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Volumn 50, Issue , 1996, Pages 183-212

Microbial hydrolysis of polysaccharides

Author keywords

1,4 glycanases; amylases; chitinases; domains; families; plant cell walls; starch

Indexed keywords

CELLULOSE; CHITIN; STARCH;

EID: 0029843079     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.50.1.183     Document Type: Review
Times cited : (305)

References (177)
  • 1
    • 0029089678 scopus 로고
    • Characterization of the subunits in an apparently homogeneous subpopulation of Clostridium thermocellum cellulosomes
    • Ali BRS, Remaniec MPM, Hazlewood GP, Freedman RB. 1995. Characterization of the subunits in an apparently homogeneous subpopulation of Clostridium thermocellum cellulosomes. Enzyme Microb. Technol. 17:705-11
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 705-711
    • Ali, B.R.S.1    Remaniec, M.P.M.2    Hazlewood, G.P.3    Freedman, R.B.4
  • 2
    • 0028869675 scopus 로고
    • Cellulases and hemicellulases of the anaerobic fungus Piromyces constitute a multiprotein cellulose-binding complex and are encoded by multigene families
    • la. Ali BRS, Zhou L, Graves FM, Freedman RB, Black GW, et al. 1995. Cellulases and hemicellulases of the anaerobic fungus Piromyces constitute a multiprotein cellulose-binding complex and are encoded by multigene families. FEMS Microbiol. Lett. 125:15-22
    • (1995) FEMS Microbiol. Lett. , vol.125 , pp. 15-22
    • Ali, B.R.S.1    Zhou, L.2    Graves, F.M.3    Freedman, R.B.4    Black, G.W.5
  • 3
    • 0027471408 scopus 로고
    • β-Mannanase of Streptomyces lividans 66: Cloning and DNA sequence of the manA gene and characterization of the enzyme
    • Arcand N, Kluepfel D, Paradis F, Morosoli R, Shareck F. 1993. β-Mannanase of Streptomyces lividans 66: cloning and DNA sequence of the manA gene and characterization of the enzyme. Biochem. J. 290:857-63
    • (1993) Biochem. J. , vol.290 , pp. 857-863
    • Arcand, N.1    Kluepfel, D.2    Paradis, F.3    Morosoli, R.4    Shareck, F.5
  • 4
    • 0028316274 scopus 로고
    • Stereochemical course of the hydrolysis reaction catalyzed by chitinase A1 from Bacillus circulans WL-12
    • Armand S, Tomita H, Heyraud A, Gey C, Watanabe T, Henrissat B. 1994. Stereochemical course of the hydrolysis reaction catalyzed by chitinase A1 from Bacillus circulans WL-12. FEBS Lett. 343:177-80
    • (1994) FEBS Lett. , vol.343 , pp. 177-180
    • Armand, S.1    Tomita, H.2    Heyraud, A.3    Gey, C.4    Watanabe, T.5    Henrissat, B.6
  • 6
    • 0030065736 scopus 로고    scopus 로고
    • Identification of two functionally different classes of exocellulases
    • Barr BK, Hsieh Y-L, Ganem B, Wilson DB. 1996. Identification of two functionally different classes of exocellulases. Biochemistry 35:586-92
    • (1996) Biochemistry , vol.35 , pp. 586-592
    • Barr, B.K.1    Hsieh, Y.-L.2    Ganem, B.3    Wilson, D.B.4
  • 7
    • 0029645413 scopus 로고
    • The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase
    • Barret T, Suresh CG, Tolley SP, Dodson EJ, Hughes MA. 1995. The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase. Structure 3:951-60
    • (1995) Structure , vol.3 , pp. 951-960
    • Barret, T.1    Suresh, C.G.2    Tolley, S.P.3    Dodson, E.J.4    Hughes, M.A.5
  • 8
    • 0027984011 scopus 로고
    • The cellulosome-a treasure trove for biotechnology
    • Bayer EA, Morag E, Lamed R. 1994. The cellulosome-a treasure trove for biotechnology. Trends Biotechnol. 12:379-86
    • (1994) Trends Biotechnol. , vol.12 , pp. 379-386
    • Bayer, E.A.1    Morag, E.2    Lamed, R.3
  • 9
  • 11
    • 0025083002 scopus 로고
    • Production and purification of a granular-starch-binding domain of glucoamylase I from Aspergillus niger
    • Belshaw NJ, Williamson G. 1990. Production and purification of a granular-starch-binding domain of glucoamylase I from Aspergillus niger. FEBS Lett. 269:350-3
    • (1990) FEBS Lett. , vol.269 , pp. 350-353
    • Belshaw, N.J.1    Williamson, G.2
  • 12
    • 0027471206 scopus 로고
    • Specificity of the binding domain of glucoamylase I
    • Belshaw NJ, Williamson G. 1993. Specificity of the binding domain of glucoamylase I. Eur. J. Biochem. 211:717-24
    • (1993) Eur. J. Biochem. , vol.211 , pp. 717-724
    • Belshaw, N.J.1    Williamson, G.2
  • 13
    • 0025029393 scopus 로고
    • Sequencing and expression of a cellodextrinase (ced1) gene from Butyrivibrio fibrisolvens H17c cloned in Escherichia coli
    • Berger E, Jones AW, Jones DT, Woods DR. 1990. Sequencing and expression of a cellodextrinase (ced1) gene from Butyrivibrio fibrisolvens H17c cloned in Escherichia coli. Mol. Gen. Genet. 223:310-18
    • (1990) Mol. Gen. Genet. , vol.223 , pp. 310-318
    • Berger, E.1    Jones, A.W.2    Jones, D.T.3    Woods, D.R.4
  • 14
    • 0024747268 scopus 로고
    • Cloning and sequencing of an endoglucanase (end1) gene from Butyrivibrio fibrisolvens H17c
    • Berger E, Jones WA, Jones DT, Woods DR. 1989. Cloning and sequencing of an endoglucanase (end1) gene from Butyrivibrio fibrisolvens H17c. Mol. Gen. Genet. 219:193-98
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 193-198
    • Berger, E.1    Jones, W.A.2    Jones, D.T.3    Woods, D.R.4
  • 15
    • 10144251219 scopus 로고
    • Molecular genetics of thermophilic bacterial genes coding for enzymes involved in cellulose and hemicellulose degradation
    • ed. K Shimada, S Hosino, K Ohmiya, K Sakka, Y Kobayashi, S Karita. Tokyo: Uni
    • Bergquist PL, Gibbs MD, Saul DJ, Te'O VSJ, Dwivedi PP, Morris D. 1994. Molecular genetics of thermophilic bacterial genes coding for enzymes involved in cellulose and hemicellulose degradation. In Genetics, Biochemistry, and Ecology of Lignocellulose Degradation, ed. K Shimada, S Hosino, K Ohmiya, K Sakka, Y Kobayashi, S Karita. pp. 53-62. Tokyo: Uni
    • (1994) Genetics, Biochemistry, and Ecology of Lignocellulose Degradation , pp. 53-62
    • Bergquist, P.L.1    Gibbs, M.D.2    Saul, D.J.3    Te'O, V.S.J.4    Dwivedi, P.P.5    Morris, D.6
  • 16
    • 0028577780 scopus 로고
    • Isolation of four major subunits from Clostridium thermocellum cellulosome and their synergism in the hydrolysis of crystalline cellulose
    • Bhat S, Goodenough PW, Bhat MK, Owen E. 1994. Isolation of four major subunits from Clostridium thermocellum cellulosome and their synergism in the hydrolysis of crystalline cellulose. Intl. J. Biol. Macromol. 16:335-42
    • (1994) Intl. J. Biol. Macromol. , vol.16 , pp. 335-342
    • Bhat, S.1    Goodenough, P.W.2    Bhat, M.K.3    Owen, E.4
  • 17
    • 0027323001 scopus 로고
    • Characteristics of an exochitinase from Streptomyces olivaceoviridis, its corresponding gene, putative protein domains, and relationship to other chitinases
    • Blaak H, Schnellman J, Walter S, Henrissat B, Schrempf H. 1993. Characteristics of an exochitinase from Streptomyces olivaceoviridis, its corresponding gene, putative protein domains, and relationship to other chitinases. Eur. J. Biochem. 214:659-69
    • (1993) Eur. J. Biochem. , vol.214 , pp. 659-669
    • Blaak, H.1    Schnellman, J.2    Walter, S.3    Henrissat, B.4    Schrempf, H.5
  • 19
  • 20
    • 0028173012 scopus 로고
    • Gene sequence and analysis of protein domains of EGB, a novel family E endoglucanase from Fibrobacter succinogens S85
    • Broussolle V, Forano E, Gaudet G, Ribot Y. 1994. Gene sequence and analysis of protein domains of EGB, a novel family E endoglucanase from Fibrobacter succinogens S85. FEMS Microbiol. Lett. 124:439-48
    • (1994) FEMS Microbiol. Lett. , vol.124 , pp. 439-448
    • Broussolle, V.1    Forano, E.2    Gaudet, G.3    Ribot, Y.4
  • 21
    • 0027973484 scopus 로고
    • Characterization of a chitinase gene (chiA) from Serratia marcescens BJL200 and one-step purification of the gene product
    • Brurberg MB, Eijsink VGH, Nes IF. 1994. Characterization of a chitinase gene (chiA) from Serratia marcescens BJL200 and one-step purification of the gene product. FEMS Microbiol. Lett. 124:399-404
    • (1994) FEMS Microbiol. Lett. , vol.124 , pp. 399-404
    • Brurberg, M.B.1    Eijsink, V.G.H.2    Nes, I.F.3
  • 22
    • 0025922643 scopus 로고
    • Afs, a novel family E endoglucanase gene from Fibrobacter succinogens AR1
    • Cavicchioli R, East PD, Watson K. 1991. Afs, a novel family E endoglucanase gene from Fibrobacter succinogens AR1. J. Bacteriol. 173:3265-68
    • (1991) J. Bacteriol. , vol.173 , pp. 3265-3268
    • Cavicchioli, R.1    East, P.D.2    Watson, K.3
  • 24
    • 0027494513 scopus 로고
    • Molecular analysis of the major cellulase (CelV) of Erwinia carotovora: Evidence for an evolutionary 'mix-and-match' of enzyme domains
    • Cooper VJC, Salmond GPC. 1993. Molecular analysis of the major cellulase (CelV) of Erwinia carotovora: evidence for an evolutionary 'mix-and-match' of enzyme domains. Mol. Gen. Genet. 241:341-50
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 341-350
    • Cooper, V.J.C.1    Salmond, G.P.C.2
  • 26
    • 0028183010 scopus 로고
    • Structural similarities in glucoamylases by hydrophobic cluster analysis
    • Coutinho PM, Reilly PJ. 1994. Structural similarities in glucoamylases by hydrophobic cluster analysis. Protein Eng. 7:749-60
    • (1994) Protein Eng. , vol.7 , pp. 749-760
    • Coutinho, P.M.1    Reilly, P.J.2
  • 27
    • 0028158011 scopus 로고
    • Structure-function relationships in the catalytic and starch binding domains of glucoamylase
    • Coutinho PM, Reilly PJ. 1994. Structure-function relationships in the catalytic and starch binding domains of glucoamylase. Protein Eng. 7:393-400
    • (1994) Protein Eng. , vol.7 , pp. 393-400
    • Coutinho, P.M.1    Reilly, P.J.2
  • 29
    • 0026410590 scopus 로고
    • Characterization of glucoamylase adsorption to raw starch
    • Dalmia BK, Nikolov ZL. 1991. Characterization of glucoamylase adsorption to raw starch. Enzyme Microb. Technol. 13:982-90
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 982-990
    • Dalmia, B.K.1    Nikolov, Z.L.2
  • 30
    • 0027455564 scopus 로고
    • Endoglucanase CasA from alkalophilic Streptomyces strain KSM-9 is a typical member of family B of β-1,4-glucanases
    • Damude HG, Gilkes NR, Kilburn DG, Miller RC Jr, Warren RAJ. 1993. Endoglucanase CasA from alkalophilic Streptomyces strain KSM-9 is a typical member of family B of β-1,4-glucanases. Gene 123:105-7
    • (1993) Gene , vol.123 , pp. 105-107
    • Damude, H.G.1    Gilkes, N.R.2    Kilburn, D.G.3    Miller Jr., R.C.4    Warren, R.A.J.5
  • 31
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G, Henrissat B. 1995. Structures and mechanisms of glycosyl hydrolases. Structure 3:853-59
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 36
    • 0029006062 scopus 로고
    • The multiplicity of domains in proteins
    • Doolittle RF. 1995. The multiplicity of domains in proteins. Annu. Rev. Biochem. 64:287-314
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 287-314
    • Doolittle, R.F.1
  • 37
    • 0029645407 scopus 로고
    • Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5
    • Ducros V, Czjzek M, Belaich A, Gaudin C, Fierobe H-P, et al. 1995. Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5. Structure 3:939-49
    • (1995) Structure , vol.3 , pp. 939-949
    • Ducros, V.1    Czjzek, M.2    Belaich, A.3    Gaudin, C.4    Fierobe, H.-P.5
  • 38
    • 0028136263 scopus 로고
    • Evidence for a polysaccharide-binding domain in Hormoconis resinae glucoamylase P: Effects of its proteolytic removal on substrate specificity and inhibition by β-cyclodextrin
    • Fagerstrom R. 1994. Evidence for a polysaccharide-binding domain in Hormoconis resinae glucoamylase P: effects of its proteolytic removal on substrate specificity and inhibition by β-cyclodextrin. Microbiol. 140:2399-2407
    • (1994) Microbiol. , vol.140 , pp. 2399-2407
    • Fagerstrom, R.1
  • 39
    • 0028786027 scopus 로고
    • The conserved non-catalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain
    • 37a. Fanutti C, Ponyi T, Black GW, Hazlewood GP, Gilbert HJ. 1995. The conserved non-catalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain. J. Biol. Chem. 270:29314-22
    • (1995) J. Biol. Chem. , vol.270 , pp. 29314-29322
    • Fanutti, C.1    Ponyi, T.2    Black, G.W.3    Hazlewood, G.P.4    Gilbert, H.J.5
  • 40
    • 0027386253 scopus 로고
    • The cellulosome: The extracellular organelle of Clostridium
    • Felix CR, Ljungdahl LG. 1993. The cellulosome: the extracellular organelle of Clostridium. Annu. Rev. Microbiol. 47:791-819
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 791-819
    • Felix, C.R.1    Ljungdahl, L.G.2
  • 42
    • 0025365489 scopus 로고
    • Spatial separation of protein domains is not essential for catalytic activity or substrate binding in a xylanase
    • Ferreira LMA, Durrant AJ, Hall J, Hazlewood GP, Gilbert HJ. 1990. Spatial separation of protein domains is not essential for catalytic activity or substrate binding in a xylanase. Biochem. J. 269:261-4
    • (1990) Biochem. J. , vol.269 , pp. 261-264
    • Ferreira, L.M.A.1    Durrant, A.J.2    Hall, J.3    Hazlewood, G.P.4    Gilbert, H.J.5
  • 43
    • 0027231373 scopus 로고
    • A bifunctional enzyme with separate xylanase and β (1,3-1,4) glucanase domains, encoded by the xynD gene of Ruminococcus flavefaciens
    • Flint HJ, Martin J, McPherson CA, Daniel A, Zhang J-X. 1993. A bifunctional enzyme with separate xylanase and β (1,3-1,4) glucanase domains, encoded by the xynD gene of Ruminococcus flavefaciens. J. Bacteriol. 175:2943-51
    • (1993) J. Bacteriol. , vol.175 , pp. 2943-2951
    • Flint, H.J.1    Martin, J.2    McPherson, C.A.3    Daniel, A.4    Zhang, J.-X.5
  • 44
    • 0027989602 scopus 로고
    • Multiplicity and expression of xylanases in the rumen cellulolytic bacterium Ruminococcus flavefaciens
    • Flint HJ, Zhang J-X, Martin J. 1994. Multiplicity and expression of xylanases in the rumen cellulolytic bacterium Ruminococcus flavefaciens. Curr. Microbiol. 29:139-43
    • (1994) Curr. Microbiol. , vol.29 , pp. 139-143
    • Flint, H.J.1    Zhang, J.-X.2    Martin, J.3
  • 45
    • 0027936491 scopus 로고
    • Molecular genetics of obligate anaerobes from the rumen
    • Flint HJ. 1994. Molecular genetics of obligate anaerobes from the rumen. FEMS Microbiol. Lett. 121:259-68
    • (1994) FEMS Microbiol. Lett. , vol.121 , pp. 259-268
    • Flint, H.J.1
  • 46
    • 0028949132 scopus 로고
    • Evidence for a general role for non-catalytic thermostabilizing domains in xylanases from thermophilic bacteria
    • Fontes CMGA, Hazlewood GP, Morag E, Hall J, Hirst BH, Gilbert HJ. 1995. Evidence for a general role for non-catalytic thermostabilizing domains in xylanases from thermophilic bacteria. Biochem. J. 307:151-58
    • (1995) Biochem. J. , vol.307 , pp. 151-158
    • Fontes, C.M.G.A.1    Hazlewood, G.P.2    Morag, E.3    Hall, J.4    Hirst, B.H.5    Gilbert, H.J.6
  • 47
    • 0027168279 scopus 로고
    • Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans
    • Fujii T, Miyashita K. 1993. Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans. J. Gen. Microbiol. 139:677-86
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 677-686
    • Fujii, T.1    Miyashita, K.2
  • 48
    • 0026890950 scopus 로고
    • Cloning of a Clostridium thermocellum DNA fragment encoding polypeptides that bind the catalytic components of the cellulosome
    • Fujino T, Beguin P, Aubert J-P. 1992. Cloning of a Clostridium thermocellum DNA fragment encoding polypeptides that bind the catalytic components of the cellulosome. FEMS Microbiol. Lett. 94:165-70
    • (1992) FEMS Microbiol. Lett. , vol.94 , pp. 165-170
    • Fujino, T.1    Beguin, P.2    Aubert, J.-P.3
  • 49
    • 0029089524 scopus 로고
    • The cellular location of Prevotella ruminicola β-1,4-D-endoglucanase and its occurrence in other strains of ruminai bacteria
    • Gardner RG, Wells JE, Russell JB, Wilson DB. 1995. The cellular location of Prevotella ruminicola β-1,4-D-endoglucanase and its occurrence in other strains of ruminai bacteria. Appl. Environ. Microbiol. 61:3288-92
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3288-3292
    • Gardner, R.G.1    Wells, J.E.2    Russell, J.B.3    Wilson, D.B.4
  • 50
    • 0029146225 scopus 로고
    • 14: Sequence relationships, synergistic interactions, and oxygen sensitivity of a novel enzyme with exoxylanase and β-(1,4)-xylosidase activities
    • 14: sequence relationships, synergistic interactions, and oxygen sensitivity of a novel enzyme with exoxylanase and β-(1,4)-xylosidase activities. Appl. Environ. Microbiol. 61:2958-64
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2958-2964
    • Gasparic, A.1    Martin, J.2    Daniel, A.S.3    Flint, H.J.4
  • 51
    • 0026640499 scopus 로고
    • Homologous catalytic domains of a rumen fungal xylanase: Evidence for gene duplication and prokaryotic origin
    • Gilbert HJ, Hazlewood GP, Laurie JI, Orpin CG, Xue G-P. 1992. Homologous catalytic domains of a rumen fungal xylanase: evidence for gene duplication and prokaryotic origin. Mol. Microbiol. 6:2065-72
    • (1992) Mol. Microbiol. , vol.6 , pp. 2065-2072
    • Gilbert, H.J.1    Hazlewood, G.P.2    Laurie, J.I.3    Orpin, C.G.4    Xue, G.-P.5
  • 52
    • 0026713683 scopus 로고
    • The adsorption of a bacterial cellulase and its two isolated domains to crystalline cellulose
    • Gilkes NR, Jervis E, Henrissat B, Tekant B, Miller RC Jr, et al. 1992. The adsorption of a bacterial cellulase and its two isolated domains to crystalline cellulose. J. Biol. Chem. 267:6743-49
    • (1992) J. Biol. Chem. , vol.267 , pp. 6743-6749
    • Gilkes, N.R.1    Jervis, E.2    Henrissat, B.3    Tekant, B.4    Miller Jr., R.C.5
  • 53
    • 0029150686 scopus 로고
    • Cloning and sequencing of a gene encoding the 69-kDa extracellular chitinase of Janthinobacterium lividum
    • Gleave AP, Taylor RK, Morris BAM, Greenwood DR. 1995. Cloning and sequencing of a gene encoding the 69-kDa extracellular chitinase of Janthinobacterium lividum. FEMS Microbiol. Lett. 131:279-88
    • (1995) FEMS Microbiol. Lett. , vol.131 , pp. 279-288
    • Gleave, A.P.1    Taylor, R.K.2    Morris, B.A.M.3    Greenwood, D.R.4
  • 54
    • 0027170387 scopus 로고
    • Characterization of the cellulose-binding domain of the Clostridium cellulovorans cellulose-binding protein A
    • Goldstein MA, Takagi M, Hashida S, Shoseyov O, Doi RH, Segel IH. 1993. Characterization of the cellulose-binding domain of the Clostridium cellulovorans cellulose-binding protein A. J. Bacteriol. 175:5762-68
    • (1993) J. Bacteriol. , vol.175 , pp. 5762-5768
    • Goldstein, M.A.1    Takagi, M.2    Hashida, S.3    Shoseyov, O.4    Doi, R.H.5    Segel, I.H.6
  • 55
    • 0028139203 scopus 로고
    • Analysis of the raw starch-binding domain by mutation of glucomylase from Aspergillus awamori var. kawachi expressed in Saccharomyces cerevisiae
    • Goto M, Semimaris T, Furukawa K, Hayashida S. 1994. Analysis of the raw starch-binding domain by mutation of glucomylase from Aspergillus awamori var. kawachi expressed in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 60:3926-30
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3926-3930
    • Goto, M.1    Semimaris, T.2    Furukawa, K.3    Hayashida, S.4
  • 56
    • 0030010947 scopus 로고    scopus 로고
    • Cloning, sequencing, and analysis of the gghA gene encoding a 1,4-β-D-glucan glucohydrolase from Microbispora bispora
    • In press
    • Goyal AK, Eveleigh DE. Cloning, sequencing, and analysis of the gghA gene encoding a 1,4-β-D-glucan glucohydrolase from Microbispora bispora. Gene. In press
    • Gene
    • Goyal, A.K.1    Eveleigh, D.E.2
  • 57
    • 0029115396 scopus 로고
    • Crystal and molecular structure at 0.16-nm resolution of the hybrid Bacillus end-1,3-1,4-β-D-glucan 4-glucanohydrolase H(A16-M)
    • Hahn M, Keitel T, Heinemann U. 1995. Crystal and molecular structure at 0.16-nm resolution of the hybrid Bacillus end-1,3-1,4-β-D-glucan 4-glucanohydrolase H(A16-M). Eur. J. Biochem. 232:849-58
    • (1995) Eur. J. Biochem. , vol.232 , pp. 849-858
    • Hahn, M.1    Keitel, T.2    Heinemann, U.3
  • 58
    • 0028812262 scopus 로고
    • Crystal structure and site-directed mutagenesis of Bacillus macerans endo-1,3-1,4-β-glucanase
    • Hahn M, Olsen O, Politz O, Borriss R, Heinemann U. 1995. Crystal structure and site-directed mutagenesis of Bacillus macerans endo-1,3-1,4-β-glucanase. J. Biol. Chem. 270:3081-88
    • (1995) J. Biol. Chem. , vol.270 , pp. 3081-3088
    • Hahn, M.1    Olsen, O.2    Politz, O.3    Borriss, R.4    Heinemann, U.5
  • 59
    • 0029090730 scopus 로고
    • The noncatalytic cellulose-binding domain of a novel cellulase from Pseudomonas fluorescens subsp. cellulosa is important for the efficient hydrolysis of Avicel
    • Hall J, Black GW, Ferreira LMA, Millward-Sadler SJ, Ali BRS, et al. 1995. The noncatalytic cellulose-binding domain of a novel cellulase from Pseudomonas fluorescens subsp. cellulosa is important for the efficient hydrolysis of Avicel. Biochem. J. 309:749-56
    • (1995) Biochem. J. , vol.309 , pp. 749-756
    • Hall, J.1    Black, G.W.2    Ferreira, L.M.A.3    Millward-Sadler, S.J.4    Ali, B.R.S.5
  • 60
    • 0024316572 scopus 로고
    • Nucleotide sequence of the chitinase B gene of Serratia marcescens QMB1466
    • Harpster MH, Dunsmuir P. 1989. Nucleotide sequence of the chitinase B gene of Serratia marcescens QMB1466. Nucl. Acids Res. 17:5395
    • (1989) Nucl. Acids Res. , vol.17 , pp. 5395
    • Harpster, M.H.1    Dunsmuir, P.2
  • 61
    • 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. 280:309-16
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 62
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B, Bairoch A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293:781-88
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 63
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon J-P, Davies G. 1995. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. USA 92:7090-94
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.-P.5    Davies, G.6
  • 64
    • 0027651651 scopus 로고
    • Activity studies of eight purified cellulases: Specificity, synergism, and binding domain effects
    • Irwin DC, Spezio M, Walker LP, Wilson DB. 1993. Activity studies of eight purified cellulases: specificity, synergism, and binding domain effects. Biotechnol. Bioeng. 42:1002-13
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 1002-1013
    • Irwin, D.C.1    Spezio, M.2    Walker, L.P.3    Wilson, D.B.4
  • 65
    • 0027522209 scopus 로고
    • Cloning and sequence analysis of the gene encoding a thermostable chitinase from Streptomyces thermoviolaceus OPC 520
    • Isujibo H, Endo H, Minoura K, Miyamoto K, Inamori Y. 1993. Cloning and sequence analysis of the gene encoding a thermostable chitinase from Streptomyces thermoviolaceus OPC 520. Gene 134:113-17
    • (1993) Gene , vol.134 , pp. 113-117
    • Isujibo, H.1    Endo, H.2    Minoura, K.3    Miyamoto, K.4    Inamori, Y.5
  • 66
    • 0028956984 scopus 로고
    • β-glucosidase, β-galactosidase, family A cellulases, family F xylanases, and two barley glycanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxyterminal ends of b-strands four and seven
    • Jenkins J, Leggio LL, Harris G, Pickersgill R. 1995. β-glucosidase, β-galactosidase, family A cellulases, family F xylanases, and two barley glycanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxyterminal ends of b-strands four and seven. FEBS Lett. 362:281-85
    • (1995) FEBS Lett. , vol.362 , pp. 281-285
    • Jenkins, J.1    Leggio, L.L.2    Harris, G.3    Pickersgill, R.4
  • 67
    • 0026040317 scopus 로고
    • Comparison of the domain-level organization of starch hydrolases and related enzymes
    • Jespersen HM, MacGregor EA, Sierks MR, Svensson B. 1991. Comparison of the domain-level organization of starch hydrolases and related enzymes. Biochem. J. 280:51-55
    • (1991) Biochem. J. , vol.280 , pp. 51-55
    • Jespersen, H.M.1    MacGregor, E.A.2    Sierks, M.R.3    Svensson, B.4
  • 68
    • 0001669533 scopus 로고
    • Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens
    • Jones JDG, Grady KL, Suslow TV, Bedbrook JR. 1986. Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens. EMBO J. 5:467-73
    • (1986) EMBO J. , vol.5 , pp. 467-473
    • Jones, J.D.G.1    Grady, K.L.2    Suslow, T.V.3    Bedbrook, J.R.4
  • 69
    • 0024041235 scopus 로고
    • Cloning of genes of the chitin utilization regulon of Serratia liquefaciens
    • Joshi S, Kozlowski M, Selvaraj G, Iyer VN, Davies RW. 1988. Cloning of genes of the chitin utilization regulon of Serratia liquefaciens. J. Bacteriol. 170:2984-88
    • (1988) J. Bacteriol. , vol.170 , pp. 2984-2988
    • Joshi, S.1    Kozlowski, M.2    Selvaraj, G.3    Iyer, V.N.4    Davies, R.W.5
  • 70
    • 0027165318 scopus 로고
    • DNA sequences and expression in Streptomyces lividans of an exoglucanase gene and an endoglucanase gene from Thermomonospora fusca
    • Jung ED, Lao G, Irwin D, Barr BK, Benjamin A, Wilson DB. 1993. DNA sequences and expression in Streptomyces lividans of an exoglucanase gene and an endoglucanase gene from Thermomonospora fusca. Appl. Environ. Microbiol. 59:3032-43
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3032-3043
    • Jung, E.D.1    Lao, G.2    Irwin, D.3    Barr, B.K.4    Benjamin, A.5    Wilson, D.B.6
  • 71
    • 0029164302 scopus 로고
    • Stereoselective hydrolysis catalyzed by a Bacillus endoglucanase in family D
    • Kawaminami S, Ozaki K, Ito S. 1995. Stereoselective hydrolysis catalyzed by a Bacillus endoglucanase in family D. Biochem. Biophys. Res. Commun. 212:539-43
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 539-543
    • Kawaminami, S.1    Ozaki, K.2    Ito, S.3
  • 72
    • 0024664947 scopus 로고
    • Cloning and expression of Cellulomonas fimi β-glucosidase genes in Escherichia coli
    • Kim HK, Pack MY. 1989. Cloning and expression of Cellulomonas fimi β-glucosidase genes in Escherichia coli. Enzyme Microb. Technol. 11:313-16
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 313-316
    • Kim, H.K.1    Pack, M.Y.2
  • 73
    • 51249172482 scopus 로고
    • Cloning of the gene coding for chitobiase of Serratia marcescens
    • Kless H, Sitrit Y, Chet I, Oppenheim AB. 1989. Cloning of the gene coding for chitobiase of Serratia marcescens. Mol. Gen. Genet. 217:471-73
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 471-473
    • Kless, H.1    Sitrit, Y.2    Chet, I.3    Oppenheim, A.B.4
  • 74
    • 0028901819 scopus 로고
    • Exoglucanase activities of the recombinant Clostridium thermocellum CelS, a major cellulosome component
    • Kruus K, Wang WK, Ching J, Wu JHD. 1995. Exoglucanase activities of the recombinant Clostridium thermocellum CelS, a major cellulosome component. J. Bacteriol. 177:1641-44
    • (1995) J. Bacteriol. , vol.177 , pp. 1641-1644
    • Kruus, K.1    Wang, W.K.2    Ching, J.3    Wu, J.H.D.4
  • 75
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during growth of Saccharomyces cerevisiae
    • Kuranda MJ, Robbins PW. 1991. Chitinase is required for cell separation during growth of Saccharomyces cerevisiae. J. Biol. Chem. 266:19758-67
    • (1991) J. Biol. Chem. , vol.266 , pp. 19758-19767
    • Kuranda, M.J.1    Robbins, P.W.2
  • 76
    • 0029002445 scopus 로고
    • Comparative analyses reveal a highly conserved endoglucanase in the cellulolytic genus Fibrobacter
    • Lin C, Stahl DA. 1995. Comparative analyses reveal a highly conserved endoglucanase in the cellulolytic genus Fibrobacter. J. Bacteriol. 177:2543-49
    • (1995) J. Bacteriol. , vol.177 , pp. 2543-2549
    • Lin, C.1    Stahl, D.A.2
  • 77
    • 0028670445 scopus 로고
    • Cloning and sequencing of an endo-β-1,4-glucanase gene mcenA from Micromonospora cellulolyticum 86W-16
    • Lin F, Marchenko G, Cheng Y-R. 1994. Cloning and sequencing of an endo-β-1,4-glucanase gene mcenA from Micromonospora cellulolyticum 86W-16. J. Ind. Microbiol. 13:344-50
    • (1994) J. Ind. Microbiol. , vol.13 , pp. 344-350
    • Lin, F.1    Marchenko, G.2    Cheng, Y.-R.3
  • 78
    • 0025032040 scopus 로고
    • Cloning, sequencing and analysis of expression of a Butyrivibrio fibrisolvens gene encoding a β-glucosidase
    • Lin L-L, Rumbak E, Zappe H, Thomson JA, Woods DR. 1990. Cloning, sequencing and analysis of expression of a Butyrivibrio fibrisolvens gene encoding a β-glucosidase. J. Gen. Microbiol. 136:1567-76
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 1567-1576
    • Lin, L.-L.1    Rumbak, E.2    Zappe, H.3    Thomson, J.A.4    Woods, D.R.5
  • 79
    • 0025772776 scopus 로고
    • Cloning, sequencing and expression of a gene encoding a 73-kDa xylanase enzyme from the rumen anaerobe Butyrivibrio fibrisolvens H17c
    • Lin L-L, Thomson JA. 1991. Cloning, sequencing and expression of a gene encoding a 73-kDa xylanase enzyme from the rumen anaerobe Butyrivibrio fibrisolvens H17c. Mol. Gen. Genet. 228:55-61
    • (1991) Mol. Gen. Genet. , vol.228 , pp. 55-61
    • Lin, L.-L.1    Thomson, J.A.2
  • 80
    • 0029122231 scopus 로고
    • Purification and characterization of a cellulose-binding β-glucosidase from cellulose-degrading cultures of Phanerochaete chrysosporium
    • Lymar ES, Li B, Enganthan V. 1995. Purification and characterization of a cellulose-binding β-glucosidase from cellulose-degrading cultures of Phanerochaete chrysosporium. Appl. Environ. Microbiol. 61:2976-80
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2976-2980
    • Lymar, E.S.1    Li, B.2    Enganthan, V.3
  • 82
    • 0028170281 scopus 로고
    • Purificaton and characterization of an α-L-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA)
    • Manin C, Shareck F, Morosoli R, Kluepfel D. 1994. Purificaton and characterization of an α-L-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA). Biochem. J. 302:443-9
    • (1994) Biochem. J. , vol.302 , pp. 443-449
    • Manin, C.1    Shareck, F.2    Morosoli, R.3    Kluepfel, D.4
  • 83
    • 0028786960 scopus 로고
    • A new chitosanase gene from a Nocardiodides sp. is a third member of glycosyl hydrolase family 46
    • Masson J-Y, Boucher I, Neugebauer WA, Ramotar D, Brzezinski R. 1995. A new chitosanase gene from a Nocardiodides sp. is a third member of glycosyl hydrolase family 46. Microbiology 141:2629-35
    • (1995) Microbiology , vol.141 , pp. 2629-2635
    • Masson, J.-Y.1    Boucher, I.2    Neugebauer, W.A.3    Ramotar, D.4    Brzezinski, R.5
  • 84
    • 0028265410 scopus 로고
    • Primary sequence of the chitosanase from Streptomyces sp. strain N174 and comparison with other endoglycosidases
    • Masson J-Y, Denis F, Brzezinski R. 1994. Primary sequence of the chitosanase from Streptomyces sp. strain N174 and comparison with other endoglycosidases. Gene 140:103-7
    • (1994) Gene , vol.140 , pp. 103-107
    • Masson, J.-Y.1    Denis, F.2    Brzezinski, R.3
  • 87
    • 0023898294 scopus 로고
    • Isolation and characterization of endoglucanases 1 and 2 from Bacteroides succinogenes
    • McGavin M, Forsberg CW. 1988. Isolation and characterization of endoglucanases 1 and 2 from Bacteroides succinogenes. J. Bacteriol. 170:2914-22
    • (1988) J. Bacteriol. , vol.170 , pp. 2914-2922
    • McGavin, M.1    Forsberg, C.W.2
  • 88
    • 0024401939 scopus 로고
    • Catalytic and substrate-binding domains of endoglucanase 2 from Bacteroides succinogenes
    • McGavin M, Forsberg CW. 1989. Catalytic and substrate-binding domains of endoglucanase 2 from Bacteroides succinogenes. J. Bacteriol. 171:3310-15
    • (1989) J. Bacteriol. , vol.171 , pp. 3310-3315
    • McGavin, M.1    Forsberg, C.W.2
  • 89
    • 0024438787 scopus 로고
    • Structure of the cel-3 gene from Fibrobacter succinogenes S85 and characteristics of the encoded gene product, endoglucanase 3
    • McGavin MJ, Forsberg CW, Crosby B, Bell AW, Dignard D, Thomas DY. 1989. Structure of the cel-3 gene from Fibrobacter succinogenes S85 and characteristics of the encoded gene product, endoglucanase 3. J. Bacteriol. 171:5587-95
    • (1989) J. Bacteriol. , vol.171 , pp. 5587-5595
    • McGavin, M.J.1    Forsberg, C.W.2    Crosby, B.3    Bell, A.W.4    Dignard, D.5    Thomas, D.Y.6
  • 90
    • 0028987862 scopus 로고
    • Enhancement of the endo-β-1,4-glucanase activity of an exocellobiohydrolase by deletion of a surface loop
    • Meinke A, Damude HG, Tomme P, Kwan E, Kilburn DG, et al. 1995. Enhancement of the endo-β-1,4-glucanase activity of an exocellobiohydrolase by deletion of a surface loop. J. Biol. Chem. 270:4383-86
    • (1995) J. Biol. Chem. , vol.270 , pp. 4383-4386
    • Meinke, A.1    Damude, H.G.2    Tomme, P.3    Kwan, E.4    Kilburn, D.G.5
  • 91
    • 8944220513 scopus 로고
    • Molecular biology of the cellulase system of Cellulomonas fimi
    • Meinke A, Warren RAJ. 1993. Molecular biology of the cellulase system of Cellulomonas fimi. Curr. Top. Mol. Genet. 1:65-74
    • (1993) Curr. Top. Mol. Genet. , vol.1 , pp. 65-74
    • Meinke, A.1    Warren, R.A.J.2
  • 92
    • 0028834548 scopus 로고
    • Novel cellulose-binding domains, NodB homologues and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonas fluorescens subsp. cellulosa and Cellvibrio mixtus
    • Millward-Sadler SJ, Davidson K, Hazelwood GP, Black GW, Gilbert HJ, Clarke JH. 1995. Novel cellulose-binding domains, NodB homologues and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonas fluorescens subsp. cellulosa and Cellvibrio mixtus. Biochem. J. 312:39-48
    • (1995) Biochem. J. , vol.312 , pp. 39-48
    • Millward-Sadler, S.J.1    Davidson, K.2    Hazelwood, G.P.3    Black, G.W.4    Gilbert, H.J.5    Clarke, J.H.6
  • 93
    • 0028214219 scopus 로고
    • Evidence for a general role for high-affinity noncatalytic cellulose binding domains in microbial plant cell wall hydrolases
    • Millward-Saddler SJ, Poole DM, Henrissat B, Hazlewood GP, Clarke JH, Gilbert HJ. 1994. Evidence for a general role for high-affinity noncatalytic cellulose binding domains in microbial plant cell wall hydrolases. Mol. Microbiol. 11:375-82
    • (1994) Mol. Microbiol. , vol.11 , pp. 375-382
    • Millward-Saddler, S.J.1    Poole, D.M.2    Henrissat, B.3    Hazlewood, G.P.4    Clarke, J.H.5    Gilbert, H.J.6
  • 94
    • 0027369127 scopus 로고
    • Presence of several cellulose-binding proteins in cell lysate of Fibrobacter succinogenes S85
    • Mitsumori M, Minato H. 1993. Presence of several cellulose-binding proteins in cell lysate of Fibrobacter succinogenes S85. J. Gen. Appl. Microbiol. 39:273-83
    • (1993) J. Gen. Appl. Microbiol. , vol.39 , pp. 273-283
    • Mitsumori, M.1    Minato, H.2
  • 95
    • 0027754185 scopus 로고
    • Purification of cellulose-binding proteins 1 and 2 from cell lysate of Fibrobacter succinogenes S85
    • Mitsumori M, Minato H. 1993. Purification of cellulose-binding proteins 1 and 2 from cell lysate of Fibrobacter succinogenes S85. J. Gen. Appl. Microbiol. 39:361-69
    • (1993) J. Gen. Appl. Microbiol. , vol.39 , pp. 361-369
    • Mitsumori, M.1    Minato, H.2
  • 96
    • 0025834867 scopus 로고
    • Molecular cloning and characterization of chitinase genes from Streptomyces lividans 66
    • Miyashita K, Fujii T, Sawada Y. 1991. Molecular cloning and characterization of chitinase genes from Streptomyces lividans 66. J. Gen. Microbiol. 137:2065-72
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2065-2072
    • Miyashita, K.1    Fujii, T.2    Sawada, Y.3
  • 98
    • 0028990024 scopus 로고
    • Correction of the β-mannanase domain of the celC pseudogene of Caldocellulosiruptor saccharolyticus and activity of the gene product on kraft pulp
    • Morris DD, Reeves RA, Gibbs MD, Saul DJ, Bergquist PL. 1995. Correction of the β-mannanase domain of the celC pseudogene of Caldocellulosiruptor saccharolyticus and activity of the gene product on kraft pulp. Appl. Environ Microbiol. 61:2262-69
    • (1995) Appl. Environ Microbiol. , vol.61 , pp. 2262-2269
    • Morris, D.D.1    Reeves, R.A.2    Gibbs, M.D.3    Saul, D.J.4    Bergquist, P.L.5
  • 100
    • 0023941166 scopus 로고
    • Cloning and nucleotide sequence of a cellulase gene, casA, from an alkalophilic Streptomyces strain
    • Nakai R, Horinouchi S, Beppu T. 1988. Cloning and nucleotide sequence of a cellulase gene, casA, from an alkalophilic Streptomyces strain. Gene 65:229-38
    • (1988) Gene , vol.65 , pp. 229-238
    • Nakai, R.1    Horinouchi, S.2    Beppu, T.3
  • 101
    • 0022486951 scopus 로고
    • Sequence of a cellulase gene of Cellulomonas uda CB4
    • Nakamura K, Misawa N, Kitamura K. 1986. Sequence of a cellulase gene of Cellulomonas uda CB4. J. Biotechnol. 4:247-54
    • (1986) J. Biotechnol. , vol.4 , pp. 247-254
    • Nakamura, K.1    Misawa, N.2    Kitamura, K.3
  • 102
    • 0029361087 scopus 로고
    • Enzyme and microbial systems involved in starch processing
    • Nigam P, Singh D. 1995. Enzyme and microbial systems involved in starch processing. Enzyme Microb. Technol. 17:770-78
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 770-778
    • Nigam, P.1    Singh, D.2
  • 104
    • 0026011001 scopus 로고
    • Enzyme immobilization using a cellulose-binding domain: Properties of a β-glucosidase fusion protein
    • Ong E, Gilkes NR, Miller RC Jr, Warren RAJ, Kilburn DG. 1991. Enzyme immobilization using a cellulose-binding domain: properties of a β-glucosidase fusion protein. Enzyme Microb. Technol. 13:59-65
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 59-65
    • Ong, E.1    Gilkes, N.R.2    Miller Jr., R.C.3    Warren, R.A.J.4    Kilburn, D.G.5
  • 106
    • 0028593509 scopus 로고
    • Protein superfamilies and domain superfolds
    • Orengo CA, Jones DT, Thornton JM. 1994. Protein superfamilies and domain superfolds. Nature 372:631-34
    • (1994) Nature , vol.372 , pp. 631-634
    • Orengo, C.A.1    Jones, D.T.2    Thornton, J.M.3
  • 107
    • 0027421141 scopus 로고
    • The xynC gene from Fibrobacter succinogenes S85 codes for a xylanase with two similar catalytic domains
    • Paradis FW, Zhu H, Krell PJ, Phillips JP, Forsberg FW. 1993. The xynC gene from Fibrobacter succinogenes S85 codes for a xylanase with two similar catalytic domains. J. Bacteriol. 175:7666-72
    • (1993) J. Bacteriol. , vol.175 , pp. 7666-7672
    • Paradis, F.W.1    Zhu, H.2    Krell, P.J.3    Phillips, J.P.4    Forsberg, F.W.5
  • 108
    • 0028774717 scopus 로고
    • Crystal structure of a bacterial chitinase at 2.3 Å resolution
    • Perrakis A, Tews I, Dauter Z, Oppenheim AB, Chet I, et al. 1994. Crystal structure of a bacterial chitinase at 2.3 Å resolution. Structure 2:1169-80
    • (1994) Structure , vol.2 , pp. 1169-1180
    • Perrakis, A.1    Tews, I.2    Dauter, Z.3    Oppenheim, A.B.4    Chet, I.5
  • 109
    • 0027572064 scopus 로고
    • Noncellulolytic fungal β-glucanases: Their physiology and regulation
    • Pitson SM, Seviour RJ, McDougall BM. 1993. Noncellulolytic fungal β-glucanases: their physiology and regulation. Enzyme Microb. Technol. 15:178-9
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 178-179
    • Pitson, S.M.1    Seviour, R.J.2    McDougall, B.M.3
  • 110
    • 0028989403 scopus 로고
    • The gene encoding the β-1,4-endoglucanase (CelA) from Myxococcus xanthus: Evidence for independent acquisition by horizontal transfer of binding and catalytic domains from actinomycetes
    • Quillet L, Barray S, Labedan B, Petit F, Guespin-Michel J. 1995. The gene encoding the β-1,4-endoglucanase (CelA) from Myxococcus xanthus: evidence for independent acquisition by horizontal transfer of binding and catalytic domains from actinomycetes. Gene 158:23-29
    • (1995) Gene , vol.158 , pp. 23-29
    • Quillet, L.1    Barray, S.2    Labedan, B.3    Petit, F.4    Guespin-Michel, J.5
  • 111
    • 0028308476 scopus 로고
    • The 92-kDa chitinase from Streptomyces olivaceoviridis contains a lysine-C endoproteinase at its N-terminus
    • Radwan HH, Plattner HJ, Menge U, Diekmann H. 1994. The 92-kDa chitinase from Streptomyces olivaceoviridis contains a lysine-C endoproteinase at its N-terminus. FEMS Microbiol. Lett. 120:31-36
    • (1994) FEMS Microbiol. Lett. , vol.120 , pp. 31-36
    • Radwan, H.H.1    Plattner, H.J.2    Menge, U.3    Diekmann, H.4
  • 112
    • 0028825707 scopus 로고
    • Low-level endoglucanase contamination in a Trichoderma reesei cellobiohydrolase II preparation affects its enzymatic activity on β-glucan
    • Reinikainen T, Henriksson K, Siika-aho M, Teleman O, Poutanen K. 1995. Low-level endoglucanase contamination in a Trichoderma reesei cellobiohydrolase II preparation affects its enzymatic activity on β-glucan. Enzyme Microb. Technol. 17:888-92
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 888-892
    • Reinikainen, T.1    Henriksson, K.2    Siika-aho, M.3    Teleman, O.4    Poutanen, K.5
  • 113
    • 0023901367 scopus 로고
    • Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli
    • Robbins PW, Albright C, Benfield B. 1988. Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli. J. Biol. Chem. 263:443-47
    • (1988) J. Biol. Chem. , vol.263 , pp. 443-447
    • Robbins, P.W.1    Albright, C.2    Benfield, B.3
  • 114
    • 0026517235 scopus 로고
    • Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus
    • Robbins PW, Overbye K, Albright C, Benfield B, Pero J. 1992. Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus. Gene 111:69-76
    • (1992) Gene , vol.111 , pp. 69-76
    • Robbins, P.W.1    Overbye, K.2    Albright, C.3    Benfield, B.4    Pero, J.5
  • 115
    • 0026772129 scopus 로고
    • Chitinases of Streptomyces olivaceoviridis and significance of processing for multiplicity
    • Romaguera A, Menge U, Breves R, Diekmann H. 1992. Chitinases of Streptomyces olivaceoviridis and significance of processing for multiplicity. J. Bacteriol. 174:3450-54
    • (1992) J. Bacteriol. , vol.174 , pp. 3450-3454
    • Romaguera, A.1    Menge, U.2    Breves, R.3    Diekmann, H.4
  • 116
    • 0028225196 scopus 로고
    • Recognition specificity of the duplicated segments present in Clostridium thermocellum endoglucanase CelD and in the cellulosome-integrating protein CipA
    • Salamitou S, Raynaud O, Lemaire M, Coughlan M, Béguin P, Aubert J-P. 1994. Recognition specificity of the duplicated segments present in Clostridium thermocellum endoglucanase CelD and in the cellulosome-integrating protein CipA. J. Bacteriol. 176:2822-27
    • (1994) J. Bacteriol. , vol.176 , pp. 2822-2827
    • Salamitou, S.1    Raynaud, O.2    Lemaire, M.3    Coughlan, M.4    Béguin, P.5    Aubert, J.-P.6
  • 117
    • 0026772722 scopus 로고
    • Involvement of separate domains of the cellulosomal protein S1 of Clostridium thermocellum in binding to cellulose and in anchoring catalytic subunits to the cellulosome
    • Salamitou S, Tokatlidis K, Béguin P, Aubert J-P. 1992. Involvement of separate domains of the cellulosomal protein S1 of Clostridium thermocellum in binding to cellulose and in anchoring catalytic subunits to the cellulosome. FEBS Lett. 304:89-92
    • (1992) FEBS Lett. , vol.304 , pp. 89-92
    • Salamitou, S.1    Tokatlidis, K.2    Béguin, P.3    Aubert, J.-P.4
  • 119
    • 0026745984 scopus 로고
    • The gene encoding the cellulase (Avicelase) Cell from Streptomyces reticuli and analysis of protein domains
    • Schlochtermeier A, Walter S, Schröder J, Moorman M, Schrempf H. 1992. The gene encoding the cellulase (Avicelase) Cell from Streptomyces reticuli and analysis of protein domains. Mol. Microbiol. 6:3611-21
    • (1992) Mol. Microbiol. , vol.6 , pp. 3611-3621
    • Schlochtermeier, A.1    Walter, S.2    Schröder, J.3    Moorman, M.4    Schrempf, H.5
  • 120
    • 0028070108 scopus 로고
    • The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline α-chitin of fungi and other organisms
    • Schnellman J, Zeltins A, Blaak H, Schrempf H. 1994. The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline α-chitin of fungi and other organisms. Mol. Microbiol. 13:807-19
    • (1994) Mol. Microbiol. , vol.13 , pp. 807-819
    • Schnellman, J.1    Zeltins, A.2    Blaak, H.3    Schrempf, H.4
  • 121
    • 34250080034 scopus 로고
    • Chitinolytic enzymes : Their contribution to basic and applied research
    • Shaikh SA, Deshpande MV. 1993. Chitinolytic enzymes : their contribution to basic and applied research. World J. Microbiol. Biotechnol. 9:468-75
    • (1993) World J. Microbiol. Biotechnol. , vol.9 , pp. 468-475
    • Shaikh, S.A.1    Deshpande, M.V.2
  • 122
    • 0028834125 scopus 로고
    • Analysis of DNA flanking the xlnB locus of Streptomyces lividans reveals genes encoding acetyl xylan esterase and the RNA component of ribonuclease P
    • Shareck F, Biely P, Morosoli R, Kluepfel D. 1995. Analysis of DNA flanking the xlnB locus of Streptomyces lividans reveals genes encoding acetyl xylan esterase and the RNA component of ribonuclease P. Gene 153:105-9
    • (1995) Gene , vol.153 , pp. 105-109
    • Shareck, F.1    Biely, P.2    Morosoli, R.3    Kluepfel, D.4
  • 123
    • 0026045488 scopus 로고
    • Sequences of three genes specifying xylanases in Streptomyces lividans
    • Shareck F, Roy C, Yaguchi M, Morosoli R, Kluepfel D. 1991. Sequences of three genes specifying xylanases in Streptomyces lividans. Gene 107:75-82
    • (1991) Gene , vol.107 , pp. 75-82
    • Shareck, F.1    Roy, C.2    Yaguchi, M.3    Morosoli, R.4    Kluepfel, D.5
  • 124
    • 0029128366 scopus 로고
    • Cellobiohydrolase B, a second exocellobiohydrolase from the cellulolytic bacterium Cellulomonas fimi
    • Shen H, Gilkes NR, Kilburn DG, Miller RC Jr, Warren RAJ. 1995. Cellobiohydrolase B, a second exocellobiohydrolase from the cellulolytic bacterium Cellulomonas fimi. Biochem. J. 311:67-74
    • (1995) Biochem. J. , vol.311 , pp. 67-74
    • Shen, H.1    Gilkes, N.R.2    Kilburn, D.G.3    Miller Jr., R.C.4    Warren, R.A.J.5
  • 126
    • 0025923034 scopus 로고
    • Deletion of the linker connecting the catalytic and cellulose-binding domains of endoglucanase a (CenA) of Cellulomonas fimi alters its conformation and catalytic activity
    • Shen H, Schmuck M, Pilz I, Gilkes NR, Kilburn DG, et al. 1991. Deletion of the linker connecting the catalytic and cellulose-binding domains of endoglucanase A (CenA) of Cellulomonas fimi alters its conformation and catalytic activity. J Biol. Chem. 266:11335-40
    • (1991) J Biol. Chem. , vol.266 , pp. 11335-11340
    • Shen, H.1    Schmuck, M.2    Pilz, I.3    Gilkes, N.R.4    Kilburn, D.G.5
  • 127
    • 0029055875 scopus 로고
    • Cloning and primary structure of the chiA gene from Aeromonas cariae
    • Sitrit Y, Vorgias CE, Cher I, Oppenheim AB. 1995. Cloning and primary structure of the chiA gene from Aeromonas cariae. J. Bacteriol. 177:4187-89
    • (1995) J. Bacteriol. , vol.177 , pp. 4187-4189
    • Sitrit, Y.1    Vorgias, C.E.2    Cher, I.3    Oppenheim, A.B.4
  • 128
    • 0026059796 scopus 로고
    • A new model for enzymatic hydrolysis of cellulose based on the two-domain structure of cellobiohydrolase I
    • Stählberg J, Johansson G, Pettersson G. 1991. A new model for enzymatic hydrolysis of cellulose based on the two-domain structure of cellobiohydrolase I. Bio/Technol. 9:286-90
    • (1991) Bio/Technol. , vol.9 , pp. 286-290
    • Stählberg, J.1    Johansson, G.2    Pettersson, G.3
  • 129
    • 0027298768 scopus 로고
    • Trichoderma reesei has no true exocellulase: All intact and truncated cellulases produce new reducing end groups on cellulose
    • Stählberg J, Johansson G, Pettersson G. 1993. Trichoderma reesei has no true exocellulase: all intact and truncated cellulases produce new reducing end groups on cellulose. Biochim. Biophys. Acta 1157:107-13
    • (1993) Biochim. Biophys. Acta , vol.1157 , pp. 107-113
    • Stählberg, J.1    Johansson, G.2    Pettersson, G.3
  • 130
    • 1842283648 scopus 로고
    • Structure function relationships in starch-hydrolases and related enzymes
    • Svensson B. 1991. Structure function relationships in starch-hydrolases and related enzymes. Denpun Kagaku 38:125-33
    • (1991) Denpun Kagaku , vol.38 , pp. 125-133
    • Svensson, B.1
  • 131
    • 0024430052 scopus 로고
    • Sequence homology between putative raw-starch binding domains from different starch degrading enzymes
    • Svensson B, Jespersen H, Sierks MR, MacGregor EA. 1989. Sequence homology between putative raw-starch binding domains from different starch degrading enzymes. Biochem. J. 264:309-11
    • (1989) Biochem. J. , vol.264 , pp. 309-311
    • Svensson, B.1    Jespersen, H.2    Sierks, M.R.3    MacGregor, E.A.4
  • 132
    • 0027299062 scopus 로고
    • Mutational analysis of glycosylase function
    • Svensson B, Sogaard M. 1993. Mutational analysis of glycosylase function. J. Biotechnol. 29:1-37
    • (1993) J. Biotechnol. , vol.29 , pp. 1-37
    • Svensson, B.1    Sogaard, M.2
  • 133
    • 0026545045 scopus 로고
    • Structure of a β-glucosidase gene from Ruminococcus albus and properties of the translated product
    • Takano M, Moriyama R, Ohmiya K. 1992. Structure of a β-glucosidase gene from Ruminococcus albus and properties of the translated product. J. Ferment. Bioeng. 73:79-88
    • (1992) J. Ferment. Bioeng. , vol.73 , pp. 79-88
    • Takano, M.1    Moriyama, R.2    Ohmiya, K.3
  • 134
    • 0029043650 scopus 로고
    • cel A, another gene coding for a multidomain cellulase enzyme from the extreme thermophile 'Caldocellum saccharolyticum.'
    • Te'O VSJ, Saul DJ, Bergquist PL. 1995. cel A, another gene coding for a multidomain cellulase enzyme from the extreme thermophile 'Caldocellum saccharolyticum.' Appl. Microbiol. Biotechnol. 43:291-96
    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 291-296
    • Te'O, V.S.J.1    Saul, D.J.2    Bergquist, P.L.3
  • 135
    • 0025366083 scopus 로고
    • DNA sequence of a Fibrobacter succinogenes mixed-linkage β-glucanase (1,3-1,4-β-D-glucan 4-glucanohydrolase) gene
    • Teather RM, Erfle JD. 1990. DNA sequence of a Fibrobacter succinogenes mixed-linkage β-glucanase (1,3-1,4-β-D-glucan 4-glucanohydrolase) gene. J. Bacteriol. 172:3837-41
    • (1990) J. Bacteriol. , vol.172 , pp. 3837-3841
    • Teather, R.M.1    Erfle, J.D.2
  • 136
    • 0027478431 scopus 로고
    • Anaerobic fungi and their cellulolytic and xylanolytic enzymes
    • Teunissen MJ, Op den Camp HJM. 1993. Anaerobic fungi and their cellulolytic and xylanolytic enzymes. Antonie van Leeuwenhoek 63:63-76
    • (1993) Antonie Van Leeuwenhoek , vol.63 , pp. 63-76
    • Teunissen, M.J.1    Op Den Camp, H.J.M.2
  • 137
    • 0026522151 scopus 로고
    • Purification and characterization of an endoglucanase from Streptomyces lividans 66 and DNA sequence of the gene
    • Thebérge M, Lacaze P, Shareck F, Morosoli R, Kluepfel D. 1992. Purification and characterization of an endoglucanase from Streptomyces lividans 66 and DNA sequence of the gene. Appl. Environ. Microbiol. 58:815-20
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 815-820
    • Thebérge, M.1    Lacaze, P.2    Shareck, F.3    Morosoli, R.4    Kluepfel, D.5
  • 138
    • 0025940435 scopus 로고
    • Interaction of the duplicated segment carried by Clostridium thermocellum cellulases with cellulosome components
    • Tokatlidis K, Salamitou S, Béguin P, Dhurjati P, Aubert J-P. 1991. Interaction of the duplicated segment carried by Clostridium thermocellum cellulases with cellulosome components. FEBS Lett. 291:185-88
    • (1991) FEBS Lett. , vol.291 , pp. 185-188
    • Tokatlidis, K.1    Salamitou, S.2    Béguin, P.3    Dhurjati, P.4    Aubert, J.-P.5
  • 139
    • 0028181024 scopus 로고
    • An internal cellulose-binding domain mediates adsorption of an engineered bifunctional xylanase/cellulase
    • Tomme P, Gilkes NR, Miller RC Jr, Warren RAJ, Kilburn DG. 1994. An internal cellulose-binding domain mediates adsorption of an engineered bifunctional xylanase/cellulase. Protein Eng. 7:117-23
    • (1994) Protein Eng. , vol.7 , pp. 117-123
    • Tomme, P.1    Gilkes, N.R.2    Miller Jr., R.C.3    Warren, R.A.J.4    Kilburn, D.G.5
  • 140
    • 10144253998 scopus 로고    scopus 로고
    • Characterization of the mixed function β-glucanase CenC, an exo-acting endoglucanase from Cellulomonas fimi hyperexpressed
    • In press
    • Tomme P, Kwan E, Gilkes NR, Kilburn DG, Warren RAJ. Characterization of the mixed function β-glucanase CenC, an exo-acting endoglucanase from Cellulomonas fimi hyperexpressed in Escherichia coli. In press
    • Escherichia Coli.
    • Tomme, P.1    Kwan, E.2    Gilkes, N.R.3    Kilburn, D.G.4    Warren, R.A.J.5
  • 142
    • 0027406938 scopus 로고
    • Amino acid sequence similarities between low molecular weight endo-1,4-β-xylanases and family H cellulases revealed by clustering analysis
    • Törrönen A, Kubicek CP, Henrissat B. 1993. Amino acid sequence similarities between low molecular weight endo-1,4-β-xylanases and family H cellulases revealed by clustering analysis. FEBS Lett. 321:135-39
    • (1993) FEBS Lett. , vol.321 , pp. 135-139
    • Törrönen, A.1    Kubicek, C.P.2    Henrissat, B.3
  • 143
    • 0027534187 scopus 로고
    • Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Alteromonas sp. strain 0-7
    • Tsujibo H, Orikoshi H, Tanno H, Fujimoto K, Miyamoto K, et al. 1993. Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Alteromonas sp. strain 0-7. J. Bacteriol. 175:176-81
    • (1993) J. Bacteriol. , vol.175 , pp. 176-181
    • Tsujibo, H.1    Orikoshi, H.2    Tanno, H.3    Fujimoto, K.4    Miyamoto, K.5
  • 144
    • 0025818617 scopus 로고
    • Sequencing and expression of the Butyrivibrio fibrisolvens xylB gene encoding a novel bifunctional protein with β-D-xylosidase and α-L-arabinofuranosidase activities
    • Utt EA, Eddy CK, Keshav KF, Ingram LO. 1991. Sequencing and expression of the Butyrivibrio fibrisolvens xylB gene encoding a novel bifunctional protein with β-D-xylosidase and α-L-arabinofuranosidase activities. Appl. Environ. Microbiol. 57:1227-34
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1227-1234
    • Utt, E.A.1    Eddy, C.K.2    Keshav, K.F.3    Ingram, L.O.4
  • 145
    • 0025992531 scopus 로고
    • The 1,4-β-D-glucan glucanohydrolases from Phanerochaete chrysosporium. Reassessment of their significance in cellulose degradation mechanisms
    • Uzcategui E, Johansson G, Ek B, Pettersson G. 1991. The 1,4-β-D-glucan glucanohydrolases from Phanerochaete chrysosporium. Reassessment of their significance in cellulose degradation mechanisms. J. Biotechnol. 21:143-60
    • (1991) J. Biotechnol. , vol.21 , pp. 143-160
    • Uzcategui, E.1    Johansson, G.2    Ek, B.3    Pettersson, G.4
  • 146
    • 0025865864 scopus 로고
    • The 1,4-β-D-glucan cellobiohydrolases from P. chrysosporium. a system of synergistically acting enzymes homologous to T. reesei
    • Uzcategui E, Ruiz A, Montesino R, Johansson G, Pettersson G. 1991. The 1,4-β-D-glucan cellobiohydrolases from P. chrysosporium. A system of synergistically acting enzymes homologous to T. reesei. J. Biotechnol. 19:271-86
    • (1991) J. Biotechnol. , vol.19 , pp. 271-286
    • Uzcategui, E.1    Ruiz, A.2    Montesino, R.3    Johansson, G.4    Pettersson, G.5
  • 147
    • 0028828695 scopus 로고
    • Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: Evidence for substrate assisted catalysis
    • van Scheltinga ACT, Armand S, Kalk KH, Isogai A, Henrissat B, Dijkstra BW. 1995. Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry 34:15619-23
    • (1995) Biochemistry , vol.34 , pp. 15619-15623
    • Van Scheltinga, A.C.T.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.5    Dijkstra, B.W.6
  • 148
    • 0028806989 scopus 로고
    • DNA sequence and transcriptional characterization of a β-glucanase gene (celB) from Ruminococcus flavefaciens FD-1
    • Vercoe PE, Finks JL, White BA. 1995. DNA sequence and transcriptional characterization of a β-glucanase gene (celB) from Ruminococcus flavefaciens FD-1. Can. J. Microbiol. 41:869-76
    • (1995) Can. J. Microbiol. , vol.41 , pp. 869-876
    • Vercoe, P.E.1    Finks, J.L.2    White, B.A.3
  • 149
    • 0026742295 scopus 로고
    • DNA sequence and transcription of an endoglucanase gene from Bacteroides (Prevotella) ruminicola AR20
    • Vercoe PE, Gregg K. 1992. DNA sequence and transcription of an endoglucanase gene from Bacteroides (Prevotella) ruminicola AR20. Mol. Gen. Genet. 233:284-92
    • (1992) Mol. Gen. Genet. , vol.233 , pp. 284-292
    • Vercoe, P.E.1    Gregg, K.2
  • 150
    • 0028929728 scopus 로고
    • Nucleotide sequence and transcriptional analysis of the celD β-glucanase gene from Ruminococcus flavefaciens FD-1
    • Vercoe PE, Spight DH, White BA. 1995. Nucleotide sequence and transcriptional analysis of the celD β-glucanase gene from Ruminococcus flavefaciens FD-1. Can J. Microbiol. 41:27-34
    • (1995) Can J. Microbiol. , vol.41 , pp. 27-34
    • Vercoe, P.E.1    Spight, D.H.2    White, B.A.3
  • 152
    • 0027910079 scopus 로고
    • Engineering cellulase mixtures by varying the mole fraction of Thermomonospora fusca E5 and E3, Trichoderma reesei CbhI, and Caldocellum saccharolyticum β-glucosidase
    • Walker LP, Belair CD, Wilson DB, Irwin DC. 1993. Engineering cellulase mixtures by varying the mole fraction of Thermomonospora fusca E5 and E3, Trichoderma reesei CbhI, and Caldocellum saccharolyticum β-glucosidase. Biotechnol. Bioeng. 42:1019-28
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 1019-1028
    • Walker, L.P.1    Belair, C.D.2    Wilson, D.B.3    Irwin, D.C.4
  • 153
    • 0026955779 scopus 로고
    • Fragmentation of cellulose by the major Thermomonospora fusca cellulases, Trichoderma reesei CbhI, and their mixtures
    • Walker LP, Wilson DB, Irwin DC, McQuire C, Price M. 1992. Fragmentation of cellulose by the major Thermomonospora fusca cellulases, Trichoderma reesei CbhI, and their mixtures. Biotechnol. Bioeng. 40:1019-26
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 1019-1026
    • Walker, L.P.1    Wilson, D.B.2    Irwin, D.C.3    McQuire, C.4    Price, M.5
  • 154
    • 0025435119 scopus 로고
    • Measuring fragmentation of cellulose by Thermomonospora fusca cellulase
    • Walker LP, Wilson DB, Irwin DC. 1990. Measuring fragmentation of cellulose by Thermomonospora fusca cellulase. Enzyme Microb. Technol. 12:378-86
    • (1990) Enzyme Microb. Technol. , vol.12 , pp. 378-386
    • Walker, L.P.1    Wilson, D.B.2    Irwin, D.C.3
  • 155
    • 0025334481 scopus 로고
    • Nucleotide sequence of the celA gene encoding a cellodextrinase of Ruminococcus flavefaciens FD-1
    • Wang W, Thomson JA. 1990. Nucleotide sequence of the celA gene encoding a cellodextrinase of Ruminococcus flavefaciens FD-1. Mol. Gen. Genet. 222:265-69
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 265-269
    • Wang, W.1    Thomson, J.A.2
  • 156
    • 0028145771 scopus 로고
    • The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans in chitin degradation
    • Watanabe T, Ito Y, Yamada T, Hashimoto M, Sekine S, Tanaka H. 1994. The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans in chitin degradation. J. Bacteriol. 176:4465-72
    • (1994) J. Bacteriol. , vol.176 , pp. 4465-4472
    • Watanabe, T.1    Ito, Y.2    Yamada, T.3    Hashimoto, M.4    Sekine, S.5    Tanaka, H.6
  • 157
    • 0026578808 scopus 로고
    • Three N-terminal domains of β-1,3-glucanase A1 are involved in binding to insoluble β-1,3-glucan
    • Watanabe T, Kasahara N, Aida K, Tanaka H. 1992. Three N-terminal domains of β-1,3-glucanase A1 are involved in binding to insoluble β-1,3-glucan. J. Bacteriol. 174:186-190
    • (1992) J. Bacteriol. , vol.174 , pp. 186-190
    • Watanabe, T.1    Kasahara, N.2    Aida, K.3    Tanaka, H.4
  • 158
    • 0026571181 scopus 로고
    • Structure of the gene encoding chitinase D of Bacillus circulans WL-12 and possible homology of the enzyme to other prokaryotic chitinases and class III plant chitinases
    • Watanabe T, Oyanagi W, Suzuki K, Ohnishi K, Tanaka H. 1992. Structure of the gene encoding chitinase D of Bacillus circulans WL-12 and possible homology of the enzyme to other prokaryotic chitinases and class III plant chitinases. J. Bacteriol. 174:408-14
    • (1992) J. Bacteriol. , vol.174 , pp. 408-414
    • Watanabe, T.1    Oyanagi, W.2    Suzuki, K.3    Ohnishi, K.4    Tanaka, H.5
  • 159
    • 0025171327 scopus 로고
    • Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to type III homology units of fibronectin
    • Watanabe T, Suzuki K, Oyanagi W, Ohnishi K, Tanaka H. 1990. Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to type III homology units of fibronectin. J. Biol. Chem. 265:15659-65
    • (1990) J. Biol. Chem. , vol.265 , pp. 15659-15665
    • Watanabe, T.1    Suzuki, K.2    Oyanagi, W.3    Ohnishi, K.4    Tanaka, H.5
  • 160
    • 0027233547 scopus 로고
    • Analyses of the gene and amino acid sequence of the Prevotella (Bacteroides) ruminicola 23 xylanase shows unexpected homology with endoglucanases from other species of bacteria
    • Whitehead TR. 1993. Analyses of the gene and amino acid sequence of the Prevotella (Bacteroides) ruminicola 23 xylanase shows unexpected homology with endoglucanases from other species of bacteria. Curr. Microbiol. 27:27-33
    • (1993) Curr. Microbiol. , vol.27 , pp. 27-33
    • Whitehead, T.R.1
  • 161
    • 0026848858 scopus 로고
    • Studies on the cellulase of the rumen anaerobic fungus Neocallimastix frontalis, with special reference to the capacity of the enzyme to degrade crystalline cellulose
    • Wilson CA, Wood TM. 1992. Studies on the cellulase of the rumen anaerobic fungus Neocallimastix frontalis, with special reference to the capacity of the enzyme to degrade crystalline cellulose. Enzyme Microb. Technol. 14:258-64
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 258-264
    • Wilson, C.A.1    Wood, T.M.2
  • 162
    • 0026547982 scopus 로고
    • The anaerobic fungus Neocallimastix frontalis: Isolation and properties of a cellulosome-type enzyme fraction with the capacity to solubilize hydrogen-bond-ordered cellulose
    • Wilson CA, Wood TM. 1992. The anaerobic fungus Neocallimastix frontalis: isolation and properties of a cellulosome-type enzyme fraction with the capacity to solubilize hydrogen-bond-ordered cellulose. Appl. Microbiol. Biotechnol. 37:125-29
    • (1992) Appl. Microbiol. Biotechnol. , vol.37 , pp. 125-129
    • Wilson, C.A.1    Wood, T.M.2
  • 163
    • 0028943508 scopus 로고
    • Approaches to labeling and identification of active site residues in glycosidases
    • Withers SG, Aebersold R. 1995. Approaches to labeling and identification of active site residues in glycosidases. Protein Sci. 4:361-72
    • (1995) Protein Sci. , vol.4 , pp. 361-372
    • Withers, S.G.1    Aebersold, R.2
  • 164
    • 0028349801 scopus 로고
    • Purification and characterization of the CeIB endoglucanase from Streptomyces lividans 66 and DNA sequence of the gene
    • Wittman S, Shareck F, Kluepfel D, Morsoli R. 1994. Purification and characterization of the CeIB endoglucanase from Streptomyces lividans 66 and DNA sequence of the gene. Appl. Environ. Microbiol. 60:1701-3
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1701-1703
    • Wittman, S.1    Shareck, F.2    Kluepfel, D.3    Morsoli, R.4
  • 165
    • 0026443120 scopus 로고
    • Cloning, characterization and nucleotide sequence of a gene encoding Microbispora bispora BglB, a thermostable β-glucosidase expressed in Escherichia coli
    • Wright RM, Yablonsky MD, Shalita ZP, Goyal AK, Eveleigh DE. 1992. Cloning, characterization and nucleotide sequence of a gene encoding Microbispora bispora BglB, a thermostable β-glucosidase expressed in Escherichia coli. Appl. Environ. Microbiol. 58:3455-65
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3455-3465
    • Wright, R.M.1    Yablonsky, M.D.2    Shalita, Z.P.3    Goyal, A.K.4    Eveleigh, D.E.5
  • 166
    • 0001747522 scopus 로고
    • Two components of an extracellular protein aggregate of Clostridium thermocellum together degrade crystalline cellulose
    • Wu JHD, Orme-Johnson WH, Demain AL. 1988. Two components of an extracellular protein aggregate of Clostridium thermocellum together degrade crystalline cellulose. Biochemistry 27:1703-9
    • (1988) Biochemistry , vol.27 , pp. 1703-1709
    • Wu, J.H.D.1    Orme-Johnson, W.H.2    Demain, A.L.3
  • 167
    • 0028809783 scopus 로고
    • 14 β-glucosidase with cellodextrinase and cyanoglycosidase activities
    • 14 β-glucosidase with cellodextrinase and cyanoglycosidase activities. J. Bacteriol. 177:5884-90
    • (1995) J. Bacteriol. , vol.177 , pp. 5884-5890
    • Wulff-Strobel, C.R.1    Wilson, D.B.2
  • 168
    • 0026496063 scopus 로고
    • A novel polysaccharide hydrolase cDNA (celD) from Neocallimastix patriciarum encoding three multi-functional catalytic domains with high endoglucanase, cellobiohydrolase, and xylanase activities
    • Xue G-P, Gobius KS, Orpin CG. 1992. A novel polysaccharide hydrolase cDNA (celD) from Neocallimastix patriciarum encoding three multi-functional catalytic domains with high endoglucanase, cellobiohydrolase, and xylanase activities. J. Gen. Microbiol. 138:2397-2403
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2397-2403
    • Xue, G.-P.1    Gobius, K.S.2    Orpin, C.G.3
  • 169
    • 0026731453 scopus 로고
    • Cloning and expression of multiple cellulase cDNAs from the anaerobic fungus Neocallimastix patriciarum in E. coli
    • Xue G-P, Gobius KS, Orpin CG. 1992. Cloning and expression of multiple cellulase cDNAs from the anaerobic fungus Neocallimastix patriciarum in E. coli. J. Gen. Microbiol. 138:1413-20
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1413-1420
    • Xue, G.-P.1    Gobius, K.S.2    Orpin, C.G.3
  • 171
    • 0025328421 scopus 로고
    • Nucleotide sequence and deletion analysis of the cellulase-encoding gene celH of Clostridium thermocellum
    • Yagüe E, Béguin P, Aubert J-P. 1990. Nucleotide sequence and deletion analysis of the cellulase-encoding gene celH of Clostridium thermocellum. Gene 89:61-67
    • (1990) Gene , vol.89 , pp. 61-67
    • Yagüe, E.1    Béguin, P.2    Aubert, J.-P.3
  • 172
    • 0025012650 scopus 로고
    • Structure of the gene encoding β-1,3-glucanase A1 of Bacillus circulans WL-12
    • Yahata N, Watanabe T, Nakamura Y, Yamamoto Y, Kamimiya S, Tanaka H. 1990. Structure of the gene encoding β-1,3-glucanase A1 of Bacillus circulans WL-12. Gene 86:113-17
    • (1990) Gene , vol.86 , pp. 113-117
    • Yahata, N.1    Watanabe, T.2    Nakamura, Y.3    Yamamoto, Y.4    Kamimiya, S.5    Tanaka, H.6
  • 173
    • 0026539865 scopus 로고
    • Purification of two chitinases from Rhizopus oligosporus and isolation and sequencing of the encoding genes
    • Yanai K, Takaya N, Kojima N, Horiuchi H, Ohta A, Takagi M. 1992. Purification of two chitinases from Rhizopus oligosporus and isolation and sequencing of the encoding genes. J. Bacteriol. 174:7398-7406
    • (1992) J. Bacteriol. , vol.174 , pp. 7398-7406
    • Yanai, K.1    Takaya, N.2    Kojima, N.3    Horiuchi, H.4    Ohta, A.5    Takagi, M.6
  • 174
    • 0026526029 scopus 로고
    • A bifunctional xylanase encoded by the xynA gene of the rumen cellulolytic bacterium Ruminococcus flavefaciens 17 comprises two dissimilar domains linked by an asparagine/glutamine-rich sequence
    • Zhang J-X, Flint HJ. 1992. A bifunctional xylanase encoded by the xynA gene of the rumen cellulolytic bacterium Ruminococcus flavefaciens 17 comprises two dissimilar domains linked by an asparagine/glutamine-rich sequence. Mol. Microbiol. 6:1013-23
    • (1992) Mol. Microbiol. , vol.6 , pp. 1013-1023
    • Zhang, J.-X.1    Flint, H.J.2
  • 175
    • 0028920918 scopus 로고
    • Characterization of a Thermomonospora fusca exocellulase
    • Zhang S, Lao G, Wilson DB. 1995. Characterization of a Thermomonospora fusca exocellulase. Biochemistry 34:3386-95
    • (1995) Biochemistry , vol.34 , pp. 3386-3395
    • Zhang, S.1    Lao, G.2    Wilson, D.B.3
  • 176
    • 0028158580 scopus 로고
    • Intronless celB from the anaerobic fungus Neocallimastix patriciarum encodes a modular family A endoglucanase
    • Zhou L, Xue G-P, Orpin CG, Black GW, Gilbert HJ, Hazlewood GP. 1994. Intronless celB from the anaerobic fungus Neocallimastix patriciarum encodes a modular family A endoglucanase. Biochem. J. 297:359-64
    • (1994) Biochem. J. , vol.297 , pp. 359-364
    • Zhou, L.1    Xue, G.-P.2    Orpin, C.G.3    Black, G.W.4    Gilbert, H.J.5    Hazlewood, G.P.6
  • 177
    • 0028332196 scopus 로고
    • Enzymatic specificities and modes of action of the two catalytic domains of the XynC xylanase from Fibrobacter succinogenes
    • Zhu H, Paradis FW, Krell PJ, Phillips JP, Forsberg CW. 1994. Enzymatic specificities and modes of action of the two catalytic domains of the XynC xylanase from Fibrobacter succinogenes. J. Bacteriol. 176:3885-94
    • (1994) J. Bacteriol. , vol.176 , pp. 3885-3894
    • Zhu, H.1    Paradis, F.W.2    Krell, P.J.3    Phillips, J.P.4    Forsberg, C.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.