메뉴 건너뛰기




Volumn 108, Issue , 2007, Pages 121-145

Thermostable enzymes in lignocellulose hydrolysis

Author keywords

Glucosidase; Cellobiohydrolase; Cellulases; Endoglucanase; Hydrolysis; Lignocellulose; Thermostable

Indexed keywords

ALCOHOL; CELLULOSE; ENZYME; LIGNIN; LIGNOCELLULOSE;

EID: 34548815422     PISSN: 07246145     EISSN: None     Source Type: Book Series    
DOI: 10.1007/10_2007_065     Document Type: Article
Times cited : (320)

References (83)
  • 1
    • 0642361702 scopus 로고
    • Cellulase production and activity in a species of Cladosporium
    • Abrha B, Gashe BA (1992) Cellulase production and activity in a species of Cladosporium. World J Microbiol Biotech 8:164-166
    • (1992) World J Microbiol Biotech , vol.8 , pp. 164-166
    • Abrha, B.1    Gashe, B.A.2
  • 2
    • 14744272350 scopus 로고
    • Cloning and amplification of the gene encoding an extracellular β-glucose from Trichoderma reesei: Evidence for improved rates of saccharification of cellulosic substrates
    • Barnett C Berka R, Fowler T (1991) Cloning and amplification of the gene encoding an extracellular β-glucose from Trichoderma reesei: evidence for improved rates of saccharification of cellulosic substrates. Biotechnology 9:562-567
    • (1991) Biotechnology , vol.9 , pp. 562-567
    • Barnett, C.1    Berka, R.2    Fowler, T.3
  • 3
    • 0030065736 scopus 로고    scopus 로고
    • Barr B Hsieh, Ganem B, Wilson BD (1996) Identification of two functionally different classes of exocellulases. Biochemistry 35:586-592
    • Barr B Hsieh, Ganem B, Wilson BD (1996) Identification of two functionally different classes of exocellulases. Biochemistry 35:586-592
  • 4
    • 0026537453 scopus 로고
    • Interlaboratory testing methods for assay of xylanase activity
    • Bailey MJ, Biely P, Poutanen K (1992) Interlaboratory testing methods for assay of xylanase activity. J Biotechnol 23:257-270
    • (1992) J Biotechnol , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 5
    • 0019554715 scopus 로고
    • Induction, isolation and testing of stable Trichoderma reesei mutants with improved production of solubilizing cellulase
    • Bailey M, Nevalainen H (1981) Induction, isolation and testing of stable Trichoderma reesei mutants with improved production of solubilizing cellulase. Enzyme Microb Technol 3:153-157
    • (1981) Enzyme Microb Technol , vol.3 , pp. 153-157
    • Bailey, M.1    Nevalainen, H.2
  • 6
    • 0043164829 scopus 로고    scopus 로고
    • Efficient cellulase production by Trichoderma reesei in continuous cultivation on lactose medium with a computer-controlled feeding strategy
    • Bailey MJ, Tähtiharju J (2003) Efficient cellulase production by Trichoderma reesei in continuous cultivation on lactose medium with a computer-controlled feeding strategy. Appl Microbiol Biotechnol 62:156-162
    • (2003) Appl Microbiol Biotechnol , vol.62 , pp. 156-162
    • Bailey, M.J.1    Tähtiharju, J.2
  • 10
    • 33748037939 scopus 로고
    • Amylases α and β
    • Colowick SP, Kaplan NO eds, Academic, New York, pp
    • Bernfeld P (1955) Amylases α and β. In: Colowick SP, Kaplan NO (eds) Methods in enzymology, vol 1. Academic, New York, pp 149-158
    • (1955) Methods in enzymology , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 11
    • 0032403607 scopus 로고    scopus 로고
    • Purification, characterization, and molecular analysis of thermostable cellulases CelA and CelB from Thermotoga neapolitana
    • Bok JD, Yernool DA, Eveleigh DE (1998) Purification, characterization, and molecular analysis of thermostable cellulases CelA and CelB from Thermotoga neapolitana. Appl Environ Microbiol 64:4774-4781
    • (1998) Appl Environ Microbiol , vol.64 , pp. 4774-4781
    • Bok, J.D.1    Yernool, D.A.2    Eveleigh, D.E.3
  • 12
    • 0025779380 scopus 로고
    • Purification and properties of a novel type exo-l,4-β-glucanase (Avicelase II) from the cellulolytic thermophile Clostridium stercorarium
    • Bronnenmeier K, Rücknagel K, Staudenbauer W (1991) Purification and properties of a novel type exo-l,4-β-glucanase (Avicelase II) from the cellulolytic thermophile Clostridium stercorarium. Eur J Biochem 200:379-385
    • (1991) Eur J Biochem , vol.200 , pp. 379-385
    • Bronnenmeier, K.1    Rücknagel, K.2    Staudenbauer, W.3
  • 13
    • 0025199681 scopus 로고
    • Cellulose hydrolysis by a highly thermostable endo-l,4-glucanase (Avicelase I) from Clostridium stercorarium
    • Bronnenmeier K, Staudenbauer W (1990) Cellulose hydrolysis by a highly thermostable endo-l,4-glucanase (Avicelase I) from Clostridium stercorarium. Enzyme Microbial Technol 12:431-436
    • (1990) Enzyme Microbial Technol , vol.12 , pp. 431-436
    • Bronnenmeier, K.1    Staudenbauer, W.2
  • 14
    • 0028924376 scopus 로고
    • Purification of Thermotoga maritima enzymes for the degradation of cellulosic materials
    • Bronnenmeier K, Kern A, Liebl W, Staudenbauer W (1995) Purification of Thermotoga maritima enzymes for the degradation of cellulosic materials. Appl Environ Microbiol 61:1339-1407
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1339-1407
    • Bronnenmeier, K.1    Kern, A.2    Liebl, W.3    Staudenbauer, W.4
  • 15
    • 0007918106 scopus 로고
    • Purification of β-D-glucoside glucohydrolases of Talaromyces emersonii
    • Coughlan M, McHale A (1988) Purification of β-D-glucoside glucohydrolases of Talaromyces emersonii. Methods Enzymol 160:437-443
    • (1988) Methods Enzymol , vol.160 , pp. 437-443
    • Coughlan, M.1    McHale, A.2
  • 16
    • 85066649922 scopus 로고    scopus 로고
    • Coutinho PM, Henrissat B (1999) Carbohydrate active enzymes. Database available at http://www.cazy.org, last visited: 10 May 2007
    • Coutinho PM, Henrissat B (1999) Carbohydrate active enzymes. Database available at http://www.cazy.org, last visited: 10 May 2007
  • 18
    • 33747013310 scopus 로고    scopus 로고
    • Thermotolerant cellulase
    • Ding S-Y (2006) Thermotolerant cellulase. Industrial Bioproc 28(7):3-4
    • (2006) Industrial Bioproc , vol.28 , Issue.7 , pp. 3-4
    • Ding, S.-Y.1
  • 19
    • 0345676498 scopus 로고    scopus 로고
    • High-resolution crystal structures reveal how a cellulose chain is bound in the 50 Å long tunnel of cellobiohydrolase I from Trichoderma reesei
    • Divne C, Ståhlberg J, Teeri T, Jones T (1998) High-resolution crystal structures reveal how a cellulose chain is bound in the 50 Å long tunnel of cellobiohydrolase I from Trichoderma reesei. J Mol Biol 275:309-325
    • (1998) J Mol Biol , vol.275 , pp. 309-325
    • Divne, C.1    Ståhlberg, J.2    Teeri, T.3    Jones, T.4
  • 20
    • 0025400283 scopus 로고
    • Optimization of temperature and enzyme concentration in the enzymatic saccharification of steam pretreated willow
    • Eklund R, Galbe M, Zacchi G (1990) Optimization of temperature and enzyme concentration in the enzymatic saccharification of steam pretreated willow. Enzyme Microb Technol 12:225-228
    • (1990) Enzyme Microb Technol , vol.12 , pp. 225-228
    • Eklund, R.1    Galbe, M.2    Zacchi, G.3
  • 21
    • 0034047876 scopus 로고    scopus 로고
    • Mechanism of substrate hydrolysis by a thermophilic endoglucanase from Thermotoga maritima
    • Evans B, Gilman A, Cordray K, Woodward J (2000) Mechanism of substrate hydrolysis by a thermophilic endoglucanase from Thermotoga maritima. Biotechnol Lett 22:735-740
    • (2000) Biotechnol Lett , vol.22 , pp. 735-740
    • Evans, B.1    Gilman, A.2    Cordray, K.3    Woodward, J.4
  • 22
    • 0025832337 scopus 로고
    • Purification and characterization of endoglucanase Ss from Clostridium thermocellum
    • Fauth U, Romaniec M, Kobayashi T, Demain A (1991) Purification and characterization of endoglucanase Ss from Clostridium thermocellum. Biochem J 279:67-73
    • (1991) Biochem J , vol.279 , pp. 67-73
    • Fauth, U.1    Romaniec, M.2    Kobayashi, T.3    Demain, A.4
  • 23
    • 0024017518 scopus 로고
    • Isolation of cellulase enzymes from the thermophilic fungus Thermoascus aurantiacus and regulation of enzyme production
    • Feldman KA, Lovett JS, Tsao GT (1988) Isolation of cellulase enzymes from the thermophilic fungus Thermoascus aurantiacus and regulation of enzyme production. Enzyme Microb Technol 10:262-272
    • (1988) Enzyme Microb Technol , vol.10 , pp. 262-272
    • Feldman, K.A.1    Lovett, J.S.2    Tsao, G.T.3
  • 25
    • 0002179409 scopus 로고    scopus 로고
    • Practical limits and prospects (kinetics)
    • Godfrey T, West S eds, 2nd edn. MacMillan, London, pp
    • Fullbrook PD (1996) Practical limits and prospects (kinetics). In: Godfrey T, West S (eds) Industrial enzymology, 2nd edn. MacMillan, London, pp 508-509
    • (1996) Industrial enzymology , pp. 508-509
    • Fullbrook, P.D.1
  • 26
    • 0034107851 scopus 로고    scopus 로고
    • Simultaneous production of high activities of thermostable endoglucanase and β-D-glucosidase by the wild thermophilic fungus Thermoascus aurantiacus
    • Gomes I, Gomes J, Gomes D, Steiner W (2000) Simultaneous production of high activities of thermostable endoglucanase and β-D-glucosidase by the wild thermophilic fungus Thermoascus aurantiacus. Appl Microbiol Biotechnol 53:461-468
    • (2000) Appl Microbiol Biotechnol , vol.53 , pp. 461-468
    • Gomes, I.1    Gomes, J.2    Gomes, D.3    Steiner, W.4
  • 27
    • 9744263969 scopus 로고    scopus 로고
    • Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii
    • Grassick A, Murray P, Thompson R, Collins C, Byrnes L, Birrane G, Higgins T, Tuohy M (2004) Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii. Eur J Biochem 271:4495-4506
    • (2004) Eur J Biochem , vol.271 , pp. 4495-4506
    • Grassick, A.1    Murray, P.2    Thompson, R.3    Collins, C.4    Byrnes, L.5    Birrane, G.6    Higgins, T.7    Tuohy, M.8
  • 29
    • 0031196245 scopus 로고    scopus 로고
    • Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237
    • Hakamada Y, Koike K, Yoshimatsu T, Mori H, Kobayashi T, Ito S (1997) Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237. Extremophiles 1:151-156
    • (1997) Extremophiles , vol.1 , pp. 151-156
    • Hakamada, Y.1    Koike, K.2    Yoshimatsu, T.3    Mori, H.4    Kobayashi, T.5    Ito, S.6
  • 30
    • 0030893813 scopus 로고    scopus 로고
    • Characterization of cellulase complex of Streptomyces albaduncus; thermostable cellulase, cellobiohydrolase and beta-glucosidase characterization
    • Harchand R, Singh S (1997) Characterization of cellulase complex of Streptomyces albaduncus; thermostable cellulase, cellobiohydrolase and beta-glucosidase characterization. J Basic Microbiol 37:93-103
    • (1997) J Basic Microbiol , vol.37 , pp. 93-103
    • Harchand, R.1    Singh, S.2
  • 31
    • 84966185447 scopus 로고
    • Synergism of cellulases from Trichoderma reesei in degradation of cellulose
    • Henrissat B, Driquez H, Viet C, Schülein M (1985) Synergism of cellulases from Trichoderma reesei in degradation of cellulose. Bio/Technology 3:722-726
    • (1985) Bio/Technology , vol.3 , pp. 722-726
    • Henrissat, B.1    Driquez, H.2    Viet, C.3    Schülein, M.4
  • 32
    • 85066693488 scopus 로고    scopus 로고
    • Himmel M, Adney W, Tucker M, Grohmann K (1994) Thermostable purified endoglucanase from Acidothermus cellulolyticus ATCC 43068. US Patent 5275944
    • Himmel M, Adney W, Tucker M, Grohmann K (1994) Thermostable purified endoglucanase from Acidothermus cellulolyticus ATCC 43068. US Patent 5275944
  • 35
    • 0032949340 scopus 로고    scopus 로고
    • Disintegration of uncooked rice by carboxymethyl cellulase from Sporotrichum sp. HG-I
    • Ishihara M, Shinkichi T, Toyama S (1999) Disintegration of uncooked rice by carboxymethyl cellulase from Sporotrichum sp. HG-I. J Biosci Bioeng 87:249-251
    • (1999) J Biosci Bioeng , vol.87 , pp. 249-251
    • Ishihara, M.1    Shinkichi, T.2    Toyama, S.3
  • 36
    • 84943470296 scopus 로고
    • Measurement of cellulase activities
    • International Union of Pure and Applied Chemistry IUPAC
    • International Union of Pure and Applied Chemistry (IUPAC) (1987) Measurement of cellulase activities. Pure Appl Chem 59:257-268
    • (1987) Pure Appl Chem , vol.59 , pp. 257-268
  • 37
    • 0037572264 scopus 로고    scopus 로고
    • Production and characterization of thermostable cellulases from Streptomyces transformant T3-1
    • Jang HD, Chen KS (2003) Production and characterization of thermostable cellulases from Streptomyces transformant T3-1. World J Microb Biotechnol 19:263-268
    • (2003) World J Microb Biotechnol , vol.19 , pp. 263-268
    • Jang, H.D.1    Chen, K.S.2
  • 38
    • 0036143264 scopus 로고    scopus 로고
    • Enzymatic degradation of carboxymethyl cellulose hydrolysed by the endoglucanases Cel5A, Cel7B and Cel45A from Humicola insolens and Cel7B, Cell2A and Cel45A core from Trichoderma reesei
    • Karlsson J, Momcilovic D, Wittgren B, Schülein M, Tjerneld F, Brinkman G (2002) Enzymatic degradation of carboxymethyl cellulose hydrolysed by the endoglucanases Cel5A, Cel7B and Cel45A from Humicola insolens and Cel7B, Cell2A and Cel45A core from Trichoderma reesei. J Biotechnol 63:32-40
    • (2002) J Biotechnol , vol.63 , pp. 32-40
    • Karlsson, J.1    Momcilovic, D.2    Wittgren, B.3    Schülein, M.4    Tjerneld, F.5    Brinkman, G.6
  • 39
    • 0025605767 scopus 로고
    • Trends in biochemistry and enzymology of cellulose degradation
    • Klyosov A (1990) Trends in biochemistry and enzymology of cellulose degradation. Biochemistry 29:10577-10585
    • (1990) Biochemistry , vol.29 , pp. 10577-10585
    • Klyosov, A.1
  • 40
    • 0032838958 scopus 로고    scopus 로고
    • Purification and biochemical characteristics of β-D-glucosidase from a thermophilic fungus, Thermomyces lanuginosus-SSBP
    • Lin J, Pillay B, Singh S (1999) Purification and biochemical characteristics of β-D-glucosidase from a thermophilic fungus, Thermomyces lanuginosus-SSBP. Biotechnol Appl Biochem 30:81-87
    • (1999) Biotechnol Appl Biochem , vol.30 , pp. 81-87
    • Lin, J.1    Pillay, B.2    Singh, S.3
  • 41
    • 0028871829 scopus 로고
    • Purification and characterization of the major beta-1,4-endoglucanase from Thermomonospora curvata
    • Lin S, Stutzenberger F (1995) Purification and characterization of the major beta-1,4-endoglucanase from Thermomonospora curvata. J Appl Bacteriol 79:447-53
    • (1995) J Appl Bacteriol , vol.79 , pp. 447-453
    • Lin, S.1    Stutzenberger, F.2
  • 42
    • 0242541601 scopus 로고    scopus 로고
    • Purification and characterization of an endocellulase from the thermophilic fungus Chaetomium thermophilum CT 2
    • Li D-C, Lu M, Li Y-A, Lu J (2003) Purification and characterization of an endocellulase from the thermophilic fungus Chaetomium thermophilum CT 2. Enzyme Microb Technol 33:932-937
    • (2003) Enzyme Microb Technol , vol.33 , pp. 932-937
    • Li, D.-C.1    Lu, M.2    Li, Y.-A.3    Lu, J.4
  • 44
    • 0029890401 scopus 로고    scopus 로고
    • Mannanase activity of endoglucanase III from Trichoderma reesei QM9414
    • Macarron R, Acebal C, Castillon M, Claeyssens M (1996) Mannanase activity of endoglucanase III from Trichoderma reesei QM9414. Biochem Lett 18:599-602
    • (1996) Biochem Lett , vol.18 , pp. 599-602
    • Macarron, R.1    Acebal, C.2    Castillon, M.3    Claeyssens, M.4
  • 46
    • 0028765765 scopus 로고
    • Adsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline cellulose
    • Medve J, Ståhlherg J, Tjerneld F (1994) Adsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline cellulose. Biotechnol Bioeng 44:1064-1073
    • (1994) Biotechnol Bioeng , vol.44 , pp. 1064-1073
    • Medve, J.1    Ståhlherg, J.2    Tjerneld, F.3
  • 48
    • 0003294265 scopus 로고
    • Radial growth responses to temperature by 58 Chaetomium species and some taxonomic relationships
    • Millner PD (1977) Radial growth responses to temperature by 58 Chaetomium species and some taxonomic relationships. Mycologia 69:492-502
    • (1977) Mycologia , vol.69 , pp. 492-502
    • Millner, P.D.1
  • 49
    • 0032079694 scopus 로고    scopus 로고
    • The effect of the initial pore volume and lignin content on the enzymatic hydrolysis of softwoods
    • Mooney C, Mansfield S, Tuohy M, Saddler J (1998) The effect of the initial pore volume and lignin content on the enzymatic hydrolysis of softwoods. Biores Technol 64:113-119
    • (1998) Biores Technol , vol.64 , pp. 113-119
    • Mooney, C.1    Mansfield, S.2    Tuohy, M.3    Saddler, J.4
  • 50
    • 0035811982 scopus 로고    scopus 로고
    • Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70
    • Murray P, Grassick A, Laffey C, Cuffe M, Higgins T, Savage A, Planas A, Tuohy M (2001) Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70. Enzyme Microb Technol 29:90-98
    • (2001) Enzyme Microb Technol , vol.29 , pp. 90-98
    • Murray, P.1    Grassick, A.2    Laffey, C.3    Cuffe, M.4    Higgins, T.5    Savage, A.6    Planas, A.7    Tuohy, M.8
  • 51
    • 0028483694 scopus 로고
    • Specific quantification of Trichoderma reesei cellulases in reconstituted mixtures and its application to cellulose-cellulose binding studies
    • Nidetzky B, Claeyssens M (1994) Specific quantification of Trichoderma reesei cellulases in reconstituted mixtures and its application to cellulose-cellulose binding studies. Biotechnol Bioeng 44:961-966
    • (1994) Biotechnol Bioeng , vol.44 , pp. 961-966
    • Nidetzky, B.1    Claeyssens, M.2
  • 52
    • 0027535915 scopus 로고
    • Synergism of Trichoderma reesei cellulases while degrading different celluloses
    • Nidetzky B, Hayn M, Macarron R, Steiner W (1993) Synergism of Trichoderma reesei cellulases while degrading different celluloses. Biotechnol Lett 151:71-76
    • (1993) Biotechnol Lett , vol.151 , pp. 71-76
    • Nidetzky, B.1    Hayn, M.2    Macarron, R.3    Steiner, W.4
  • 53
    • 0028353231 scopus 로고
    • Cellulose hydrolysis by the cellulases from Trichoderma reesei: A new model for synergistic interaction
    • Nidetzky B, Steiner W, Hayn M, Claeyssens M (1994) Cellulose hydrolysis by the cellulases from Trichoderma reesei: A new model for synergistic interaction. Biochem J 298:705-710
    • (1994) Biochem J , vol.298 , pp. 705-710
    • Nidetzky, B.1    Steiner, W.2    Hayn, M.3    Claeyssens, M.4
  • 54
    • 84985262218 scopus 로고
    • Influence of sugars on the activity of cellulose systems from two basidomycetes cultures
    • Nigam P, Prabhu KA (1991) Influence of sugars on the activity of cellulose systems from two basidomycetes cultures. J Basic Microbiol 31:279-283
    • (1991) J Basic Microbiol , vol.31 , pp. 279-283
    • Nigam, P.1    Prabhu, K.A.2
  • 55
    • 0032534110 scopus 로고    scopus 로고
    • Progress curves a mean for functional classification of cellulases
    • Nutt A, Sild V, Petterson G, Johansson G (1998) Progress curves a mean for functional classification of cellulases. Eur J Biochem 258:200-206
    • (1998) Eur J Biochem , vol.258 , pp. 200-206
    • Nutt, A.1    Sild, V.2    Petterson, G.3    Johansson, G.4
  • 56
    • 2542474192 scopus 로고    scopus 로고
    • Role of oxidative enzymatic treatments on enzymatic hydrolysis of softwood
    • Palonen H, Viikari L (2004) Role of oxidative enzymatic treatments on enzymatic hydrolysis of softwood. Biotechnol Bioeng 86:550-557
    • (2004) Biotechnol Bioeng , vol.86 , pp. 550-557
    • Palonen, H.1    Viikari, L.2
  • 57
    • 19644383897 scopus 로고    scopus 로고
    • Purification and characterization of cellulases (CBH I and EGL 1) produced by thermophilic microorganism Streptomyces sp. M23
    • Park C, Kawaguchi T, Sumitani J, Arai M (2001) Purification and characterization of cellulases (CBH I and EGL 1) produced by thermophilic microorganism Streptomyces sp. M23. Appl Biol Sci 7(1):27-35
    • (2001) Appl Biol Sci , vol.7 , Issue.1 , pp. 27-35
    • Park, C.1    Kawaguchi, T.2    Sumitani, J.3    Arai, M.4
  • 58
    • 0035156434 scopus 로고    scopus 로고
    • Biochemical characterization and mechanism of action of a thermostable β-glucosidase purified from Thermoascus aurantiacus
    • Parry N, Beever D, Owen E, Vandenbergh I, van Beeumen J, Bhat M (2001) Biochemical characterization and mechanism of action of a thermostable β-glucosidase purified from Thermoascus aurantiacus. Biochem J 353:117-127
    • (2001) Biochem J , vol.353 , pp. 117-127
    • Parry, N.1    Beever, D.2    Owen, E.3    Vandenbergh, I.4    van Beeumen, J.5    Bhat, M.6
  • 59
    • 0037102477 scopus 로고    scopus 로고
    • Biochemical characterization and mode of action of a thermostable endoglucanase purified from Thermoascus aurantiacus
    • Parry N, Beever D, Owen E, Nerinckx W, Claeyssens M, Van Beeumen J, Bhat M (2002) Biochemical characterization and mode of action of a thermostable endoglucanase purified from Thermoascus aurantiacus. Arch Biochem Biophys 404:243-253
    • (2002) Arch Biochem Biophys , vol.404 , pp. 243-253
    • Parry, N.1    Beever, D.2    Owen, E.3    Nerinckx, W.4    Claeyssens, M.5    Van Beeumen, J.6    Bhat, M.7
  • 60
    • 0027587608 scopus 로고
    • Study of the enzymatic hydrolysis of cellulose for production of fuel ethanol by the simultaneous saccharification and fermentation process
    • Phillippidis GP, Smith TK, Wyman CE (1993) Study of the enzymatic hydrolysis of cellulose for production of fuel ethanol by the simultaneous saccharification and fermentation process. Biotechnol Bioeng 41:846-853
    • (1993) Biotechnol Bioeng , vol.41 , pp. 846-853
    • Phillippidis, G.P.1    Smith, T.K.2    Wyman, C.E.3
  • 61
    • 0026566601 scopus 로고
    • Purification and characterization of a new endoglucanase from Clostridium thermocellum
    • Romaniec M, Fauth U, Kobayashi T, Huskisson N, Barker P, Demain A (1992) Purification and characterization of a new endoglucanase from Clostridium thermocellum. Biochem J 283:69-73
    • (1992) Biochem J , vol.283 , pp. 69-73
    • Romaniec, M.1    Fauth, U.2    Kobayashi, T.3    Huskisson, N.4    Barker, P.5    Demain, A.6
  • 62
    • 33646017710 scopus 로고    scopus 로고
    • Efficiency of new fungal cellulose systems in boosting enzymatic degradation of barley straw lignocellulose
    • Rosgaard L, Pedersen S, Cherry JR, Harris P, Meyer AS (2006) Efficiency of new fungal cellulose systems in boosting enzymatic degradation of barley straw lignocellulose. Biotechnol Progr 22:493-498
    • (2006) Biotechnol Progr , vol.22 , pp. 493-498
    • Rosgaard, L.1    Pedersen, S.2    Cherry, J.R.3    Harris, P.4    Meyer, A.S.5
  • 63
    • 0025486314 scopus 로고
    • Effect of temperature on the production and location of cellulose components in Myceliopthora thermophila D-14 (ATCC 48104)
    • Roy S, Raha S, Dey S, Chakrabarty S (1990) Effect of temperature on the production and location of cellulose components in Myceliopthora thermophila D-14 (ATCC 48104). Enzyme Microb Technol 12:710-713
    • (1990) Enzyme Microb Technol , vol.12 , pp. 710-713
    • Roy, S.1    Raha, S.2    Dey, S.3    Chakrabarty, S.4
  • 64
    • 0025913198 scopus 로고
    • Thermostable cellobiohydrolase from the thermophilic eubacterium Thermotoga sp. strain FjSS3-B.1: Purification and properties
    • Ruttersmith L, Daniel R (1991) Thermostable cellobiohydrolase from the thermophilic eubacterium Thermotoga sp. strain FjSS3-B.1: purification and properties. Biochem J 277:887-890
    • (1991) Biochem J , vol.277 , pp. 887-890
    • Ruttersmith, L.1    Daniel, R.2
  • 65
    • 0032799265 scopus 로고    scopus 로고
    • The βglycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Enzyme activity and conformational dynamics at temperatures above 100 °C
    • Saboto D, Nucci R, Rossi M, Gryczynski I, Gryczynski Z, Lakowicz J (1999) The βglycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: enzyme activity and conformational dynamics at temperatures above 100 °C. Biophys Chem 81:23-31
    • (1999) Biophys Chem , vol.81 , pp. 23-31
    • Saboto, D.1    Nucci, R.2    Rossi, M.3    Gryczynski, I.4    Gryczynski, Z.5    Lakowicz, J.6
  • 66
    • 0028136713 scopus 로고
    • Production, purification and properties of a thermostable β-glucosidase from a color variant strain of Aureobasidium pullulans
    • Saha B, Freer S, Bothast R (1994) Production, purification and properties of a thermostable β-glucosidase from a color variant strain of Aureobasidium pullulans. Appl Env Microbiol 60:3774-3780
    • (1994) Appl Env Microbiol , vol.60 , pp. 3774-3780
    • Saha, B.1    Freer, S.2    Bothast, R.3
  • 67
    • 0029740205 scopus 로고    scopus 로고
    • Crystal structure of thermostable family 5 endoglucanase EI from Acidothermus cellulolyticus in complex with cellotetraose
    • Sakon J, Adney W, Himmel M, Thomas S, Karplus P (1996) Crystal structure of thermostable family 5 endoglucanase EI from Acidothermus cellulolyticus in complex with cellotetraose. Biochemistry 35:10648-10660
    • (1996) Biochemistry , vol.35 , pp. 10648-10660
    • Sakon, J.1    Adney, W.2    Himmel, M.3    Thomas, S.4    Karplus, P.5
  • 68
    • 85066716546 scopus 로고    scopus 로고
    • Sarker M, Ilias M, Mozammel H (1998) Charaterization of xylanase and CMCase from Rhizomucor pusillus. Bangladesh J Microbiol 15(2):41-47
    • Sarker M, Ilias M, Mozammel H (1998) Charaterization of xylanase and CMCase from Rhizomucor pusillus. Bangladesh J Microbiol 15(2):41-47
  • 69
    • 33746899350 scopus 로고    scopus 로고
    • Bioethanol production based on simultaneous saccharification and fermentation of steam-pretreated salix at high dry-matter content
    • Sassner P, Galbe M, Zacchi G (2006) Bioethanol production based on simultaneous saccharification and fermentation of steam-pretreated salix at high dry-matter content. Enzyme Microb Technol 39:756-762
    • (2006) Enzyme Microb Technol , vol.39 , pp. 756-762
    • Sassner, P.1    Galbe, M.2    Zacchi, G.3
  • 70
    • 0019395842 scopus 로고
    • Substrate specificity and mode of action of the cellulases from the thermophilic fungus Thermoascus aurantiacus
    • Shepherd M, Tong C, Cole A (1981) Substrate specificity and mode of action of the cellulases from the thermophilic fungus Thermoascus aurantiacus. Biochem J 193:67-84
    • (1981) Biochem J , vol.193 , pp. 67-84
    • Shepherd, M.1    Tong, C.2    Cole, A.3
  • 71
    • 0021050307 scopus 로고
    • Characterization and properties of cellulases purified from Trichoderma reesei strain L27
    • Shoemakers, WattK, Tsikovsky G, Cox R (1983) Characterization and properties of cellulases purified from Trichoderma reesei strain L27. Bio/Technology 1:687-690
    • (1983) Bio/Technology , vol.1 , pp. 687-690
    • Shoemakers, W.1    Tsikovsky, G.2    Cox, R.3
  • 72
    • 0034690215 scopus 로고    scopus 로고
    • Effect of substrate and cellulose concentration on simultaneous saccharification and fermentation of steam pretreated softwood for ethanol production
    • Stenberg K, Bollok M, Reczey K, Galbe M, Zacchi G (2000) Effect of substrate and cellulose concentration on simultaneous saccharification and fermentation of steam pretreated softwood for ethanol production. Biotechnol Bioeng 68:204-210
    • (2000) Biotechnol Bioeng , vol.68 , pp. 204-210
    • Stenberg, K.1    Bollok, M.2    Reczey, K.3    Galbe, M.4    Zacchi, G.5
  • 74
    • 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, 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
    • (1999) J Biochem , vol.125 , pp. 728-736
    • Takashima, S.1    Nakamura, A.2    Hidaka, M.3    Masaki, H.4    Uozumi, T.5
  • 75
    • 0034629241 scopus 로고    scopus 로고
    • An α-glucuronidase of Schizophyllum commune acting on polymeric xylan
    • Tenkanen M, Siika-aho M (2000) An α-glucuronidase of Schizophyllum commune acting on polymeric xylan. J Biotechnol 75:149-161
    • (2000) J Biotechnol , vol.75 , pp. 149-161
    • Tenkanen, M.1    Siika-aho, M.2
  • 76
    • 0029043650 scopus 로고
    • CelA, another gene coding for a multidomain cellulases from the extreme thermophile Caldocellum saccharolyticum
    • Te'o V, Saul D, Bergquist P (1995) CelA, another gene coding for a multidomain cellulases from the extreme thermophile Caldocellum saccharolyticum. Appl Microbiol Biotechnol 43:291-296
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 291-296
    • Te'o, V.1    Saul, D.2    Bergquist, P.3
  • 77
    • 0025111144 scopus 로고
    • Adsorption of two cellobiohydrolases from Trichoderma reesei to Avicel: Evidence for exo-exo synergism and possible "loose complex" formation
    • Tomme P, Heriben V, Claeyssens M (1990) Adsorption of two cellobiohydrolases from Trichoderma reesei to Avicel: Evidence for exo-exo synergism and possible "loose complex" formation. Biotechnol Lett 127:525-530
    • (1990) Biotechnol Lett , vol.127 , pp. 525-530
    • Tomme, P.1    Heriben, V.2    Claeyssens, M.3
  • 79
    • 0036005993 scopus 로고    scopus 로고
    • Extracellular β-D-glucosidase from Chaetomium thermophilum var. coprophilum: Production, purification and some properties
    • Venturi L, Polizeli M, Terenzi H, Furriel R, Jorge J (2002) Extracellular β-D-glucosidase from Chaetomium thermophilum var. coprophilum: production, purification and some properties. J Basic Microbiol 42:55-66
    • (2002) J Basic Microbiol , vol.42 , pp. 55-66
    • Venturi, L.1    Polizeli, M.2    Terenzi, H.3    Furriel, R.4    Jorge, J.5
  • 80
    • 0032522362 scopus 로고    scopus 로고
    • The initial kinetics of hydrolysis by cellobiohydrolase I and II is consistent with a cellulose surface - erosion model
    • Väljamäe P, Sild V, Petterson G, Johansson G (1998) The initial kinetics of hydrolysis by cellobiohydrolase I and II is consistent with a cellulose surface - erosion model. Eur J Biochem 253:469-475
    • (1998) Eur J Biochem , vol.253 , pp. 469-475
    • Väljamäe, P.1    Sild, V.2    Petterson, G.3    Johansson, G.4
  • 81
    • 0002027542 scopus 로고
    • Simultaneous saccharification and fermentation of lignocellulose: Process evaluation
    • Wright JD, Wyman CE, Grohmann K (1988) Simultaneous saccharification and fermentation of lignocellulose: process evaluation. Appl Biochem Biotechnol 18:75-90
    • (1988) Appl Biochem Biotechnol , vol.18 , pp. 75-90
    • Wright, J.D.1    Wyman, C.E.2    Grohmann, K.3
  • 82
    • 84967108792 scopus 로고    scopus 로고
    • Properties and gene structure of a bifunctional cellulolytic enzyme (CelA) from the extreme thermophile Anaerocellum thermophilum with separate glycosyl hydrolase family 9 and 48 catalytic domains
    • Zverlov V, Mahr S, Riedel K, Bronnenmeier K (1998) Properties and gene structure of a bifunctional cellulolytic enzyme (CelA) from the extreme thermophile Anaerocellum thermophilum with separate glycosyl hydrolase family 9 and 48 catalytic domains. Microbiology 143:3537-3542
    • (1998) Microbiology , vol.143 , pp. 3537-3542
    • Zverlov, V.1    Mahr, S.2    Riedel, K.3    Bronnenmeier, K.4
  • 83
    • 33847256319 scopus 로고    scopus 로고
    • High temperature enzymatic hydrolysis prior to simultaneous saccharification and fermentation of steam pretreated corn stover for ethanol production
    • Öhgren K, Vehmaanperä J, Siika-aho M, Galbe M, Viikari L, Zacchi G (2007) High temperature enzymatic hydrolysis prior to simultaneous saccharification and fermentation of steam pretreated corn stover for ethanol production. Enzyme Microb Technol 40:607-613
    • (2007) Enzyme Microb Technol , vol.40 , pp. 607-613
    • Öhgren, K.1    Vehmaanperä, J.2    Siika-aho, M.3    Galbe, M.4    Viikari, L.5    Zacchi, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.