Fermentation Research, Helsinki. Pp. 229-238.
    • (1993) Proceedings of the TRICEL 93 Symposium Workshop, Espoo, Finland , pp. 229-238
    • Paloheimo, M.1    Miettinen-Oinonen, A.2    Torkkeli, T.3    Nevalainen, H.4    Suominen, P.5
  • 136
    • 2142855140 scopus 로고    scopus 로고
    • High-Yield Production of a Bacterial Xylanase in the Filamentous Fungus Trichoderma reesei Requires a Carrier Polypeptide with an Intact Domain Structure
    • DOI 10.1128/AEM.69.12.7073-7082.2003
    • Paloheimo, M., Mäntylä, A., Kallio, J. and Suominen, P. 2003. High-yield production of a bacterial xylanase in the filamentous fungus Trichoderma reesei requires a carrier polypeptide with an intact domain structure. Appl. Environ. Microbiol. 69:7073-7082. (Pubitemid 38585354)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.12 , pp. 7073-7082
    • Paloheimo, M.1    Mantyla, A.2    Kallio, J.3    Suominen, P.4
  • 139
    • 0022969096 scopus 로고
    • Homology between cellulase genes of Trichoderma reesei: Complete nucleotide sequence of the endoglucanase I gene
    • DOI 10.1016/0378-1119(86)90023-5
    • Penttilä, M., Lehtovaara, P., Nevalainen, H., Bhikhabhai, R. and Knowles, J. 1986. Homology between cellulase genes of Trichoderma reesei: complete nucleotide sequence of the endoglucanase I gene. Gene 45:253-263. (Pubitemid 17202577)
    • (1986) Gene , vol.45 , Issue.3 , pp. 253-263
    • Penttila, M.1    Lehtovaara, P.2    Nevalainen, H.3
  • 140
    • 0023553310 scopus 로고
    • A versatile transformation system for the cellulolytic filamentous fungus Trichoderma reesei
    • DOI 10.1016/0378-1119(87)90110-7
    • Penttilä, M., Nevalainen, H., Rättö, M., Salminen, E. and Knowles, J. 1987. A versatile transformation system for cellulolytic filamentous fungus Trichoderma reesei. Gene 61:155-164. (Pubitemid 18064710)
    • (1987) Gene , vol.61 , Issue.2 , pp. 155-164
    • Penttila, M.1    Nevalainen, H.2    Ratto, M.3    Salminen, E.4    Knowles, J.5
  • 141
    • 13444289171 scopus 로고    scopus 로고
    • Molecular biology of Trichoderma and biotechnological applications
    • Arora, D. (ed.) Marcel Dekker, Inc.
    • Penttilä, M., Limon, C. and Nevalainen, H. 2004. Molecular biology of Trichoderma and biotechnological applications In: Arora, D. (ed.) Handbook of fungal biotechnology. Marcel Dekker, Inc. Pp. 413-427.
    • (2004) Handbook of Fungal Biotechnology , pp. 413-427
    • Penttilä, M.1    Limon, C.2    Nevalainen, H.3
  • 142
    • 0029325347 scopus 로고
    • Effects of purified Trichoderma reesei cellulases on the fiber properties of kraft pulp
    • Pere, J., Siika-aho, M., Buchert, J. and Viikari, L. 1995. Effects of purified Trichoderma reesei cellulases on the fiber properties of kraft pulp. Tappi J. 78:71-78.
    • (1995) Tappi J. , vol.78 , pp. 71-78
    • Pere, J.1    Siika-aho, M.2    Buchert, J.3    Viikari, L.4
  • 143
    • 0035940054 scopus 로고    scopus 로고
    • Action of purified Trichoderma reesei cellulases on cotton fibers and yarn
    • DOI 10.1016/S0168-1656(01)00308-X, PII S016816560100308X
    • Pere, J., Puolakka, A., Nousiainen, P. and Buchert, J. 2001. Action of purified Trichoderma reesei cellulases on cotton fibers and yarn. J. Biotechnol. 89:247-255. (Pubitemid 32739063)
    • (2001) Journal of Biotechnology , vol.89 , Issue.2-3 , pp. 247-255
    • Pere, J.1    Puolakka, A.2    Nousiainen, P.3    Buchert, J.4
  • 144
    • 77957819632 scopus 로고    scopus 로고
    • Enhancement of TMP reject refining by enzymatic modification of pulp carbohydrates - A mill study
    • Viikari, L. & Lantto, R. (eds.) Progress in Biotechnology, Elsevier Science B.V.
    • Pere, J., Ellmen, J., Honkasalo, J., Taipalus, P. and Tienvieri, T. 2002. Enhancement of TMP reject refining by enzymatic modification of pulp carbohydrates - A mill study. In: Viikari, L. & Lantto, R. (eds.) Biotechnology in the Pulp and Paper Industry: 8th ICBPPI Meeting, Progress in Biotechnology, Elsevier Science B.V. Vol. 21. Pp. 281-290.
    • (2002) Biotechnology in the Pulp and Paper Industry: 8th ICBPPI Meeting , vol.21 , pp. 281-290
    • Pere, J.1    Ellmen, J.2    Honkasalo, J.3    Taipalus, P.4    Tienvieri, T.5
  • 145
    • 0032787088 scopus 로고    scopus 로고
    • Biochemical properties of xylanases from a thermophilic fungus, Melanocarpus albomyces, and their action on plant cell walls
    • Prabhu, A. and Maheshwari, R. 1999. Biochemical properties of xylanases from a thermophilic fungus, Melanocarpus albomyces, and their action on plant cell walls. J. Biosci. 24:461-470.
    • (1999) J. Biosci. , vol.24 , pp. 461-470
    • Prabhu, A.1    Maheshwari, R.2
  • 146
    • 84884726163 scopus 로고    scopus 로고
    • Cellulose-binding domains: Tools for innovation in cellulosic fiber production and modification
    • Mansfield, S. and Saddler, J. (eds.) Applications of enzymes to lignicellulosics. American Chemical Society, Washington DC
    • Quentin, M., van der Valk, H., van Dam, J. and de Jong, E. 2003. Cellulose-binding domains: tools for innovation in cellulosic fiber production and modification. In: Mansfield, S. and Saddler, J. (eds.) Applications of enzymes to lignicellulosics. ACS Symposium Series 855, American Chemical Society, Washington DC. Pp. 132-155.
    • (2003) ACS Symposium Series 855 , pp. 132-155
    • Quentin, M.1    Van Der Valk, H.2    Van Dam, J.3    De Jong, E.4
  • 147
    • 68949166881 scopus 로고
    • Cellulolytic activity of some thermophilic and thermotolerant fungi of Pakistan
    • Qureshi, M., Mirza, J. and Malik, K. 1980. Cellulolytic activity of some thermophilic and thermotolerant fungi of Pakistan. Biologia (Lahore) 26:201-217.
    • (1980) Biologia (Lahore) , vol.26 , pp. 201-217
    • Qureshi, M.1    Mirza, J.2    Malik, K.3
  • 148
    • 0343924362 scopus 로고    scopus 로고
    • Synthesis of biotechnologically relevant heterologous proteins in filamentous fungi
    • DOI 10.1016/S0032-9592(97)00004-6, PII S0032959297000046
    • Radzio, R. and Kück, U. 1997. Synthesis of biotechnologically relevant heterologous proteins in filamentous fungi. Process Biochemistry 32:529-539. (Pubitemid 27265716)
    • (1997) Process Biochemistry , vol.32 , Issue.6 , pp. 529-539
    • Radzio, R.1    Kuck, U.2
  • 153
    • 0025182502 scopus 로고
    • Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei
    • Rouvinen, J., Bergfors, T., Teeri, T., Knowles, J. and Jones, 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.4    Jones, A.5
  • 154
    • 0028361655 scopus 로고
    • A novel, small endoglucanase gene, egl5, from Trichoderma reesei isolated by expression in yeast
    • DOI 10.1111/j.1365-2958.1994.tb00417.x
    • Saloheimo, A., Henrissat, B., Hoffren, A., Teleman, O. and Penttilä, M. 1994. A novel, small endoglucanase gene, egl5, from Trichoderma reesei isolated by expression in yeast. Mol. Microbiol. 13:219-228. (Pubitemid 24225494)
    • (1994) Molecular Microbiology , vol.13 , Issue.2 , pp. 219-228
    • Saloheimo, A.1    Henrissat, B.2    Hoffren, A.-M.3    Teleman, O.4    Penttila, M.5
  • 155
    • 0034102428 scopus 로고    scopus 로고
    • 2 transcription factor involved in regulation of activity of the cellulase promoter cbh1 of Trichoderma reesei
    • 2 transcription factor involved in regulation of activity of the cellulase promoter cbh1 of Trichoderma reesei. J. Biol. Chem. 275:5817-5825.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5817-5825
    • Saloheimo, A.1    Aro, N.2    Ilmén, M.3    Penttilä, M.4
  • 157
    • 0026356867 scopus 로고
    • Heterologous production of a ligninolytic enzyme: Expression of the Phlebia radiata laccase gene in Trichoderma reesei
    • Saloheimo, M. and Niku-Paavola, M.-L. 1991. Heterologous production of a ligninolytic enzyme: expression of the Phlebia radiata laccase gene in Trichoderma reesei. Bio/Technology 9:987-990.
    • (1991) Bio/Technology , vol.9 , pp. 987-990
    • Saloheimo, M.1    Niku-Paavola, M.-L.2
  • 158
    • 0030669760 scopus 로고    scopus 로고
    • cDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast
    • Saloheimo, M., Nakari-Setälä, T., Tenkanen, M. and Penttilä, M. 1997. cDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast. Eur. J. Biochem. 249:584-591. (Pubitemid 27455803)
    • (1997) European Journal of Biochemistry , vol.249 , Issue.2 , pp. 584-591
    • Saloheimo, M.1    Nakari-Setala, T.2    Tenkanen, M.3    Penttila, M.4
  • 159
    • 0032884910 scopus 로고    scopus 로고
    • The protein disulphide isomerase gene of the fungus Trichoderma reesei is induced by endoplasmic reticulum stress and regulated by the carbon source
    • DOI 10.1007/s004380051057
    • Saloheimo, M., Lund, M. and Penttilä, M. 1999. The protein disulphide isomerase gene of the fungus Trichoderma reesei is induced by endoplasmic reticulum stress and regulated by the carbon source. Mol. Gen. Genet. 262:35-45. (Pubitemid 29423900)
    • (1999) Molecular and General Genetics , vol.262 , Issue.1 , pp. 35-45
    • Saloheimo, M.1    Lund, M.2    Penttila, M.E.3
  • 160
    • 0036729340 scopus 로고    scopus 로고
    • Enzymatic properties and intracellular localization of the novel Trichoderma reesei β-glucosidase BGLII (Cel1A)
    • DOI 10.1128/AEM.68.9.4546-4553.2002
    • Saloheimo, M., Kuja-Panula, J., Ylösmäki, E., Ward, M. and Penttilä, M. 2002a. Enzymatic properties and intracellulase loalization of the novel Trichoderma reesei β-glucosidase BGLII (Cel1A). Appl. Environ. Microbiol. 68:4546-4553. (Pubitemid 34988140)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.9 , pp. 4546-4553
    • Saloheimo, M.1    Kuja-Panula, J.2    Ylosmaki, E.3    Ward, M.4    Penttila, M.5
  • 161
    • 0036046037 scopus 로고    scopus 로고
    • Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials
    • DOI 10.1046/j.1432-1033.2002.03095.x
    • Saloheimo, M., Paloheimo, M., Hakola, S., Pere, J., Swanson, B., Nyyssönen, E., Bhatia, A., Ward, M. and Penttilä, M. 2002b. Swollenin, a Trichoderma reesei protein with sequence similarity to plant expansins, exhibits disruption activity on cellulosic materials. Eur. J. Biochem. 269:4202-4211. (Pubitemid 35026007)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.17 , pp. 4202-4211
    • Saloheimo, M.1    Paloheimo, M.2    Hakola, S.3    Pere, J.4    Swanson, B.5    Nyyssonen, E.6    Bhatia, A.7    Ward, M.8    Penttila, M.9
  • 162
    • 0037323934 scopus 로고    scopus 로고
    • Activation mechanisms of the HAC1-mediated unfolded protein response in filamentous fungi
    • DOI 10.1046/j.1365-2958.2003.03363.x
    • Saloheimo, M., Valkonen, M. and Penttilä, M. 2003a. Activation mechanisms of the HACI-mediated unfolded protein reponse in filamentous fungi. Mol. Microbiol. 47:1149-1161. (Pubitemid 36232808)
    • (2003) Molecular Microbiology , vol.47 , Issue.4 , pp. 1149-1161
    • Saloheimo, M.1    Valkonen, M.2    Penttila, M.3
  • 164
    • 0347760411 scopus 로고    scopus 로고
    • Characterization of Secretory Genes ypt1/yptA and nsf1/nsfA from Two Filamentous Fungi: Induction of Secretory Pathway Genes of Trichoderma reesei under Secretion Stress Conditions
    • DOI 10.1128/AEM.70.1.459-467.2004
    • Saloheimo, M., Wang, H., Valkonen, M., Vasara, T., Huuskonen, A., Riikonen, M., Pakula, T., Ward, M. and Penttilä, M. 2004. Characterization of secretory genes ypt1/yptA and nsf1/nsfA from two filamentous fungi: induction of secretory pathway genes of Trichoderma reesei under secretion stress conditions. Appl. Environ. Microbiol. 70:459-467. (Pubitemid 38090237)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.1 , pp. 459-467
    • Saloheimo, M.1    Wang, H.2    Valkonen, M.3    Vasara, T.4    Huuskonen, A.5    Riikonen, M.6    Pakula, T.7    Ward, M.8    Penttila, M.9
  • 167
    • 0038396111 scopus 로고    scopus 로고
    • Enzymatic properties of cellulases from Humicola insolens
    • DOI 10.1016/S0168-1656(97)00090-4, PII S0168165697000904
    • Schülein, M. 1997. Enzymatic properties of cellulases from Humicola insolens. J. Biotechnol. 57:71-81. (Pubitemid 27397472)
    • (1997) Journal of Biotechnology , vol.57 , Issue.1-3 , pp. 71-81
    • Schulein, M.1
  • 171
    • 0028099874 scopus 로고
    • The use of conserved cellulase family-specific sequences to clone cellulase homologue cDNAs from Fusarium oxysporum
    • Sheppard, P., Grant, F., Oort, P., Sprecher, C., Foster, D., Hagen, F., Upshall, A., Mcknight, G. and O'hara, P. 1994. The use of conserved cellulase family-specific sequences to clone cellulase homologue cDNAs from Fusarium oxysporum. Gene 150:163-167.
    • (1994) Gene , vol.150 , pp. 163-167
    • Sheppard, P.1    Grant, F.2    Oort, P.3    Sprecher, C.4    Foster, D.5    Hagen, F.6    Upshall, A.7    Mcknight, G.8    O'Hara, P.9
  • 172
    • 0021052116 scopus 로고
    • Molecular cloning of exo-cellobiohydrolase I derived from Trichoderma reesei strain L27
    • Shoemaker, S., Schweickart, V., Ladner, M., Gelfand, D., Kwok, S. and Myambo, K. 1983. Molecular cloning of exo-cellobiohydrolase derived from Trichoderma reesei strain L27. Bio/Technology 1:691-696. (Pubitemid 14247507)
    • (1983) Bio/Technology , vol.1 , Issue.8 , pp. 691-696
    • Shoemaker, S.1    Schweickart, V.2    Ladner, M.3
  • 173
    • 0035940079 scopus 로고    scopus 로고
    • Application of microassays for investigation of cellulase abrasive activity and backstaining
    • Sinitsyn, A., Gusakov, A., Grishutin, S., Sinitsyna, O. and Ankudimova, N. Application of microassays for investigation of cellulase abrasive activity and backstaining. J. Biotechnol. 89:233-238.
    • J. Biotechnol. , vol.89 , pp. 233-238
    • Sinitsyn, A.1    Gusakov, A.2    Grishutin, S.3    Sinitsyna, O.4    Ankudimova, N.5
  • 175
    • 0035491731 scopus 로고    scopus 로고
    • Cloning and expression of an endocellulase gene from a novel streptomycete isolated from an East African soda lake
    • DOI 10.1007/s007920100198
    • van Solingen, P., Meijer, D., van der Kleij, W., Barnett, C., Bolle, R., Power, S. and Jones, B. 2001. Cloning and expression of an endocellulase gene from a novel streptomycete isolated from an East African soda lake. Extremophiles 5:333-341. (Pubitemid 33737383)
    • (2001) Extremophiles , vol.5 , Issue.5 , pp. 333-341
    • Van Solingen, P.1    Meijer, D.2    Van Der, K.W.A.H.3    Barnett, C.4    Bolle, R.5    Power, S.D.6    Jones, B.E.7
  • 177
    • 0027498957 scopus 로고
    • Characterization of the Trichoderma reesei cbh2 promoter
    • DOI 10.1007/BF00352009
    • Stangl, H., Gruber, F. and Kubicek, C. 1993. Characterization of the Trichoderma reesei cbh2 promoter. Curr. Genet. 23:115-122. (Pubitemid 23045011)
    • (1993) Current Genetics , vol.23 , Issue.2 , pp. 115-122
    • Stangl, H.1    Gruber, F.2    Kubicek, C.P.3
  • 179
    • 0029856409 scopus 로고    scopus 로고
    • Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: Substrate distortion gives rise to the preferred axial orientation for the leaving group
    • DOI 10.1021/bi961946h
    • Sulzenbacher, G., Driguez, H., Henrissat, B., Schülein, M. and Davies, G. 1996. Structure of the Fusarium oxysporium endoglucanase I with a nonhydrolyzable substrate-analog, substrate distortion gives rise to the preferred axial orientation for the leaving group. Biochemistry 35:15280-15287. (Pubitemid 26408862)
    • (1996) Biochemistry , vol.35 , Issue.48 , pp. 15280-15287
    • Sulzenbacher, G.1    Driguez, H.2    Henrissat, B.3    Schulein, M.4    Davies, G.J.5
  • 180
    • 0027131591 scopus 로고
    • High frequency one-step gene replacement in Trichoderma reesei. II. Effects of deletions of individual cellulase genes
    • DOI 10.1007/BF00279894
    • Suominen, P., Mäntylä, A., Karhunen, T., Hakola, S. and Nevalainen, H. 1993. High frequency one-step gene replacement in Trichoderma reesei. II. Effects of deletions of individual cellulase genes. Mol. Gen. Genet. 241:523-30. (Pubitemid 24003871)
    • (1993) Molecular and General Genetics , vol.241 , Issue.5-6 , pp. 523-530
    • Suominen, P.L.1    Mantyla, A.L.2    Karhunen, T.3    Haokla, S.4    Nevlainen, H.5
  • 181
    • 0034204550 scopus 로고    scopus 로고
    • Trichoderma reesei cellulases and their core domains in the hydrolysis and modification of chemical pulp
    • Suurnäkki, A., Tenkanen, M., Siika-aho, M., Niku-Paavola, M.-L.,Viikari, L. and Buchert, J. 2000. Trichoderma reesei cellulases and their core domains in the hydrolysis and modification of chemical pulp. Cellulose 7:189-209.
    • (2000) Cellulose , vol.7 , pp. 189-209
    • Suurnäkki, A.1    Tenkanen, M.2    Siika-aho, M.3    Niku-Paavola, M.-L.4    Viikari, L.5    Buchert, J.6
  • 183
    • 0032937042 scopus 로고    scopus 로고
    • Molecular cloning and expression of the novel fungal β-glucosidase genes from Humicola grisea and Trichoderma reesei
    • Takashima, S., Nakamura, A., Hidaka, M., Masaki, H. and Uozumi, T. 1999. Molecular cloning and expression of the novel fungal β-glucosidase genes from Humicola grisea and Trichoderma reesei. J. Biochem. 125:728-736. (Pubitemid 29192494)
    • (1999) Journal of Biochemistry , vol.125 , Issue.4 , pp. 728-736
    • Takashima, S.1    Nakamura, A.2    Hidaka, M.3    Masaki, H.4    Uozumi, T.5
  • 184
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: New insight into the function of cellobiohydrolases
    • DOI 10.1016/S0167-7799(97)01032-9, PII S0167779997010329
    • Teeri, T. 1997. Crystalline cellulose degradation: new insight into the function of cellobiohydrolases. Tibtech. 15:160-167. (Pubitemid 27219573)
    • (1997) Trends in Biotechnology , vol.15 , Issue.5 , pp. 160-167
    • Teeri, T.T.1
  • 185
    • 0002937488 scopus 로고
    • Cellulose degradation by native and engineered fundal cellulases
    • Teeri, T. and Koivula, A. 1995. Cellulose degradation by native and engineered fundal cellulases. Carbohydr. Eur. 12:28-33.
    • (1995) Carbohydr. Eur. , vol.12 , pp. 28-33
    • Teeri, T.1    Koivula, A.2
  • 186
    • 0021063872 scopus 로고
    • The molecular cloning of the major cellulase gene from Trichoderma reesei
    • Teeri, T., Salovuori, I. and Knowles, J. 1983. The molecular cloning of the major cellulase gene from Trichoderma reesei. Bio/Technology 1:696-699. (Pubitemid 14247508)
    • (1983) Bio/Technology , vol.1 , Issue.8 , pp. 696-699
    • Teeri, T.1    Salovuori, I.2    Knowles, J.3
  • 187
    • 0023132478 scopus 로고
    • Homologous domains in Trichoderma reesei cellulolytic enzymes: Gene sequence and expression of cellobiohydrolase II
    • DOI 10.1016/0378-1119(87)90472-0
    • Teeri, T., Lehtovaara, P., Kauppinen, S., Salovuori, I. and Knowles, J. 1987. Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II. Gene 51:43-52. (Pubitemid 17048551)
    • (1987) Gene , vol.51 , Issue.1 , pp. 43-52
    • Teeri, T.T.1    Lehtovaara, P.2    Kauppinen, S.3
  • 188
    • 0034283706 scopus 로고    scopus 로고
    • Codon optimization of xylanase gene xynB from the thermophilic bacterium Dictyoglomus thermophilum for expression in the filamentous fungus Trichoderma reesei
    • DOI 10.1016/S0378-1097(00)00308-6, PII S0378109700003086
    • Te'o, V., Cziferszky, A., Bergquist, P. and Nevalainen, H. 2000. Codon optimization of xylanase gene xynB from the thermophilic bacterium Dictyoglomus thermophilum for expression in the filamentous fungus Trichoderma reesei. FEMS Microbiol. Lett. 190:13-19. (Pubitemid 30645828)
    • (2000) FEMS Microbiology Letters , vol.190 , Issue.1 , pp. 13-19
    • Te'o, V.S.J.1    Cziferszky, A.E.2    Bergquist, P.L.3    Nevalainen, K.M.H.4
  • 189
    • 77957054571 scopus 로고
    • Fluorogenic and chromogenic glycosides as substrates and ligands of carbohydrases
    • van Tilbeurgh, H., Loonties, F., de Bruyne, C. and Clayessens, M. 1988. Fluorogenic and chromogenic glycosides as substrates and ligands of carbohydrases. Meth. Enzymol. 160:45-59.
    • (1988) Meth. Enzymol. , vol.160 , pp. 45-59
    • Van Tilbeurgh, H.1    Loonties, F.2    De Bruyne, C.3    Clayessens, M.4
  • 190
    • 0028874441 scopus 로고
    • Cellulose hydrolysis by bacteria and fungi
    • Poole, R. (ed.) Academic Press, London, UK
    • Tomme, P., Warren, R. and Gilkes, N. 1995a. Cellulose hydrolysis by bacteria and fungi. In: Poole, R. (ed.) Advances Microbial Physiology. Academic Press, London, UK. Vol. 37. Pp. 1-81.
    • (1995) Advances Microbial Physiology , vol.37 , pp. 1-81
    • Tomme, P.1    Warren, R.2    Gilkes, N.3
  • 191
    • 0001594653 scopus 로고
    • Enzymatic degradation of insoluble carbohydrates
    • Saddler, J. and Penner, M. (eds.) Washington D.C.
    • Tomme, P., Warren, R., Miller, R., Kilburn, D. and Gilkes, N. 1995b. In: Saddler, J. and Penner, M. (eds.) Enzymatic degradation of insoluble carbohydrates, Am. Chem. Soc. Symp. Ser., Washington D.C. Vol. 618. Pp. 142-163.
    • (1995) Am. Chem. Soc. Symp. Ser. , vol.618 , pp. 142-163
    • Tomme, P.1    Warren, R.2    Miller, R.3    Kilburn, D.4    Gilkes, N.5
  • 194
    • 0025097250 scopus 로고
    • Upgrading garment washing techniques
    • Tyndall, M. 1990. Upgrading garment washing techniques. American Dyestuff Reporter 5:22-30.
    • (1990) American Dyestuff Reporter , vol.5 , pp. 22-30
    • Tyndall, M.1
  • 195
    • 0026807197 scopus 로고
    • Application of cellulase enzymes to cotton fabrics and garments
    • Tyndall, R.M. 1992. Application of cellulase enzymes to cotton fabrics and garments. Textile Chemist and Colorist 24:23.
    • (1992) Textile Chemist and Colorist , vol.24 , pp. 23
    • Tyndall, R.M.1
  • 196
    • 67649161403 scopus 로고    scopus 로고
    • Enzymes in fruit and vegetable juice extraction
    • Whitehurst, R. and Law, B. (eds.) Sheffield, Academic Press, CRC Press
    • Urlaub, R. 2002. Enzymes in fruit and vegetable juice extraction. In: Whitehurst, R. and Law, B. (eds.) Enzymes in food technology. Sheffield, Academic Press, CRC Press. Pp. 145-183.
    • (2002) Enzymes in Food Technology , pp. 145-183
    • Urlaub, R.1
  • 197
    • 84884728574 scopus 로고    scopus 로고
    • Redeposition or backstain inhibition during stonewashing process
    • Pat. US 2002/0066144 A1
    • Uyama, N. and Daimon, K. 2002. Redeposition or backstain inhibition during stonewashing process. Pat. US 2002/0066144 A1.
    • (2002)
    • Uyama, N.1    Daimon, K.2
  • 199
    • 9644280788 scopus 로고
    • Isolation and characterization of genes involved in basic metabolism of the filamentous fungus Trichoderma reesei
    • Ph. D. Thesis. Espoo
    • Vanhanen, S. 1991. Isolation and characterization of genes involved in basic metabolism of the filamentous fungus Trichoderma reesei. Ph. D. Thesis. Espoo: VTT Publications 75. 119 p.
    • (1991) VTT Publications , vol.75 , pp. 119
    • Vanhanen, S.1
  • 201
    • 0030685697 scopus 로고    scopus 로고
    • Isolation and analysis of functional homologues of the secretion-related SAR1 gene of Saccharomyces cerevisiae from Aspergillus niger and Trichoderma reesei
    • Veldhuisen, G., Saloheimo, M. Fiers, M., Punt, P., Contreras, R., Penttilä, M. and van den Hondel, C. 1997. Isolation and analysis of functional homologues of the secretion-related SAR1 gene of Saccharomyces cerevisiae from Aspergillus niger and Trichoderma reesei. Mol. Gen. Genet. 256:446-455.
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 446-455
    • Veldhuisen, G.1    Saloheimo, M.2    Fiers, M.3    Punt, P.4    Contreras, R.5    Penttilä, M.6    Van Den Hondel, C.7
  • 202
    • 0029077782 scopus 로고
    • Molecular genetic strain improvement for the overproduction of fungal proteins by filamentous fungi
    • Verdoes, J., Punt, P. and van den Hondel, C. 1995. Molecular genetic strain improvement for the overproduction of fungal proteins by filamentous fungi. Appl. Microbial. Biotechnol. 43:195-205.
    • (1995) Appl. Microbial. Biotechnol. , vol.43 , pp. 195-205
    • Verdoes, J.1    Punt, P.2    Van Den Hondel, C.3
  • 203
    • 84884707753 scopus 로고
    • A process for defuzzing and depilling cellulosic fabrics
    • Pat. WO 93/20278
    • Videbaek, T. and Andersen, L. 1993. A process for defuzzing and depilling cellulosic fabrics. Pat. WO 93/20278.
    • (1993)
    • Videbaek, T.1    Andersen, L.2
  • 205
    • 0028998104 scopus 로고
    • Cloning, characterization and functional expression of an endoglucanase-encoding gene from the phytopathogenic fungus Macrophomina phaseolina
    • Wang, H. and Jones, R. 1995a. Cloning, characterization and functional expression of an endoglucanase-encoding gene from the phytopathogenic fungus Macrophomina phaseolina. Gene 158:125-128.
    • (1995) Gene , vol.158 , pp. 125-128
    • Wang, H.1    Jones, R.2
  • 206
    • 0029016541 scopus 로고
    • An unique endoglucanase-encoding gene cloned from the phytopathogenic fungus Macrophomina phaseolina
    • Wang, H. and Jones, R. 1995b. An unique endoglucanase-encoding gene cloned from the phytopathogenic fungus Macrophomina phaseolina. Appl. Environ. Microbiol. 61:2004-2006.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2004-2006
    • Wang, H.1    Jones, R.2
  • 207
    • 0000964263 scopus 로고
    • Cloning, sequence and preliminary structural analysis of a small high pI endoglucanase (EGIII) from Trichoderma reesei
    • P. Suominen and T. Reinikainen (eds.)Espoo Foundation for Biotechnical and Industrial Fermentation Research, Helsinki, Finland
    • Ward, M., Wu, S., Dauberman, J., Weiss, G., Larenas, E., Bower, B., Rey, M., Clarkson, K. and Bott, R. 1993. Cloning, sequence and preliminary structural analysis of a small high pI endoglucanase (EGIII) from Trichoderma reesei. In: P. Suominen and T. Reinikainen (eds.) Proceedings of the Second Tricel Symposium on Trichoderma cellulases and other hydrolases, Espoo, Vol. 8. Foundation for Biotechnical and Industrial Fermentation Research, Helsinki, Finland. Pp. 153-158.
    • (1993) Proceedings of the Second Tricel Symposium on Trichoderma Cellulases and Other Hydrolases , vol.8 , pp. 153-158
    • Ward, M.1    Wu, S.2    Dauberman, J.3    Weiss, G.4    Larenas, E.5    Bower, B.6    Rey, M.7    Clarkson, K.8    Bott, R.9
  • 209
    • 0032545260 scopus 로고    scopus 로고
    • Two adjacent protein binding motifs in the cbh2 (cellobiohydrolase II-encoding) promoter of the fungus Hypocrea jecorina (Trichoderma reesei) cooperate in the unduction by cellulose
    • Zeilinger, S., Mach, R. and Kubicek, C. 1998. Two adjacent protein binding motifs in the cbh2 (cellobiohydrolase II-encoding) promoter of the fungus Hypocrea jecorina (Trichoderma reesei) cooperate in the unduction by cellulose. J. Biol. Chem. 51:34463-34471.
    • (1998) J. Biol. Chem. , vol.51 , pp. 34463-34471
    • Zeilinger, S.1    Mach, R.2    Kubicek, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.