메뉴 건너뛰기




Volumn 13, Issue 1, 1996, Pages 101-132

Xylanases: From biology to biotechnology

Author keywords

[No Author keywords available]

Indexed keywords

XYLAN; XYLAN 1,4 BETA XYLOSIDASE; XYLAN ENDO 1,3 BETA XYLOSIDASE; XYLOSE;

EID: 0030334262     PISSN: 02648725     EISSN: 20465556     Source Type: Journal    
DOI: 10.1080/02648725.1996.10647925     Document Type: Article
Times cited : (211)

References (207)
  • 1
    • 0027487614 scopus 로고
    • Enzymes and proteins from organisms that grow ear and above 100°c
    • Adams, M. W. W. (1993). Enzymes and proteins from organisms that grow ear and above 100°C. Annual Review of Microbiology 47, 627-658.
    • (1993) Annual Review of Microbiology , vol.47 , pp. 627-658
    • Adams, M.1
  • 2
    • 0024007897 scopus 로고
    • Degradation of polysaccharides and lignin by ruminai bacteria and fungi
    • Akin, D. E. and Benner, R. (1988). Degradation of polysaccharides and lignin by ruminai bacteria and fungi. Applied and Environmental Microbiology 54, 1117-1125.
    • (1988) Applied and Environmental Microbiology , vol.54 , pp. 1117-1125
    • Akin, D.E.1    Benner, R.2
  • 3
    • 0028869675 scopus 로고
    • Cellulases and hemicellulases of the anaerobic funguspiromvces constitute a muftiprotein cellulose-binding complex and are encoded by multigene families
    • All B. R S., Zhou, L., Graves, F. M., Freedman, R. B., Black, G. W., Gilbert, Hj. and Hazlewood, G. P. (1995). Cellulases and hemicellulases of the anaerobic fungusPiromvces constitute a muftiprotein cellulose-binding complex and are encoded by multigene families. FEMS Microbiology Letters 125, 15-22.
    • (1995) FEMS Microbiology Letters , vol.125 , pp. 15-22
    • All, B.1    Zhou, L.2    Graves, F.M.3    Freedman, R.B.4    Black, G.W.5    Gilbert, H.J.6    Hazlewood, G.P.7
  • 4
    • 0017886341 scopus 로고
    • Multimolecular substrate reactions catalyzed by carbohydrases: Asperglhts orvz. Ae a-amylase degradation of maltooligosaccharides
    • Allen, J. D. and Thoma, J. A. (1978). Multimolecular substrate reactions catalyzed by carbohydrases: Asperglhts orvz. ae a-amylase degradation of maltooligosaccharides. Biochemistry 17, 2338-2344.
    • (1978) Biochemistry , vol.17 , pp. 2338-2344
    • Allen, J.D.1    Thoma, J.A.2
  • 6
    • 0027631061 scopus 로고
    • Cloning and targeted gene disruption of xyll, a beta 1.4-xylanase gene from the maize pathogen cochliobolus carbontim
    • Apel, P. C., Panaccione, D. G., Holden, F. R. and Walton, J. D. (1993). Cloning and targeted gene disruption of XYLl, a beta 1.4-xylanase gene from the maize pathogen Cochliobolus carbontim. Molecular Plant-Microbe Interactions 6, 467-473.
    • (1993) Molecular Plant-Microbe Interactions , vol.6 , pp. 467-473
    • Apel, P.C.1    Panaccione, D.G.2    Holden, F.R.3    Walton, J.D.4
  • 7
    • 84945039885 scopus 로고
    • The roie of fungus-fiber contact in ihe biobleaching of kraft brownstock by trameies (Coriolus) versicolor
    • Archibald, F. S. (1992). The roie of fungus-fiber contact in ihe biobleaching of kraft brownstock by Trameies (coriolus) versicolor. Holforschung 46, 305-310.
    • (1992) Holforschung , vol.46 , pp. 305-310
    • Archibald, F.S.1
  • 8
    • 0027934796 scopus 로고
    • Effects of disruption of xylanase-eneoding genes on the xykinolytic system of streptomvces lividans
    • Armin, F. F., Shareck, F., Kluepfel, D. and Morosoli, R. (1994). Effects of disruption of xylanase-eneoding genes on the xykinolytic system of Streptomvces lividans. Journal of Bacteriology 16, 4924-4930.
    • (1994) Journal of Bacteriology , vol.16 , pp. 4924-4930
    • Armin, F.F.1    Shareck, F.2    Kluepfel, D.3    Morosoli, R.4
  • 9
    • 0028304351 scopus 로고
    • Identification and characterization of clustered genes for thermostable xylan-degrading enzymes, bela-xylosidase and xylanase. Of bacillus stearothermophiltts-22
    • Baba, T., Shinke, R. and Nanmorï, T. (1994). Identification and characterization of clustered genes for thermostable xylan-degrading enzymes, bela-xylosidase and xylanase. of Bacillus stearothermophiltts-22. Appl Environ Microb 60, 2252-2258.
    • (1994) Appl Environ Microb , vol.60 , pp. 2252-2258
    • Baba, T.1    Shinke, R.2    Nanmorï, T.3
  • 11
    • 0026583354 scopus 로고
    • Efficient fermentation of pinussp acid hydrolysates by an ethanologenic strain of escherichia coli
    • Barbosa, M. D. S., Bock, M. J., Fein, J. E., Pons, D. and Ingram, L. O. (1992). Efficient fermentation of Pinussp acid hydrolysates by an ethanologenic strain of Escherichia coli. Applied and Environmental Microbiology 58, 1382-1384.
    • (1992) Applied and Environmental Microbiology , vol.58 , pp. 1382-1384
    • Barbosa, M.1    Bock, M.J.2    Fein, J.E.3    Pons, D.4    Ingram, L.O.5
  • 12
    • 0024788874 scopus 로고
    • Biology of gut anaerobic fungi
    • Bauchop, T. (1989). Biology of gut anaerobic fungi. BioSystems 23, 53-64.
    • (1989) Biosystems , vol.23 , pp. 53-64
    • Bauchop, T.1
  • 13
    • 0022512490 scopus 로고
    • Infrastructure of the cell surface cellulosome of c. Ihermocelhmt and its interaction with cellulose
    • Bayer, E. A. and Lamed, R. (1986). infrastructure of the cell surface cellulosome of C. ihermocelhmt and its interaction with cellulose. Journal of Bacteriology 167, 828-836.
    • (1986) Journal of Bacteriology , vol.167 , pp. 828-836
    • Bayer, E.A.1    Lamed, R.2
  • 14
    • 0001095062 scopus 로고
    • Fermentation of pentoses from wood hydrolysates
    • J. N. Saddler, CAB International, UK. Wallingford
    • Beck, M. J. (1993). Fermentation of pentoses from wood hydrolysates, in Bioconversion of forest and agricultural plant residues. (J. N. Saddler, Eds). Vol. 9, pp. 211-229. CAB International, UK. Wallingford.
    • (1993) Bioconversion of Forest and Agricultural Plant Residues , vol.9 , pp. 211-229
    • Beck, M.J.1
  • 15
    • 0025168749 scopus 로고
    • Molecular biology of cellulose degradation
    • Béguin, P. (1990). Molecular biology of cellulose degradation. Annual Review of Microbiology 44, 219-248.
    • (1990) Annual Review of Microbiology , vol.44 , pp. 219-248
    • Béguin, P.1
  • 17
    • 0026749529 scopus 로고
    • Cellulose degradation by clostridium thermo-cellum: From manure to molecular biology
    • Béguin, P., Millet, J. and Aubert, J. P. (1992). Cellulose degradation by Clostridium thermo-cellum: From manure to molecular biology. FEMS Microbiology Letters 100, 523-528.
    • (1992) FEMS Microbiology Letters , vol.100 , pp. 523-528
    • Béguin, P.1    Millet, J.2    Aubert, J.P.3
  • 18
    • 0022386956 scopus 로고
    • Microbial xyianolytic systems
    • Blely, P. (1985). Microbial xyianolytic systems. Trends in Biotechnol 3, 286-290.
    • (1985) Trends in Biotechnol , vol.3 , pp. 286-290
    • Blely, P.1
  • 19
    • 0003131715 scopus 로고
    • Biochemical aspects of the production of microbial hemicelluiases
    • M. P. Coughlan and G. P. Hazlevvood, Portland Press, Cambridge
    • Biely, P. (1993). Biochemical aspects of the production of microbial hemicelluiases. In Hemicellulose and hemicellulases. (M. P. Coughlan and G. P. Hazlevvood. Eds). pp. 29-51. Portland Press, Cambridge.
    • (1993) Hemicellulose and Hemicellulases , pp. 29-51
    • Biely, P.1
  • 20
    • 0021759937 scopus 로고
    • Glycosidic bond rearrangements in isomeric xyiobiose by yeast xylan-degrading enzymes
    • Blely, P. and Petraková, E. (1984a). Glycosidic bond rearrangements in isomeric xyiobiose by yeast xylan-degrading enzymes. FEBS Lettersers 178, 323-326.
    • (1984) FEBS Lettersers , vol.178 , pp. 323-326
    • Blely, P.1    Petraková, E.2
  • 21
    • 0021174999 scopus 로고
    • Novel inducers of the xylan-degrading enzyme system of cryptococcus albidus
    • Blely, P. and Petráková, E. (1984b). Novel inducers of the xylan-degrading enzyme system of Cryptococcus albidus. Journal of Bacteriology 160, 408-412.
    • (1984) Journal of Bacteriology , vol.160 , pp. 408-412
    • Blely, P.1    Petráková, E.2
  • 22
    • 0019869086 scopus 로고
    • Substrate-binding site of endo-l. 4-ß-xylanase of the yeast crvptococcus albidus
    • Biely, P., Krátky, Z. and Vrsanská, M. (1981). Substrate-binding site of endo-l. 4-ß-xylanase of the yeast Crvptococcus albidus. European Journal of Biochemistry 119, 559-559.
    • (1981) European Journal of Biochemistry , vol.119 , pp. 559-559
    • Biely, P.1    Krátky, Z.2    Vrsanská, M.3
  • 23
    • 0020580149 scopus 로고
    • The active site of an acidic endo-1, 4-ß-xylanase of aspergillus niger
    • Biely, P., Vrsanská, M. and Gorbachev A.V. I. (1983). The active site of an acidic endo-1, 4-ß-xylanase of Aspergillus niger. Biochimica and Biophysica Acta 743, 155-161.
    • (1983) Biochimica and Biophysica Acta , vol.743 , pp. 155-161
    • Biely, P.1    Vrsanská, M.2    Gorbachev, A.3
  • 24
    • 0019857533 scopus 로고
    • Mechanisms of substrate digestion by endo-1, 4-ß-xylanase of cryptococcus albidus
    • Biely, P., Vrsanská, M. and Krátky, M. (1981). MECHANISMS OF SUBSTRATE DIGESTION BY ENDO-1, 4-ß-xylanase of Cryptococcus albidus. European Journal of Biochemistry 119, 565-571.
    • (1981) European Journal of Biochemistry , vol.119 , pp. 565-571
    • Biely, P.1    Vrsanská, M.2    Krátky, M.3
  • 25
    • 0018857071 scopus 로고
    • Xylan-degrading enzymes of the yeast crvptococcus albidus. Identification and cellular localization
    • Blely, P., Vrsanská, M. and Kratky, Z. (1980). Xylan-degrading enzymes of the yeast Crvptococcus albidus. Identification and cellular localization. European Journal of Biochemistry 108, 313-321.
    • (1980) European Journal of Biochemistry , vol.108 , pp. 313-321
    • Blely, P.1    Vrsanská, M.2    Kratky, Z.3
  • 26
    • 0018899930 scopus 로고
    • Induction and inducers of endo-1-4-ß-xylanase in the y east crvptococcus albidus
    • Biely, P., Krátky, Z., Vrsanská, M. and Urmanicova, D. (1980). Induction and inducers of endo-1-4-ß-xylanase in the y east Crvptococcus albidus. European Journal of Biochemistry 108, 323-329.
    • (1980) European Journal of Biochemistry , vol.108 , pp. 323-329
    • Biely, P.1    Krátky, Z.2    Vrsanská, M.3    Urmanicova, D.4
  • 27
    • 0023029475 scopus 로고
    • Cooperativity of esterases and xylanases in the enzymatic degradation of acetyl xylan
    • Biely, P., Mackenzie, C. R., Puls, J. and Schneider, H. (1986). Cooperativity of esterases and xylanases in the enzymatic degradation of acetyl xylan. Biotechnology 4, 731-733.
    • (1986) Biotechnology , vol.4 , pp. 731-733
    • Biely, P.1    Mackenzie, C.R.2    Puls, J.3    Schneider, H.4
  • 28
    • 0027536224 scopus 로고
    • Mode of action of three endo-ß-1-4 xylanases of streptoniyces lividans
    • Biely, P., Kluepiel, R., Morosoli, R. and Sharek, F. (1993). Mode of action of three endo-ß-1-4 xylanases of Streptoniyces lividans. Biochimica and Biophysica Acta 1162, 246-254.
    • (1993) Biochimica and Biophysica Acta , vol.1162 , pp. 246-254
    • Biely, P.1    Kluepiel, R.2    Morosoli, R.3    Sharek, F.4
  • 30
    • 0028207144 scopus 로고
    • Xylanase b from neocallimastix patriciarum contains a non-catalytic 455-residue i inker sequence comprised of 57 repeats of an octapeptide
    • Black, G. W., Hallewood, G. P., Xue, G. P., Orpin, C. G. and Gilbert, H. J. (1994). Xylanase B from Neocallimastix patriciarum contains a non-catalytic 455-residue I inker sequence comprised of 57 repeats of an octapeptide. Biochemical Journal 299, 381-387.
    • (1994) Biochemical Journal , vol.299 , pp. 381-387
    • Black, G.W.1    Hallewood, G.P.2    Xue, G.P.3    Orpin, C.G.4    Gilbert, H.J.5
  • 32
    • 0024657936 scopus 로고
    • Fermentation products and plant cell wali-degrading enzymes produced by monocentric and polycentric anaerobic ruminai fungi
    • Borneman, W. S., Akin, D. E. and Ljungdahl, L. G. (1989). Fermentation products and plant cell wali-degrading enzymes produced by monocentric and polycentric anaerobic ruminai fungi. Applied and Environmental Microbiology 55, 1066-1073.
    • (1989) Applied and Environmental Microbiology , vol.55 , pp. 1066-1073
    • Borneman, W.S.1    Akin, D.E.2    Ljungdahl, L.G.3
  • 34
    • 0026448264 scopus 로고
    • Purification and partial characterization of two feruloyl esterases from the anaerobic fungus neocallimastix strain mc-2
    • Borneman, W. S., Ljungdahl, L. G., Hartley, R. D. and Akin, D. E. (1992). Purification and partial characterization of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC-2. Applied and Environmental Microbiology 58, 3762-3766.
    • (1992) Applied and Environmental Microbiology , vol.58 , pp. 3762-3766
    • Borneman, W.S.1    Ljungdahl, L.G.2    Hartley, R.D.3    Akin, D.E.4
  • 35
    • 0028346601 scopus 로고
    • Fermentation of l-arabinosc, d-xylose and d-glucose by ethanologenic recombinant klebsiella oxytoca strain p2
    • Bothast, R. J., Saha, B. C., Flosenzier, A. V. and Ingram, L. O. (1994). Fermentation of L-arabinosc, D-xylose and D-glucose by ethanologenic recombinant Klebsiella oxytoca strain P2. Biotechnol Lett 16, 401-406.
    • (1994) Biotechnol Lett , vol.16 , pp. 401-406
    • Bothast, R.J.1    Saha, B.C.2    Flosenzier, A.V.3    Ingram, L.O.4
  • 36
    • 0025168177 scopus 로고
    • Essential carboxy groups in xylanase a
    • Bray, M. R. and Clarke, A. J. (1990). Essential carboxy groups in xylanase A. Biochemical Journal 270, 91-96.
    • (1990) Biochemical Journal , vol.270 , pp. 91-96
    • Bray, M.R.1    Clarke, A.J.2
  • 37
    • 0026540828 scopus 로고
    • Action pattern of xyio-oxigosaccharide hydrolysis by schizophyllum commune xylanase a
    • Bray, M. R. and Clarke, A. J. (1992). Action pattern of xyio-oxigosaccharide hydrolysis by Schizophyllum commune xylanase A. European Journal of Biochemistry 204, 191-196.
    • (1992) European Journal of Biochemistry , vol.204 , pp. 191-196
    • Bray, M.R.1    Clarke, A.J.2
  • 38
    • 0028084395 scopus 로고
    • Identification of a glutamate residue at the active-site of xylanase a from schizophyllum commune
    • Bray, M. R. and Clarke, A. J. (1994). Identification of a glutamate residue at the active-site of xylanase A from Schizophyllum commune. European Journal of Biochemistry 219, 821-827.
    • (1994) European Journal of Biochemistry , vol.219 , pp. 821-827
    • Bray, M.R.1    Clarke, A.J.2
  • 40
    • 0026608164 scopus 로고
    • Conversion of xylan to ethanol by ethanologenic strains of escherichia coli and klebsiella oxytoca
    • Burchhardt, G. and Ingram, L. O. (1992). Conversion of xylan to ethanol by ethanologenic strains of Escherichia coli and Klebsiella oxytoca. Applied and Environmental Microbiology 58, 1128-1133.
    • (1992) Applied and Environmental Microbiology , vol.58 , pp. 1128-1133
    • Burchhardt, G.1    Ingram, L.O.2
  • 41
    • 0026744443 scopus 로고
    • Chromosomal and genetic analysis of the electrophoretic karyotype of trichoderma reesei: Mapping of the cellulase and xylanase genes
    • Carter, G. L., Allison, D., Rey, M. W. and Dunn, C. N. (1992). Chromosomal and genetic analysis of the electrophoretic karyotype of Trichoderma reesei: mapping of the cellulase and xylanase genes. Molecular Microbiology 6: 2167-2174.
    • (1992) Molecular Microbiology , vol.6 , pp. 2167-2174
    • Carter, G.L.1    Allison, D.2    Rey, M.W.3    Dunn, C.N.4
  • 42
    • 0026668809 scopus 로고
    • Site-directed mutagenesis of essential carboxylic residues in clostridium theimocellum endoglucanase cel d
    • Chauvaux, S., Béguin, P. and Aubert, J. (1992). Site-directed mutagenesis of essential carboxylic residues in Clostridium theimocellum endoglucanase Cel D. Journal of Biological Chemistry 267, 4472-4478.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 4472-4478
    • Chauvaux, S.1    Béguin, P.2    Aubert, J.3
  • 43
    • 0014558453 scopus 로고
    • Mechanism of lysozyme action
    • Chipman, D. M. and Sharon, N. (1969). Mechanism of lysozyme action. Science 165, 454-465.
    • (1969) Science , vol.165 , pp. 454-465
    • Chipman, D.M.1    Sharon, N.2
  • 44
    • 0027051606 scopus 로고
    • Specificity mapping of cellulolytic enzymes: Classification into families of structurally related proteins confirmed by biochemical analysis
    • Claeyssens, M. and Henrissat, B. (1992), Specificity mapping of cellulolytic enzymes: classification into families of structurally related proteins confirmed by biochemical analysis. Protein Science I, 1293-1297.
    • (1992) Protein Science I , pp. 1293-1297
    • Claeyssens, M.1    Henrissat, B.2
  • 45
    • 0021865554 scopus 로고
    • The role of carboxyl groups in the function of endo-ß-1, 4-glucanase from schizophyllum commune
    • Clarke, A. J. and Yaguchi, M. (1985). The role of carboxyl groups in the function of endo-ß-1, 4-glucanase from Schizophyllum commune. European Journal of Biochemistry 149, 233-238.
    • (1985) European Journal of Biochemistry , vol.149 , pp. 233-238
    • Clarke, A.J.1    Yaguchi, M.2
  • 46
    • 0026503034 scopus 로고
    • The binding of cellulomonas endoglucanase c (Cenc) to cellulose and sephadex is mediated by the n-terminal repeats
    • Coutinho, J. B., Gllkes, N. R., Warren, D. G. and Miller R. C. (1992). The binding of Cellulomonas endoglucanase C (CenC) to cellulose and Sephadex is mediated by the N-terminal repeats. Molec Microbiol 6, 1243-1252.
    • (1992) Molec Microbiol , vol.6 , pp. 1243-1252
    • Coutinho, J.B.1    Gllkes, N.R.2    Warren, D.G.3    Miller, R.C.4
  • 47
    • 0028140060 scopus 로고
    • Two different, adjacent and divergent zinc finger binding sites are necessary for crea-mediated carbon catabolite repression in the proiine gene cluster of aspergillus nidulans
    • Cuuero, B. and Scazzocchio, C. (1994). Two different, adjacent and divergent zinc finger binding sites are necessary for CREA-mediated carbon catabolite repression in the proiine gene cluster of Aspergillus nidulans. EMBO Journal 13, 407-415.
    • (1994) EMBO Journal , vol.13 , pp. 407-415
    • Cuuero, B.1    Scazzocchio, C.2
  • 48
    • 0003004012 scopus 로고
    • Biotechnological modification of lignin structure and composition in forest trees
    • Dean, J. F. D. and Eriksson, K. E. L. (1992). Biotechnological modification of lignin structure and composition in forest trees. Holzforschung 46, 135-147.
    • (1992) Holzforschung , vol.46 , pp. 135-147
    • Dean, J.1    Eriksson, K.2
  • 49
    • 0025018850 scopus 로고
    • Purification and properties of an endo-1, 4-xylanase excreted by a hydrolytic thermophilic anaerobe. Clostridium thermolacticum. A proposal for its action mechanism on larchwood 4-0-methylglucuronoxylan
    • Debesre, P., Priem, B., Strecker, G. and Vignon, M. (1990). Purification and properties of an endo-1, 4-xylanase excreted by a hydrolytic thermophilic anaerobe. Clostridium thermolacticum. A proposal for its action mechanism on larchwood 4-0-methylglucuronoxylan. European Journal of Biochemistry 187, 573-580.
    • (1990) European Journal of Biochemistry , vol.187 , pp. 573-580
    • Debesre, P.1    Priem, B.2    Strecker, G.3    Vignon, M.4
  • 50
    • 0026848872 scopus 로고
    • Positional isomers of thioxylobiose. Their synthesis and inducing ability for d-xylan-degrading enzymes in the yeast ciyptococcus albidus
    • Defaye, J., Guillot, J. M., Biely, P. and Vrsanská, M. (1992). Positional isomers of thioxylobiose. their synthesis and inducing ability for D-xylan-degrading enzymes in the yeast Ciyptococcus albidus. Carbohydrate Research 228, 47-64.
    • (1992) Carbohydrate Research , vol.228 , pp. 47-64
    • Defaye, J.1    Guillot, J.M.2    Biely, P.3    Vrsanská, M.4
  • 51
    • 0028365483 scopus 로고
    • Regulation of the xylanase-eneoding. V/h/l gene of aspergillus tubigensis
    • Degraaff, L. H., Vandenbroeck, H. C., V Anooijen, A. J. J. and Vlsser, B. (1994). Regulation of the xylanase-eneoding. v/H/l gene of Aspergillus tubigensis. Molec Microl 12, 479-490.
    • (1994) Molec Microl , vol.12 , pp. 479-490
    • Degraaff, L.H.1    Vandenbroeck, H.C.2    Vanooijen, A.3    Vlsser, B.4
  • 52
    • 1542596333 scopus 로고
    • Developmental control of enzyme production and cell wall modification in rust fungi, and defense reactions of the host plant
    • (U. Stahl and P. Ttidzynski. Eds), VCH-Verlag. Weinheim. FRG
    • Dhising, H. and Mendgen, K. (1991). Developmental control of enzyme production and cell wall modification in rust fungi, and defense reactions of the host plant. In Molecular Biology of Filamentous Fungi. (U. Stahl and P. Ttidzynski. Eds), pp. 27-44. VCH-Verlag. Weinheim. FRG.
    • (1991) Molecular Biology of Filamentous Fungi , pp. 27-44
    • Dhising, H.1    Mendgen, K.2
  • 53
    • 0028070908 scopus 로고
    • Crysial-slructure. At 2.6-angstrom resolution, of the streptomxces livijans xylanase a, a member of the f-family of beta-Î, 4-d-glycanases
    • Derewenda, I., Swenson, L., Green, R., Wei, Y. Y., Morosoli, R., Si Iareck, F., Klueppeu D. and Derewenda, Z. S. (1994). Crysial-slructure. at 2.6-angstrom resolution, of the Streptomxces liviJans xylanase A, a member of the f-family of beta-Î, 4-D-glycanases. Journal of Biological Chemistry 269, 20811-20814.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 20811-20814
    • Derewenda, I.1    Swenson, L.2    Green, R.3    Wei, Y.Y.4    Morosoli, R.5    Si Iareck, F.6    Klueppeu, D.7    Derewenda, Z.S.8
  • 55
    • 0017870220 scopus 로고
    • Enzyme mechanisms involved in cellulose hydrolysis by the rot fungus sporotrichtmt pulverulentum
    • Eriksson, K. R. L (1978). Enzyme mechanisms involved in cellulose hydrolysis by the rot fungus Sporotrichtmt pulverulentum. Biotechnology and Bioengineering 70, 317-332.
    • (1978) Biotechnology and Bioengineering , vol.70 , pp. 317-332
    • Eriksson, K.1
  • 56
    • 85024031741 scopus 로고
    • A biotechnological approach to pulp bleaching
    • (M. P. Coughlan, Eds), Elsevier Applied Science. New York
    • Eriksson, K. E. L. (1989). A biotechnological approach to pulp bleaching. In Enzyme Systems for Lignocelhtlose Degradation. (M. P. Coughlan, Eds), pp. 101-109. Elsevier Applied Science. New York.
    • (1989) Enzyme Systems for Lignocelhtlose Degradation , pp. 101-109
    • Eriksson, K.1
  • 57
    • 34249959547 scopus 로고
    • Biotechnology in the pulp and paper industry
    • Eriksson, K. E. L. (1990). Biotechnology in the pulp and paper industry. Wood Science Technology 24, 79-101.
    • (1990) Wood Science Technology , vol.24 , pp. 79-101
    • Eriksson, K.1
  • 59
    • 0016040572 scopus 로고
    • Pleiotropic mutants of the wood-rotting fungus polypoms adustus lacking cellulose, mannanase and xylanase
    • Eriksson, K. E. L. and Goodell, E. W. (1974). Pleiotropic mutants of the wood-rotting fungus Polypoms adustus lacking cellulose, mannanase and xylanase. Canadian Journal of Microbiology 20, 371-378.
    • (1974) Canadian Journal of Microbiology , vol.20 , pp. 371-378
    • Eriksson, K.1    Goodell, E.W.2
  • 60
    • 0001807070 scopus 로고
    • Structural studies on the chemical bonds between lignins and carbohydrates in spruce woods
    • Eriksson, Ö., Goring, D. A. I. and Lindgren, B. O. (1980). Structural studies on the chemical bonds between lignins and carbohydrates in spruce woods. Wood Science Technology 14, 267-279.
    • (1980) Wood Science Technology , vol.14 , pp. 267-279
    • Eriksson1    Goring, D.2    Lindgren, B.O.3
  • 62
    • 0025954878 scopus 로고
    • The purification and characterization of 4-hydroxy-3-methoxycinnamic (Feruiic) acid esterase fromstreptomycesolivochromogenes
    • Faulds, C. B. and Williamson, G. (1991). The purification and characterization of 4-hydroxy-3-methoxycinnamic (feruiic) acid esterase fromStreptomycesolivochromogenes, Journal of General Microbiology 137, 2339-2345.
    • (1991) Journal of General Microbiology , vol.137 , pp. 2339-2345
    • Faulds, C.B.1    Williamson, G.2
  • 63
    • 0027386253 scopus 로고
    • The cellulosome: The exocellular organeile of clostridium
    • Felix, R. C. and Ljungdahl, L. G. (1993). The cellulosome: The exocellular organeile of Clostridium. Annual Review of Microbiology 47, 791-819.
    • (1993) Annual Review of Microbiology , vol.47 , pp. 791-819
    • Felix, R.C.1    Ljungdahl, L.G.2
  • 64
    • 0025365489 scopus 로고
    • Spatial separation of protein domains is not necessary for catalytic activity or substrate binding in a xylanase
    • Ferreira, L. M., Durrant, A. J., Hall, J., Hazlewood, G. P. and Gilbert, H. J. (1990). Spatial separation of protein domains is not necessary for catalytic activity or substrate binding in a xylanase. Biochemical Journal 269, 261-264.
    • (1990) Biochemical Journal , vol.269 , pp. 261-264
    • Ferreira, L.M.1    Durrant, A.J.2    Hall, J.3    Hazlewood, G.P.4    Gilbert, H.J.5
  • 65
    • 0027169343 scopus 로고
    • A modular esterase from pseudomonas fluorescens subsp. Cellubsa contains a non-calalytic cellulose binding domain
    • Ferreira, L. M., Wood, T. M., Williamson, G., Faulds, C., Hazlewood, G. P., Black, G. W. and Gilber T. H. J. (1993). A modular esterase from Pseudomonas fluorescens subsp. cellubsa contains a non-calalytic cellulose binding domain. Biochemical Journal 294, 349-355.
    • (1993) Biochemical Journal , vol.294 , pp. 349-355
    • Ferreira, L.M.1    Wood, T.M.2    Williamson, G.3    Faulds, C.4    Hazlewood, G.P.5    Black, G.W.6    Gilber, T.7
  • 66
    • 0027231373 scopus 로고
    • A biftmc-tional enzyme, with separate xylanase and beta(1, 3-1, 4)-glucanase domains, encoded by the xvnd gene of rittninococcusflavefuciens
    • Flint, H. J., Martin, J., Mcpherson, C. A., Daniel, A. S. and Zhang, J. X. (1993). A biftmc-tional enzyme, with separate xylanase and beta(1, 3-1, 4)-glucanase domains, encoded by the xvnD gene of Rittninococcusflavefuciens. Journal of Bacteriology 175, 2943-2951.
    • (1993) Journal of Bacteriology , vol.175 , pp. 2943-2951
    • Flint, H.J.1    Martin, J.2    McPherson, C.A.3    Daniel, A.S.4    Zhang, J.X.5
  • 67
    • 0026505539 scopus 로고
    • Characterization and comparison of clostridium ceuubvorans endoglucanases-xylanases engb and engd hyperexpressed in escherichia coli
    • Foong, F. C. and Doi, R. H. (1992). Characterization and comparison of Clostridium ceUubvorans endoglucanases-xylanases EngB and EngD hyperexpressed in Escherichia coli. Journal of Bacteriology 174, 1403-1409.
    • (1992) Journal of Bacteriology , vol.174 , pp. 1403-1409
    • Foong, F.C.1    Doi, R.H.2
  • 68
    • 27244461764 scopus 로고
    • The mechanism of ß-glycosidases: A reassessment of some seminal papers
    • Franck, R. W. (1992). The mechanism of ß-glycosidases: A reassessment of some seminal papers. Bioorganic Chemistry 20, 77-88.
    • (1992) Bioorganic Chemistry , vol.20 , pp. 77-88
    • Franck, R.W.1
  • 69
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyze amino acid sequences
    • Gahoriaud, C., Blssey, V., Benctietrit, T. and Mornon, J. P. (1987). Hydrophobic cluster analysis: An efficient new way to compare and analyze amino acid sequences. FEBS Letters 224, 149-155.
    • (1987) FEBS Letters , vol.224 , pp. 149-155
    • Gahoriaud, C.1    Blssey, V.2    Benctietrit, T.3    Mornon, J.P.4
  • 70
    • 0024042175 scopus 로고
    • Expression of the bacillus subtilis xvl operon is repressed at the level of transcription and is induced by xylose
    • Gärtner, D., Geissendöreer, M. and Hillen, W. (1988). Expression of the Bacillus subtilis xvl operon is repressed at the level of transcription and is induced by xylose. Journal of Bacteriology 170, 3102-3109.
    • (1988) Journal of Bacteriology , vol.170 , pp. 3102-3109
    • Gärtner, D.1    Geissendöreer, M.2    Hillen, W.3
  • 73
    • 0023474814 scopus 로고
    • Evidence for nmiiiple carboxy methy icel lu i ase genes in pseudomonas fluorescence subsp. Ccllulosa
    • Gilbert, H. J., Jenkins, G., Sullivan, D. A. and Hai, L. J. (1987). Evidence for nmiiiple carboxy methy Icel lu I ase genes in Pseudomonas fluorescence subsp. ccllulosa. Molecular and General Genetic. s 210, 551-556.
    • (1987) Molecular and General Genetic. S , vol.210 , pp. 551-556
    • Gilbert, H.J.1    Jenkins, G.2    Sullivan, D.A.3    Hai, L.J.4
  • 74
    • 0025353263 scopus 로고
    • The n-terminal region of an endoglucanase from pseudomonas fluorescens subspecies celluiosa constitutes a cellulose-binding domain that is distinct from the catalytic centre
    • Gilbert, H. J., Hai, L. J., Hazlewood, G. P. and Ferreira, L. M. (1990). The N-terminal region of an endoglucanase from Pseudomonas fluorescens subspecies celluiosa constitutes a cellulose-binding domain that is distinct from the catalytic centre. Molecular Microbiology 4, 759-767.
    • (1990) Molecular Microbiology , vol.4 , pp. 759-767
    • Gilbert, H.J.1    Hai, L.J.2    Hazlewood, G.P.3    Ferreira, L.M.4
  • 75
    • 0026640499 scopus 로고
    • Homologous catalytic domains in a rumen fungal xylanase: Evidence for gene duplication and prokaryotic origin
    • Gilbert, H. J., Hazlewood, G. P., Laurie, J. İ., Orpin, C. G. and Xue, G. P. (1992). Homologous catalytic domains in a rumen fungal xylanase: evidence for gene duplication and prokaryotic origin. Molecular Microbiology 6, 2065-2072.
    • (1992) Molecular Microbiology , vol.6 , pp. 2065-2072
    • Gilbert, H.J.1    Hazlewood, G.P.2    Laurie, J.3    Orpin, C.G.4    Xue, G.P.5
  • 77
    • 0025804758 scopus 로고
    • Domains in microbial ß-1, 4-glycanases: Sequence conservation, function, and enzyme families
    • Gílkes, N. R., Henrissat, B., Kilburn, D. G., Miller-Jr, R. C. and Warren, R. A. (1991). Domains in microbial ß-1, 4-glycanases: sequence conservation, function, and enzyme families. Microbiological Reviews 55, 303-315.
    • (1991) Microbiological Reviews , vol.55 , pp. 303-315
    • Gílkes, N.R.1    Henrissat, B.2    Kilburn, D.G.3    Miller-Jr, R.C.4    Warren, R.A.5
  • 78
    • 0024448551 scopus 로고
    • Structural and functional analysis of a bacterial celiulase by proteolysis
    • Gilkes, N. R., Warren, D. G., Miller-Jr, R. C. and Warren, R. A. J. (1989). Structural and functional analysis of a bacterial celiulase by proteolysis. Journal of Biological Chemistry 264, 17802-17808.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 17802-17808
    • Gilkes, N.R.1    Warren, D.G.2    Miller-Jr, R.C.3    Warren, R.4
  • 79
    • 0024297010 scopus 로고
    • Precise excision of the cellulose binding domain from two cclluhmonas fimi cellulases by a homologous protease and the effect on catalysis
    • Gilkes, N. R., Warren, R. A. J., Miller-Jr, R. C. and Kilburn, D. G. (1988). Precise excision of the cellulose binding domain from two Cclluhmonas fimi cellulases by a homologous protease and the effect on catalysis. Journal of Biological Chemistry 263, 10401-10407.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 10401-10407
    • Gilkes, N.R.1    Warren, R.2    Miller-Jr, R.C.3    Kilburn, D.G.4
  • 80
    • 0024506247 scopus 로고
    • Regulation of the production of hemicellulolytic and cellulolvtic enzymes by astreptoınyces sp. Growing on lignoceliulose
    • Godden, B., Legon, T., Helvenstein, P. and Penninckx, M. (1989). Regulation of the production of hemicellulolytic and cellulolvtic enzymes by aStreptoınyces sp. growing on lignoceliulose. Journal of General Microbiology 135, 285-292.
    • (1989) Journal of General Microbiology , vol.135 , pp. 285-292
    • Godden, B.1    Legon, T.2    Helvenstein, P.3    Penninckx, M.4
  • 81
    • 0344913883 scopus 로고
    • Chemicals from wood and other biomass. Part 1: Future supply of organic chemicals
    • Goheen, D. W. (1981). Chemicals from wood and other biomass. Part 1: Future supply of organic chemicals. Journal of Chemical Education 58, 465-468.
    • (1981) Journal of Chemical Education , vol.58 , pp. 465-468
    • Goheen, D.W.1
  • 82
    • 0027201148 scopus 로고
    • Production of a high level cellulase-free xylanase by the thermophilic fungus thermomyces lanuginosus in laboratory and pilot scale using lignocellulosic materials
    • Gomes, J., Purkarthofer, H., Hayn, M., Kappmoller, J., Sínner, M. and Steiner, W. (1993). Production of a high level cellulase-free xylanase by the thermophilic fungus Thermomyces lanuginosus in laboratory and pilot scale using lignocellulosic materials. Applied Microbiology and Technology 39, 700-707.
    • (1993) Applied Microbiology and Technology , vol.39 , pp. 700-707
    • Gomes, J.1    Purkarthofer, H.2    Hayn, M.3    Kappmoller, J.4    Sínner, M.5    Steiner, W.6
  • 83
    • 0025748793 scopus 로고
    • Two beta-glycanase genes arc clustered in bacillus polymyxa: Molecular cloning, expression, and sequence analysis of genes encoding a xylanase and an endo-beta-(1, 3)-(1, 4)-glucanase
    • Gosalbes, M. J., Perez, G. J., Gonzalez, R. and Navarro, A. (1991). Two beta-glycanase genes arc clustered in Bacillus polymyxa: molecular cloning, expression, and sequence analysis of genes encoding a xylanase and an endo-beta-(1, 3)-(1, 4)-glucanase. Journal of Bacteriology 173, 7705-7710.
    • (1991) Journal of Bacteriology , vol.173 , pp. 7705-7710
    • Gosalbes, M.J.1    Perez, G.J.2    Gonzalez, R.3    Navarro, A.4
  • 85
  • 86
    • 0024722941 scopus 로고
    • Conserved serine-rich sequences in xylanase and celiulase from pseudomonasfluorescens subspecies cellulosa: Internal signal sequence and unusual protein processing
    • Hall, J., Hazlewood, G. P., Huskisson, N. S., Durrant, A. J. and Gilbert, H. J. (1989). Conserved serine-rich sequences in xylanase and celiulase from Pseudomonasfluorescens subspecies cellulosa: internal signal sequence and unusual protein processing. Molecular Microbiology 3, 1211-1219.
    • (1989) Molecular Microbiology , vol.3 , pp. 1211-1219
    • Hall, J.1    Hazlewood, G.P.2    Huskisson, N.S.3    Durrant, A.J.4    Gilbert, H.J.5
  • 88
  • 90
    • 1542386612 scopus 로고
    • Cellulolytic enzymes of the obligately biotroph rust fungus uromyces viciae-fabae are regulated differentiation-specifically
    • Heiler, S., Mendgen, K. and Deising, H. (1993). Cellulolytic enzymes of the obligately biotroph rust fungus Uromyces viciae-fabae are regulated differentiation-specifically. Mycological Research 97, 77-85.
    • (1993) Mycological Research , vol.97 , pp. 77-85
    • Heiler, S.1    Mendgen, K.2    Deising, H.3
  • 91
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and Bairoch, A. (1993). New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochemical Journal 293, 781-788.
    • (1993) Biochemical Journal , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 92
    • 0024419181 scopus 로고
    • Celiulase families revealed by hydrophobic cluster analysis
    • Henrissat, B., Claeyssens, M., Tomme, P., Lemesle, I. and Mornon, J. P. (1989). Celiulase families revealed by hydrophobic cluster analysis. Gene 81, 83-95.
    • (1989) Gene , vol.81 , pp. 83-95
    • Henrissat, B.1    Claeyssens, M.2    Tomme, P.3    Lemesle, I.4    Mornon, J.P.5
  • 93
    • 0025508612 scopus 로고
    • Physiology and genetics of xylan degradation by gastrointestinal tract bacteria
    • Hespell, R. B. and Whitehead, T. R. (1990). Physiology and genetics of xylan degradation by gastrointestinal tract bacteria. Journal of Dairy Science 73, 3013-3022.
    • (1990) Journal of Dairy Science , vol.73 , pp. 3013-3022
    • Hespell, R.B.1    Whitehead, T.R.2
  • 94
    • 0024516271 scopus 로고
    • Differences in active site structure in a family of beta-glucan endohydroiases deduced from the kinetics of inactivation by epoxyalky i beta-oligogiucosides
    • Høj, P. B., Rodriguez, E. B., Stick, R. V. and Stone, B. A. (1989). DIFFERENCES IN ACTIVE SITE STRUCTURE IN A FAMILY OF BETA-GLUCAN ENDOHYDROIASES DEDUCED FROM THE KINETICS OF INACTIVATION BY EPOXYALKY I BETA-OLIGOGIUCOSIDES. JOURNAL OF BIOLOGICAL CHEMISTRY. 264, 4939-4947.
    • (1989) JOURNAL OF BIOLOGICAL CHEMISTRY , vol.264 , pp. 4939-4947
    • Høj, P.B.1    Rodriguez, E.B.2    Stick, R.V.3    Stone, B.A.4
  • 95
    • 0022576842 scopus 로고
    • Specificity of celiulase and ß-xylanase induction in trichoderma reesei
    • Hrmová, M., Blely, P. and Vrsanskâ, M. (1986). Specificity of celiulase and ß-xylanase induction in Trichoderma reesei. Archives of Microbiology 144, 307-311.
    • (1986) Archives of Microbiology , vol.144 , pp. 307-311
    • Hrmová, M.1    Blely, P.2    Vrsanskâ, M.3
  • 96
    • 0024729057 scopus 로고
    • Cellulose-and xylan-degrading enzymes of aspergillus terreus and aspergillus niger
    • Hrmova, M., Biely, P. and Vrsanskâ, M. (1989). Cellulose-and xylan-degrading enzymes of Aspergillus terreus and Aspergillus niger. Enzyme and Microbial Technology 11, 610-616.
    • (1989) Enzyme and Microbial Technology , vol.11 , pp. 610-616
    • Hrmova, M.1    Biely, P.2    Vrsanskâ, M.3
  • 97
    • 0026029476 scopus 로고
    • Induction of ceilulose-and xylan-degrading enzyme systems in aspergillus terreus by homo-and heterodisaccharides composed of glucose and xyiose
    • Hrmová, M., Petráková, E. and Blely, P. (1991). Induction of ceilulose-and xylan-degrading enzyme systems in Aspergillus terreus by homo-and heterodisaccharides composed of glucose and xyiose. Journal of General Microbiology 137, 541-547.
    • (1991) Journal of General Microbiology , vol.137 , pp. 541-547
    • Hrmová, M.1    Petráková, E.2    Blely, P.3
  • 98
    • 0028907495 scopus 로고
    • Catabolite repression in bacillus subtilis: A global regulatory mechanism for the gram-positive bacteria?
    • Hueck, C. J. and Hillen, W. (1995). Catabolite repression in Bacillus subtilis: a global regulatory mechanism for the Gram-positive bacteria? Molecular Microbiology 15, 395-401.
    • (1995) Molecular Microbiology , vol.15 , pp. 395-401
    • Hueck, C.J.1    Hillen, W.2
  • 99
    • 0017668198 scopus 로고
    • Chemical modification of celiulase from aspergillus niger
    • Hurst, P. L., Sullivan, P. A. and Shepherd, M. G. (1977). Chemical modification of celiulase from Aspergillus niger. Biochemical Journal 167, 549-556.
    • (1977) Biochemical Journal , vol.167 , pp. 549-556
    • Hurst, P.L.1    Sullivan, P.A.2    Shepherd, M.G.3
  • 100
    • 0028116250 scopus 로고
    • Strain selection, taxonomy, and genetics of xylose-fermenting yeasts
    • Jeffries, T. W. and Kurtzman, C. P. (1994). Strain selection, taxonomy, and genetics of xylose-fermenting yeasts. Enzyme and Microbial Technology 16, 922-932.
    • (1994) Enzyme and Microbial Technology , vol.16 , pp. 922-932
    • Jeffries, T.W.1    Kurtzman, C.P.2
  • 101
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen, R. A. (1976). Enzyme recruitment in evolution of new function. Annual Review of Microbiology 30, 409-425.
    • (1976) Annual Review of Microbiology , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 102
    • 0010739909 scopus 로고
    • Ultrastructure of the plant cell wall: Biochemical viewpoint
    • New Series
    • Kato, K. (1981). Ultrastructure of the plant cell wall: biochemical viewpoint. Encyclopedia of Plant Physiology, New Series 13B, 29-46.
    • (1981) Encyclopedia of Plant Physiology , vol.13B , pp. 29-46
    • Kato, K.1
  • 103
    • 0000377115 scopus 로고
    • Isolation and identification of 0-(5-0-feruloyl-oc-l-arabin of uranosyl)-(l->3)-0-ß-d-xylopyranosyl-(l->4)-d-xylopyranose as a component of zea shoot cell walls
    • Kato, Y. and Nevins, D. J. (1985). Isolation and identification of 0-(5-0-feruloyl-oc-L-arabin of uranosyl)-(l->3)-0-ß-D-xylopyranosyl-(l->4)-D-xylopyranose as a component of Zea shoot cell walls. Carbohydrate Research 137, 139-150.
    • (1985) Carbohydrate Research , vol.137 , pp. 139-150
    • Kato, Y.1    Nevins, D.J.2
  • 104
    • 0025605798 scopus 로고
    • Xylanase b and an arabin of uranosidase from pseudomonas fluorescens subsp. Cellulosa contain identical cellulose binding domains and are encoded by adjacent genes
    • Kellett, L. E., Poole, D. M., Ferreira, L. M., Durrant, A. J., Hazlewood, G. P. and Gilbert, H. J. (1990). Xylanase B and an arabin of uranosidase from Pseudomonas fluorescens subsp. cellulosa contain identical cellulose binding domains and are encoded by adjacent genes. Biochemical Journal 272, 369-376.
    • (1990) Biochemical Journal , vol.272 , pp. 369-376
    • Kellett, L.E.1    Poole, D.M.2    Ferreira, L.M.3    Durrant, A.J.4    Hazlewood, G.P.5    Gilbert, H.J.6
  • 105
    • 0026542662 scopus 로고
    • Characterization and sequencing of an active site cysteine containing peptide from the xylanase of a themiotolerant strepto-myces
    • Keskar, S. S., Rao, M. B. and Deshpande, V. V. (1992). Characterization and sequencing of an active site cysteine containing peptide from the xylanase of a themiotolerant Strepto-myces. Biochemical Journal 281, 601-605.
    • (1992) Biochemical Journal , vol.281 , pp. 601-605
    • Keskar, S.S.1    Rao, M.B.2    Deshpande, V.V.3
  • 107
    • 0025270742 scopus 로고
    • Purification and characterization of a new xylanase (Xylanase b) produced by streptomyces lividans 66
    • Kluepfel, D., Vats, M. S., Aumont, F., Shareck, F. and Morosoli, R. (1990). Purification and characterization of a new xylanase (xylanase B) produced by Streptomyces lividans 66. Biochemical Journal 267, 45-50.
    • (1990) Biochemical Journal , vol.267 , pp. 45-50
    • Kluepfel, D.1    Vats, M.S.2    Aumont, F.3    Shareck, F.4    Morosoli, R.5
  • 109
    • 0025742882 scopus 로고
    • Purification and characterization of a (L, 4)-ß-arabinoxylanarabin of uranohydroiase from aspergillus awamori
    • Kormelink, Searije-Van Leeuwen, M. J. F., Wood, T. M. and Voragen, A. G. J. (1991). Purification and characterization of a (l, 4)-ß-arabinoxylanarabin of uranohydroiase from Aspergillus awamori. Applied Microbiology and Biotechnology 35, 753-758.
    • (1991) Applied Microbiology and Biotechnology , vol.35 , pp. 753-758
    • Kormelink Searije-Van Leeuwen, M.1    Wood, T.M.2    Voragen, A.3
  • 110
    • 0027365675 scopus 로고
    • Catabolite repression of ß-glucanasc synthesis in bacillus subtilis
    • Krüger, S., Stulke, J. and Hecker, M. (1993). Catabolite repression of ß-glucanasc synthesis in Bacillus subtilis. Journal of General Microbiology 139, 2047-2054.
    • (1993) Journal of General Microbiology , vol.139 , pp. 2047-2054
    • Krüger, S.1    Stulke, J.2    Hecker, M.3
  • 112
    • 0027214236 scopus 로고
    • Triggering of cellulase biosynthesis by cellulose in trichodenna reesei. Involvement of a constitutive, sophorose-inducible. Glucose-inhibitedß-diglucosidc permease
    • Kubicek, C. P., Messner, R., Gruber, F., Mander, M. and Kubiœk-Pranz, E. M. (1993b). Triggering of cellulase biosynthesis by cellulose in Trichodenna reesei. Involvement of a constitutive, sophorose-inducible. glucose-inhibitedß-diglucosidc permease. Journal of Biological Chemistry 268, 19364-19368.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 19364-19368
    • Kubicek, C.P.1    Messner, R.2    Gruber, F.3    Mander, M.4    Kubiœk-Pranz, E.M.5
  • 113
    • 0027481684 scopus 로고
    • Specific binding sites in ihealcr and«/cvt promoters of the ethanol regulon for the crea repressor mediating carbon catabolite repression in aspergillus nidulans
    • Kulmburg, P., Mathieu, M., Dowzer, C., Kelly, J. and Felenbok, B. (1993). Specific binding sites in ihealcR and«/cvt promoters of the ethanol regulon for the CREA repressor mediating carbon catabolite repression in Aspergillus nidulans. Molecular Microbiology 7, 847-857.
    • (1993) Molecular Microbiology , vol.7 , pp. 847-857
    • Kulmburg, P.1    Mathieu, M.2    Dowzer, C.3    Kelly, J.4    Felenbok, B.5
  • 114
    • 0001855475 scopus 로고
    • The cellulosome concept: Exocelluiar/extraccllular enzyme reactor centers for efficient binding and cellulolysis
    • (J. P. Aubert, P, Beguin and J. Millet, Eds),, Academic Press. London
    • Lamed, R. and Bayer, E. A. (1987). The cellulosome concept: exocelluiar/extraccllular enzyme reactor centers for efficient binding and cellulolysis. In Biochemistry and genetics of cellulose degradation. (J. P. Aubert, P, Beguin and J. Millet, Eds), pp. 101-116. Academic Press. London.
    • (1987) Biochemistry and Genetics of Cellulose Degradation , pp. 101-116
    • Lamed, R.1    Bayer, E.A.2
  • 115
    • 0027274760 scopus 로고
    • Characterization of the active site and thermostability regions of endo-xylanase from thermoanaembacterium saccharolyticum b6a-ri
    • Lee, Y. E., Lowe, S. E., Henrissat, B. and Zeikus, J. G. (1993). Characterization of the active site and thermostability regions of endo-xylanase from Thermoanaembacterium saccharolyticum B6A-RI. Journal of Bacteriology 175, 5890-5898.
    • (1993) Journal of Bacteriology , vol.175 , pp. 5890-5898
    • Lee, Y.E.1    Lowe, S.E.2    Henrissat, B.3    Zeikus, J.G.4
  • 116
    • 0028330705 scopus 로고
    • Regulation of xyianolytic enzymes in bacillus subtilis
    • Lindner, C., Stulke, J. and Hecker, M. (1994). Regulation of xyianolytic enzymes in Bacillus subtilis. Microbiology 140, 753-757.
    • (1994) Microbiology , vol.140 , pp. 753-757
    • Lindner, C.1    Stulke, J.2    Hecker, M.3
  • 117
    • 0002448290 scopus 로고
    • New developments in the application of enzymes for biomass processing
    • (M. P. Coughan, Eds), Elsevier Applied Science. New York
    • Linko, M., Poutanen, K. and Viikari, L. (1989). New developments in the application of enzymes for biomass processing. In Enzyme Systems for Lignocellulose Degradation (M. P. Coughan, Eds), pp. 331-346. Elsevier Applied Science. New York.
    • (1989) Enzyme Systems for Lignocellulose Degradation , pp. 331-346
    • Linko, M.1    Poutanen, K.2    Viikari, L.3
  • 118
    • 0023223030 scopus 로고
    • Cellulases and xylanases of an anaerobic fungus grown on wheat-straw iignoceltulose. Wheat-straw holocellulose and xylan
    • Lowe, S. E., Theodorou, M. K. and Trinci, A. P. J. (1987). Cellulases and xylanases of an anaerobic fungus grown on wheat-straw iignoceltulose. wheat-straw holocellulose and xylan. Applied and Environmental Microbiology 53, 1216-1223.
    • (1987) Applied and Environmental Microbiology , vol.53 , pp. 1216-1223
    • Lowe, S.E.1    Theodorou, M.K.2    Trinci, A.3
  • 119
    • 0025237055 scopus 로고
    • Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile caldocellum saccharolyticum
    • Luthi, E., Love, D. R., Mcanulty, J. T., Wallace, C., Caughey, P. A., Saul, D. and Bergquist, P. L. (1990). Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile Caldocellum saccharolyticum. Applied and Environmental Microbiology 56, 1017-1024.
    • (1990) Applied and Environmental Microbiology , vol.56 , pp. 1017-1024
    • Luthi, E.1    Love, D.R.2    McAnulty, J.T.3    Wallace, C.4    Caughey, P.A.5    Saul, D.6    Bergquist, P.L.7
  • 120
    • 0024388545 scopus 로고
    • Identification of three distinct clostridium thermocellum xylanase genes by molecular cloning
    • Mackenzie, C. R., Yang, R. C., Patel, G. B., Bilous, D. and Narang, S. A. (1989). Identification of three distinct Clostridium thermocellum xylanase genes by molecular cloning. Archives of Microbiology 152, 377-381.
    • (1989) Archives of Microbiology , vol.152 , pp. 377-381
    • Mackenzie, C.R.1    Yang, R.C.2    Patel, G.B.3    Bilous, D.4    Narang, S.A.5
  • 122
    • 0028303157 scopus 로고
    • The acid/base catalyst in the exoglucanase/xylanase from cellulonwnas fimi is glutamic acid 127: Evidence from detailed kinetic studies of mutants
    • Macleod, A. M., Lindhorst, T., Withers, S. G. and Warren, R. A. J. (1994). The acid/base catalyst in the exoglucanase/xylanase from Cellulonwnas fimi is glutamic acid 127: evidence from detailed kinetic studies of mutants. Biochemistry 33, 6371-6376.
    • (1994) Biochemistry , vol.33 , pp. 6371-6376
    • Macleod, A.M.1    Lindhorst, T.2    Withers, S.G.3    Warren, R.4
  • 125
    • 85032069287 scopus 로고
    • Infection structures of fungai plant pathogens-a cytological and physiological evaluation
    • Mendgen, K. and Deising, H. (1993). Infection structures of fungai plant pathogens-a cytological and physiological evaluation. New Phytology 124, 193-213.
    • (1993) New Phytology , vol.124 , pp. 193-213
    • Mendgen, K.1    Deising, H.2
  • 126
    • 14744299296 scopus 로고
    • Thermal stabilization of xylose isomerase from thermoanaerobacterium thermosulutigenes
    • Meng, M., Bagdasarian, M. and Zeikus, J. G. (1993). Thermal stabilization of xylose isomerase from Thermoanaerobacterium thermosulutigenes. Bio/Technologv 11, 1157-1161.
    • (1993) Bio/Technologv , vol.11 , pp. 1157-1161
    • Meng, M.1    Bagdasarian, M.2    Zeikus, J.G.3
  • 127
    • 0028244925 scopus 로고
    • Identification of glutamic acid 78 as the active-site nucleophile in bacillus subtilis xylanase using electrospray tandem mass spectrometry
    • Miao, S. C., Ziser, L., Aebersold, R. and Withers, S. G. (1994). Identification of glutamic acid 78 as the active-site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry. Biochemistry 33, 7027-7032.
    • (1994) Biochemistry , vol.33 , pp. 7027-7032
    • Miao, S.C.1    Ziser, L.2    Aebersold, R.3    Withers, S.G.4
  • 128
    • 0027571711 scopus 로고
    • Characterization of xylanase production by a local isolate of pénicillium janthinellum
    • Milagres, A. M. F., Lacis, L. S. and Prade, R. A. (1993). Characterization of xylanase production by a local isolate of Pénicillium janthinellum. Enzyme and Microbial Technology 15, 248-253.
    • (1993) Enzyme and Microbial Technology , vol.15 , pp. 248-253
    • Milagres, A.1    Lacis, L.S.2    Prade, R.A.3
  • 129
    • 0028470886 scopus 로고
    • Production of xylanases from pénicillium janthinellum and its use in the recovery of cellulosic textile fibers
    • Milagres, A. M. F. and Prade, R. A. (1994). Production of xylanases from Pénicillium janthinellum and its use in the recovery of cellulosic textile fibers. Enzyme and Microbial Technology 16, 627-632.
    • (1994) Enzyme and Microbial Technology , vol.16 , pp. 627-632
    • Milagres, A.1    Prade, R.A.2
  • 130
    • 0028214219 scopus 로고
    • Evidence for a general role for high-affmity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases
    • Millward-Sadler, S. J., Poole, D. M., Henrissat, B., Hazlewood, G. P., Clarke, J. H. and Gilbert, H. J. (1994). Evidence for a general role for high-affmity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases. Molecular Microbiology 11, 375-382.
    • (1994) Molecular Microbiology , vol.11 , pp. 375-382
    • Millward-Sadler, S.J.1    Poole, D.M.2    Henrissat, B.3    Hazlewood, G.P.4    Clarke, J.H.5    Gilbert, H.J.6
  • 132
    • 0022885127 scopus 로고
    • Cloning the xylanase gene of streptomyces lividons
    • Mondou, F., Shareck, F., Morosoli, R. and Kluepfel, D. (1986). Cloning the xylanase gene of Streptomyces lividons. Gene 49, 323-329.
    • (1986) Gene , vol.49 , pp. 323-329
    • Mondou, F.1    Shareck, F.2    Morosoli, R.3    Kluepfel, D.4
  • 133
    • 0025030207 scopus 로고
    • Relationship of cellulosonial and non-cellulosomul xylanases of clostridium thermocellum to cellulose-degrading enzymes
    • Morag, E., Bayer, É. A. and Lamed, R. (1990). Relationship of cellulosonial and non-cellulosomul xylanases of Clostridium thermocellum to cellulose-degrading enzymes. Journal of Bacteriology 172, 6098-6105.
    • (1990) Journal of Bacteriology , vol.172 , pp. 6098-6105
    • Morag, E.1    Bayer2    Lamed, R.3
  • 134
    • 0027968572 scopus 로고
    • Identification of two acidic residues involved in the catalysis of xylanase a from streptomyces lividans
    • Moreau, A., Roberge, M., Manin, C., Shareck, F., Kluepfel, D. and Morosoli, R. (1994a). Identification of two acidic residues involved in the catalysis of xylanase A from Streptomyces lividans. Biochemical Journal 302, 291-295.
    • (1994) Biochemical Journal , vol.302 , pp. 291-295
    • Moreau, A.1    Roberge, M.2    Manin, C.3    Shareck, F.4    Kluepfel, D.5    Morosoli, R.6
  • 135
    • 0028115935 scopus 로고
    • Alteration of the cleavage mode and of the iransglycosyiation reactions of the xylanase a of streptomyces lividans 1326 by site-directed mutagenesis of the asnl73 residue
    • Moreau, A., Shareck, F., Kluepfel, D. and Morosoli, R. (1994b). Alteration of the cleavage mode and of the iransglycosyiation reactions of the xylanase A of Streptomyces lividans 1326 by site-directed mutagenesis of the Asnl73 residue. European Journal of Biochemistry 219, 261-266.
    • (1994) European Journal of Biochemistry , vol.219 , pp. 261-266
    • Moreau, A.1    Shareck, F.2    Kluepfel, D.3    Morosoli, R.4
  • 136
    • 0022446556 scopus 로고
    • Isolation and partial primary sequence of a xylanase from the yeast crvptococcus albidus
    • Morosoli, R., Roy, C. and Yagushi, M. (1986). Isolation and partial primary sequence of a xylanase from the yeast Crvptococcus albidus. Biochimica et Biophvsica Acta 870, 473-478.
    • (1986) Biochimica Et Biophvsica Acta , vol.870 , pp. 473-478
    • Morosoli, R.1    Roy, C.2    Yagushi, M.3
  • 137
    • 0024653081 scopus 로고
    • Production of xyianase by the ruminai anaerobic funvusneociiltiinastixfrontalis
    • Mountfört, D. O. and Asher, R. A. (1989). Production of xyianase by the ruminai anaerobic funvusNeociiltiinastixfrontalis. Applied and Environmental Microbiology 55, 1016-1022.
    • (1989) Applied and Environmental Microbiology , vol.55 , pp. 1016-1022
    • Mountfört, D.O.1    Asher, R.A.2
  • 139
    • 0002533314 scopus 로고
    • Control of plant cell wall biogenesis: An overview
    • (N. G. Paice and M. G. Lewis, eds.)
    • Northcote, D. H. (1989). Control of plant cell wall biogenesis: an overview. In ACS Symp. Series. (N. G. Paice and M. G. Lewis, eds.). vol. 399, pp. 1-5.
    • (1989) ACS Symp. Series , vol.399 , pp. 1-5
    • Northcote, D.H.1
  • 140
    • 0025099098 scopus 로고
    • Effects of environmental conditions on xylose fermentation by recombinant escherichia coli
    • Ohta, K., Alterthum, F. and Ingram, L. O. (1990). Effects of environmental conditions on xylose fermentation by recombinant Escherichia coli. Applied and Environmental Microbiology 56, 463-465.
    • (1990) Applied and Environmental Microbiology , vol.56 , pp. 463-465
    • Ohta, K.1    Alterthum, F.2    Ingram, L.O.3
  • 141
    • 0025825737 scopus 로고
    • Genetic improvement of escherichia coli for ethanol production: Chromosomal integration of zymomonas ntobilis genes encoding pyruvate decarboxylase and alcohol dehydrogenase ii
    • Ohta, K., Beall, D. S., Mejia, J. P., Shanmugam, K. T, and Ingram, L. O. (1991a). Genetic improvement of Escherichia coli for ethanol production: chromosomal integration of Zymomonas ntobilis genes encoding pyruvate decarboxylase and alcohol dehydrogenase II, Applied and Environmental Microbiology 57, 893-900.
    • (1991) Applied and Environmental Microbiology , vol.57 , pp. 893-900
    • Ohta, K.1    Beall, D.S.2    Mejia, J.P.3    Shanmugam, K.T.4    Ingram, L.O.5
  • 143
    • 0011750654 scopus 로고
    • Tertiary structure of xylanase and estimation of active sites by site directed mutagenesis
    • Okada, H. (1989). Tertiary structure of xylanase and estimation of active sites by site directed mutagenesis. Advances in Protein Design 12, 81-86.
    • (1989) Advances in Protein Design , vol.12 , pp. 81-86
    • Okada, H.1
  • 145
    • 84930939574 scopus 로고
    • Ligııin-carbohydrate complexes from poplar wood. Isolation and enzymatic degradation
    • G. F. Leatham and M. E. Himmel, eds.), American Chemical Society, Boston
    • Overend, R. P. and Johnson, K. G. (1991). Ligııin-carbohydrate complexes from poplar wood. Isolation and enzymatic degradation. In Enzymes for fuels and chemicalfeedstocks. (G. F. Leatham and M. E. Himmel, eds.). vol. 460, pp. 270-287. American Chemical Society, Boston.
    • (1991) Enzymes for Fuels and Chemicalfeedstocks , vol.460 , pp. 270-287
    • Overend, R.P.1    Johnson, K.G.2
  • 146
    • 0021449279 scopus 로고
    • Removing hemicellulose from pulps by specific enzyme hydrolysis
    • Paice, M. G. and Jurasek, L. (1984). Removing hemicellulose from pulps by specific enzyme hydrolysis. Journal of Wood Chemistry Technology 4, 187-198.
    • (1984) Journal of Wood Chemistry Technology , vol.4 , pp. 187-198
    • Paice, M.G.1    Jurasek, L.2
  • 147
    • 0021686807 scopus 로고
    • Two forms of endoglucanase from the basidiomycete schizophyllum commune and their relationship to other ß-1.4-glucoside hydrolases
    • Paice, M. G., Desrochers, M., Rho, D., Jurasek, L., Roy, C., Rollin, C. F., Demiguel, E. and Yagushi, M. (1984). TWO FORMS OF ENDOGLUCANASE FROM THE BASIDIOMYCETE Schizophyllum commune and their relationship to other ß-1.4-glucoside hydrolases. Bio/ Technology 2, 535-539.
    • (1984) Bio/ Technology , vol.2 , pp. 535-539
    • Paice, M.G.1    Desrochers, M.2    Rho, D.3    Jurasek, L.4    Roy, C.5    Rollin, C.F.6    Demiguel, E.7    Yagushi, M.8
  • 149
    • 0025953505 scopus 로고
    • Characterization of hybrid proteins consisting of the catalytic domains of clostridium and ruminococctts endoglucanases, fused to pseudomonas non-catalytic cellulose-binding domains
    • Poole, D. M., Durrant, A. J., Hazlewood, G. P. and Gilbert, H. J. (1991). Characterization of hybrid proteins consisting of the catalytic domains of Clostridium and Ruminococctts endoglucanases, fused to Pseudomonas non-catalytic cellulose-binding domains. Biochemical Journal 279, 787-792.
    • (1991) Biochemical Journal , vol.279 , pp. 787-792
    • Poole, D.M.1    Durrant, A.J.2    Hazlewood, G.P.3    Gilbert, H.J.4
  • 150
    • 0027386771 scopus 로고
    • The role of conserved tryptophan residues in the interaction of a bacterial cellulose binding domain with its ligand
    • Poole, D. M., Hazlewood, G. P., Huskisson, N. S., Vjrdem, R. and Glibert, H. J. (1993). The role of conserved tryptophan residues in the interaction of a bacterial cellulose binding domain with its ligand. FEMS Microbiology Letters 80, 77-83.
    • (1993) FEMS Microbiology Letters , vol.80 , pp. 77-83
    • Poole, D.M.1    Hazlewood, G.P.2    Huskisson, N.S.3    Vjrdem, R.4    Glibert, H.J.5
  • 153
    • 0028533528 scopus 로고
    • Process parameters and environmental factors affecting d-xylose fermentation by yeasts
    • Preez, J. C. (1994). Process parameters and environmental factors affecting D-xylose fermentation by yeasts. Enzyme Microbial Technology 16, 944-956.
    • (1994) Enzyme Microbial Technology , vol.16 , pp. 944-956
    • Preez, J.C.1
  • 155
    • 0003053318 scopus 로고
    • Comparison of steam pretreatment of eucalyptus, aspen and spruce wood chips and their enzymatic hydrolysis
    • Ramos, L. P., Breuil, C. and Saddler, J. N. (1992). Comparison of steam pretreatment of Eucalyptus, Aspen and Spruce wood chips and their enzymatic hydrolysis. Applied Biochemistry and Biotechnology 34, 37-48.
    • (1992) Applied Biochemistry and Biotechnology , vol.34 , pp. 37-48
    • Ramos, L.P.1    Breuil, C.2    Saddler, J.N.3
  • 156
    • 0014939925 scopus 로고
    • The action pattern of porcine pancreatic alfa-aniylase in relationship to the substrate binding site of the enzyme
    • Robyt, J. F. and French, D. (1970). The action pattern of porcine pancreatic alfa-aniylase in relationship to the substrate binding site of the enzyme. Journal of Biological Chemistry 245, 3917-3927.
    • (1970) Journal of Biological Chemistry , vol.245 , pp. 3917-3927
    • Robyt, J.F.1    French, D.2
  • 157
    • 0026986905 scopus 로고
    • Biotechnology for the conversion of lignoceliulosics
    • Saddler, J. N. (1992). Biotechnology for the conversion of lignoceliulosics. Biomass and Bioenergy 2, 229-238.
    • (1992) Biomass and Bioenergy , vol.2 , pp. 229-238
    • Saddler, J.N.1
  • 158
    • 0002484034 scopus 로고
    • Steam pretreatment of lignocellulosic residues
    • (J. N. Saddler, Eds), CAB International, Wallingford, UK
    • Saddler, J. N., Ramos, L. P. and Breuil, C. (1993). Steam pretreatment of lignocellulosic residues. In Bioconversion of forest and agricultural plant residues. (J. N. Saddler, Eds), vol. 9. pp. 73-91. CAB International, Wallingford, UK.
    • (1993) Bioconversion of Forest and Agricultural Plant Residues , vol.9 , pp. 73-91
    • Saddler, J.N.1    Ramos, L.P.2    Breuil, C.3
  • 159
    • 0027548085 scopus 로고
    • Nucleotide sequence of the clostridium stercorarium xyna gene encoding xyianase a: Identification of catalytic and cellulose binding domains
    • Sakka, K., Kojima, Y., Kondo, T., Karita, S., Ohmya, K. and Shimada, K. (1993). Nucleotide sequence of the Clostridium stercorarium xynA gene encoding xyianase A: Identification of catalytic and cellulose binding domains. Biochemistry 57, 273-277.
    • (1993) Biochemistry , vol.57 , pp. 273-277
    • Sakka, K.1    Kojima, Y.2    Kondo, T.3    Karita, S.4    Ohmya, K.5    Shimada, K.6
  • 160
    • 0001978215 scopus 로고
    • A technical and economic analysis of acid-catalyzed steam explosion and dilute sulfuric acid pretreatments using wheat straw or aspen wood chips
    • Schell, D. J., Torget, R., Power, A., Walter, P. J., Grohmann, K. and Hinnman, N. D. (1991). A technical and economic analysis of acid-catalyzed steam explosion and dilute sulfuric acid pretreatments using wheat straw or aspen wood chips. Applied Biochemistry and Biotechnology 28/29, 87-97.
    • (1991) Applied Biochemistry and Biotechnology , vol.28 , Issue.29 , pp. 87-97
    • Schell, D.J.1    Torget, R.2    Power, A.3    Walter, P.J.4    Grohmann, K.5    Hinnman, N.D.6
  • 161
    • 0024306141 scopus 로고
    • Conversion of pentoses to ethanol by yeasts and fungi
    • Schneider, H. (1989). Conversion of pentoses to ethanol by yeasts and fungi. Critical Reviews of Biotechnology 9, 1-40.
    • (1989) Critical Reviews of Biotechnology , vol.9 , pp. 1-40
    • Schneider, H.1
  • 162
    • 0025576522 scopus 로고
    • Endo-polygalacturonase is not required for pathogenicity of cochliobolus carbonum on maize
    • Scott-Craig, J. S., Panaccione, D. G., Cervone, F. and Walton, J. D. (1990). Endo-polygalacturonase is not required for pathogenicity of Cochliobolus carbonum on maize. Plant Cell 2, 1191-1200.
    • (1990) Plant Cell , vol.2 , pp. 1191-1200
    • Scott-Craig, J.S.1    Panaccione, D.G.2    Cervone, F.3    Walton, J.D.4
  • 163
    • 0022307516 scopus 로고
    • Developments in the chemistry and biochemistry of pectic and hemicellulosic polymers
    • Selvendran, R. R. (1985). Developments in the chemistry and biochemistry of pectic and hemicellulosic polymers. Journal of Cell Science, Supplement 2, 51-88.
    • (1985) Journal of Cell Science, Supplement , vol.2 , pp. 51-88
    • Selvendran, R.R.1
  • 164
    • 0026915020 scopus 로고
    • Use of xyianase to decrease the formation of aox in kraft pulp bleaching
    • Senior, D. J. and Hamilton, J. (1992). Use of xyianase to decrease the formation of AOX in kraft pulp bleaching. Journal of Pulp Paper Science 18, 165-169.
    • (1992) Journal of Pulp Paper Science , vol.18 , pp. 165-169
    • Senior, D.J.1    Hamilton, J.2
  • 165
    • 0000362530 scopus 로고
    • Reduction in chlorine use during bleaching of kraft pulp following xylanase treatment
    • Senior, D. J., Hamilton, J., Bernier, R L. and Dumanoir, J. R. (1992). Reduction in chlorine use during bleaching of kraft pulp following xylanase treatment. Tappi Journal 11, 125-130.
    • (1992) Tappi Journal , vol.11 , pp. 125-130
    • Senior, D.J.1    Hamilton, J.2    Bernier, R.L.3    Dumanoir, J.R.4
  • 166
    • 0026045488 scopus 로고
    • Sequences of three genes specifying xylanases in streptomyces lividans
    • Shareck, F., Roy, C., Yagucui, M., Morosoli, R. and 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    Yagucui, M.3    Morosoli, R.4    Kluepfel, D.5
  • 168
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • Sinnott, M. L. (1990). Catalytic mechanisms of enzymic glycosyl transfer. Chemical Reviews 90, 1171-1202.
    • (1990) Chemical Reviews , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 169
    • 0001917552 scopus 로고
    • Occurrence and nature of ferulic acid substitution at cell wall polysaccharides in graminaceous plants
    • Smith, M. M. and Hartley, R. D. (1983). Occurrence and nature of ferulic acid substitution at cell wall polysaccharides in graminaceous plants. Carbohydrate Research 118, 65-80.
    • (1983) Carbohydrate Research , vol.118 , pp. 65-80
    • Smith, M.M.1    Hartley, R.D.2
  • 170
    • 0026871097 scopus 로고
    • Cutinase is not required for fungal pathogenicity on pea
    • Stahl, D. J. and Schafer, W. (1992). Cutinase is not required for fungal pathogenicity on pea. Plant Cell 4, 621-629.
    • (1992) Plant Cell , vol.4 , pp. 621-629
    • Stahl, D.J.1    Schafer, W.2
  • 171
    • 0024278446 scopus 로고
    • A binding site-deficient catalyti-cally active core protein of endoglucanase 111 from the culture filtrate of trichoderma reesei
    • Stahlberg, J., Johansson, G. and Pettersson, G. (1988). A binding site-deficient catalyti-cally active core protein of endoglucanase 111 from the culture filtrate of Trichoderma reesei. European Journal of Biochemistry 173, 179-183.
    • (1988) European Journal of Biochemistry , vol.173 , pp. 179-183
    • Stahlberg, J.1    Johansson, G.2    Pettersson, G.3
  • 172
    • 0023645371 scopus 로고
    • Studies on a wild type strain ohschizophyllum commune. Celiulase and xylanase production and formation of the extracellular polysacchari de schizophillan
    • Steiner, W., Laitcrty, R. M., Gomes, I. and Esterbauer, H. (1987). Studies on a wild type strain oHSchizophyllum commune. Celiulase and xylanase production and formation of the extracellular polysacchari de schizophillan. Biotechnology and Bioengineering 30, 169-178.
    • (1987) Biotechnology and Bioengineering , vol.30 , pp. 169-178
    • Steiner, W.1    Laitcrty, R.M.2    Gomes, I.3    Esterbauer, H.4
  • 173
    • 0018736190 scopus 로고
    • Induction of ceilulolytic enzymes intrichoderma reesei by sophorose
    • Sternberg, D. and Mandels, G. R. (1979). Induction of ceilulolytic enzymes inTrichoderma reesei by sophorose. Journal of Bacteriology 139, 761-769.
    • (1979) Journal of Bacteriology , vol.139 , pp. 761-769
    • Sternberg, D.1    Mandels, G.R.2
  • 175
    • 0027299062 scopus 로고
    • Mutational analysis of glycosila. Se function
    • Svensson, B. and Sogaard, M. (1993). Mutational analysis of glycosila. se function. Journal of Biotechnology 29, 1-37.
    • (1993) Journal of Biotechnology , vol.29 , pp. 1-37
    • Svensson, B.1    Sogaard, M.2
  • 176
    • 0028124152 scopus 로고
    • Ethanol production from pentose and hexoses by recombinantfec/ienwi/ii coli
    • Takahashi, D. F., Carvalho, M. L. and Alterthum, F. (1994). Ethanol production from pentose and hexoses by recombinantfec/ienWi/ii coli. Biotechnology Letters 16, 747-750.
    • (1994) Biotechnology Letters , vol.16 , pp. 747-750
    • Takahashi, D.F.1    Carvalho, M.L.2    Alterthum, F.3
  • 178
    • 0027478431 scopus 로고
    • Anaerobic fungi and their ceilulolytic and xyianolytic enzymes
    • Teuníssen, M. J. and Op-Den Camp, H. J. (1993). Anaerobic fungi and their ceilulolytic and xyianolytic enzymes. Antonie Van Leeuwenhoek 63, 63-76.
    • (1993) Antonie Van Leeuwenhoek , vol.63 , pp. 63-76
    • Teuníssen, M.J.1    Op-Den Camp, H.J.2
  • 179
    • 34250512499 scopus 로고
    • Recent progress in the chemistry' of wood hemicelluloses
    • Tlmel, T. E. (1967). Recent progress in the chemistry' of wood hemicelluloses. Wood Science Technology 1, 45-70.
    • (1967) Wood Science Technology , vol.1 , pp. 45-70
    • Tlmel, T.E.1
  • 180
    • 0002347167 scopus 로고
    • The use of enzymes to decrease the cl2 requirements in pulp bleaching
    • Tolan, J. S. and Canovas, R. V. (1992). The use of enzymes to decrease the CL2 requirements in pulp bleaching. Pulp and Paper Canada 93, 39-40.
    • (1992) Pulp and Paper Canada , vol.93 , pp. 39-40
    • Tolan, J.S.1    Canovas, R.V.2
  • 181
    • 0028181024 scopus 로고
    • An internal cellulose-binding domain mediates adsorption of an engineered bifunctionai xyianase celiulase
    • Tomme, P., Gilkes, N. R., Miller R. C., Warren, A. J. and Kilburn, D. G. (1994). An internal cellulose-binding domain mediates adsorption of an engineered bifunctionai xyianase celiulase. Protein Engineering 7, 117-123.
    • (1994) Protein Engineering , vol.7 , pp. 117-123
    • Tomme, P.1    Gilkes, N.R.2    Miller, R.C.3    Warren, A.J.4    Kilburn, D.G.5
  • 182
    • 0028911057 scopus 로고
    • Structural comparison of two major endo-1, 4-xyianases from trichoderma reesei
    • Törrönen, A. and Rouvinen, J. (1995). Structural comparison of two major endo-1, 4-xyianases from Trichoderma reesei. Biochemistry 34, 847-856.
    • (1995) Biochemistry , vol.34 , pp. 847-856
    • Törrönen, A.1    Rouvinen, J.2
  • 183
    • 0028338985 scopus 로고
    • Three dimensional structure of endo-1, 4-ß-xylanase ii from trichoderma reesei: Two conformational stales in the active site
    • Törrönen, A., Harkki, A. and Rouvinen, J. (1994). THREE DIMENSIONAL STRUCTURE OF ENDO-1, 4-ß-xylanase II from Trichoderma reesei: two conformational stales in the active site. EMBO Journal 13, 2493-2501.
    • (1994) EMBO Journal , vol.13 , pp. 2493-2501
    • Törrönen, A.1    Harkki, A.2    Rouvinen, J.3
  • 184
    • 0027406938 scopus 로고
    • Amino acid sequence similarities between low molecular weight endo-1, 4-ß-xylanases and family h celiulases revealed by clustering analysis
    • Törrönen, A., Kubicek, C. P. and Henrissat, B. (1993a). Amino acid sequence similarities between low molecular weight endo-1, 4-ß-xylanases and family H celiulases revealed by clustering analysis. FEBS Letters 321, 135-139.
    • (1993) FEBS Letters , vol.321 , pp. 135-139
    • Törrönen, A.1    Kubicek, C.P.2    Henrissat, B.3
  • 185
    • 0027519339 scopus 로고
    • Crystallization and preliminary x-ray analysis of two major xylanases from trichoderma reesei
    • Törrönen, A., Rouvinen, J., Ahlgren, M., Harkki, A. and Visuri, K. (1993b). Crystallization and preliminary X-ray analysis of two major xylanases from Trichoderma reesei. Journal of Molecular Biology 233, 313-316.
    • (1993) Journal of Molecular Biology , vol.233 , pp. 313-316
    • Törrönen, A.1    Rouvinen, J.2    Ahlgren, M.3    Harkki, A.4    Visuri, K.5
  • 186
  • 187
    • 0026055093 scopus 로고
    • Glutamic acid 274 is the nucleophile in the active site of a ‘retaining’ exo-giucanase from cellulomonas fimi
    • Tull, D., Withers, S. G., Gilkes, N. R., Kilburn, D. G., Warren, R. A. J. and Aebersold, R. (1991). Glutamic acid 274 is the nucleophile in the active site of a ‘retaining’ exo-giucanase from Cellulomonas fimi. Journal of Biological Chemistry 266, 15621-15625.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 15621-15625
    • Tull, D.1    Withers, S.G.2    Gilkes, N.R.3    Kilburn, D.G.4    Warren, R.5    Aebersold, R.6
  • 188
    • 0000744115 scopus 로고
    • Xylanase enzymes promote pulp bleaching
    • Viikarl L., Sundquíst, J. and Kettunen, J. (1991). Xylanase enzymes promote pulp bleaching. Paper Timber 73, 384-389.
    • (1991) Paper Timber , vol.73 , pp. 384-389
    • Viikarl, L.1    Sundquíst, J.2    Kettunen, J.3
  • 189
    • 0000477362 scopus 로고
    • Characterization of pulps treated with hemicellulolytic enzymes prior to bleaching
    • (K. T. Kirk and H. -M. Chang. Eds),, Butterworth-Heinemann. Boston
    • Viikari, L., Kantelinen, A., Poutanen, K. and Ranua, M. (1990). Characterization of pulps treated with hemicellulolytic enzymes prior to bleaching. In Biotechnology in Pulp and Paper Manufacture (K. T. Kirk and H. -M. Chang. Eds), pp. 145-151. Butterworth-Heinemann. Boston.
    • (1990) Biotechnology in Pulp and Paper Manufacture , pp. 145-151
    • Viikari, L.1    Kantelinen, A.2    Poutanen, K.3    Ranua, M.4
  • 191
    • 0025704906 scopus 로고
    • Hydrolysis of (I-3)-and (1-2)-d-xyiosidic linkages by an endo-(1-4)-ß-d-xylanase afcryptococcusalhidus
    • Vrsanská, M., Hirsch, J., Kovác, P. and Biely, P. (1990). Hydrolysis of (I-3)-and (1-2)-D-xyiosidic linkages by an endo-(1-4)-ß-D-xylanase afCryptococcusalhidus. Carbohydrate Research 206, 251-256.
    • (1990) Carbohydrate Research , vol.206 , pp. 251-256
    • Vrsanská, M.1    Hirsch, J.2    Kovác, P.3    Biely, P.4
  • 192
    • 0028211360 scopus 로고
    • Mutational and crystallographic analyses of the active-site residues of the bacillus circulons xylanase
    • Wakarchuk, W. W., Campbell, R. L., Sung, W. L., Davoodi, J. and Yaguchi, M. (1994a). Mutational and crystallographic analyses of the active-site residues of the Bacillus circulons xylanase. Protein Science 3, 467-475.
    • (1994) Protein Science , vol.3 , pp. 467-475
    • Wakarchuk, W.W.1    Campbell, R.L.2    Sung, W.L.3    Davoodi, J.4    Yaguchi, M.5
  • 194
    • 0026619921 scopus 로고
    • Rumen microbiology, biotechnology and ruminant nutrition: The application of research to a complcx microbial ecosystem
    • Wallace, R. J. (1992). Rumen microbiology, biotechnology and ruminant nutrition: The application of research to a complcx microbial ecosystem. FEMS Microbiology Letters 100, 529-534.
    • (1992) FEMS Microbiology Letters , vol.100 , pp. 529-534
    • Wallace, R.J.1
  • 195
    • 0025273798 scopus 로고
    • The genes for three xylan-degrading activities from bac. Teroides ovatus are clustered in a 3.8-kilobase region
    • Whitehead, T. R. and Hespell, R. B. (1990). The genes for three xylan-degrading activities from Bac. teroides ovatus are clustered in a 3.8-kilobase region. Journal of Bacteriology 172, 2408-2412.
    • (1990) Journal of Bacteriology , vol.172 , pp. 2408-2412
    • Whitehead, T.R.1    Hespell, R.B.2
  • 196
    • 0025968678 scopus 로고
    • Introduction of the bacteroides nmiinicola xylanase gene into\ht bacteroides thetaiotaomicron chromosome for production of xylanase activity
    • Whitehead, T. R., Cotta, M. A. and Hespell, R. B. (1991). Introduction of the Bacteroides nmiinicola xylanase gene into\ht Bacteroides thetaiotaomicron chromosome for production of xylanase activity. Applied and Environmental Microbiology 57, 277-282.
    • (1991) Applied and Environmental Microbiology , vol.57 , pp. 277-282
    • Whitehead, T.R.1    Cotta, M.A.2    Hespell, R.B.3
  • 198
    • 0024087074 scopus 로고
    • Multiplicity of (3-1-4-xylanase in microorganism: Functions and applications
    • Wong, K. K. Y., Tan, L. U. L. and Saddler, J. N. (1988). Multiplicity of 3-1-4-xylanase in microorganism: Functions and applications. Microbiological Reviews 52, 305-317.
    • (1988) Microbiological Reviews , vol.52 , pp. 305-317
    • Wong, K.1    Tan, L.2    Saddler, J.N.3
  • 199
    • 0001747522 scopus 로고
    • Two components of an extracellular protein aggregate of clostridium thermocellum together degrade crystalline cellulose
    • Wu, J. H. D., Orme-Johnson, W. H. and Demain, A. L. (1988). Two components of an extracellular protein aggregate of Clostridium thermocellum together degrade crystalline cellulose. Biochemistry 27, 1703-1709.
    • (1988) Biochemistry , vol.27 , pp. 1703-1709
    • Wu, J.1    Orme-Johnson, W.H.2    Demain, A.L.3
  • 200
    • 0027235452 scopus 로고
    • Biology, fiber-degradation, and enzymology of anaerobic zoosporic fungi
    • Wubah, D. A., Akin, D. É. and Borneman, W. S. (1993). Biology, fiber-degradation, and enzymology of anaerobic zoosporic fungi. Critical Reviews of Microbiology 19, 99-115.
    • (1993) Critical Reviews of Microbiology , vol.19 , pp. 99-115
    • Wubah, D.A.1    Akin, D.2    Borneman, W.S.3
  • 201
    • 0026496063 scopus 로고
    • A novel polysaccharidc hydrolase cdna (Ceid) from neocallimastix patriciarum encoding three multi-functional catalytic domains with high endoglucanase, cellobiohydrolase and xylanase activities
    • Xue, G. P., Gobius, K. S. and Orpin, C. G. (1992). A novel polysaccharidc hydrolase cDNA (ceID) from Neocallimastix patriciarum encoding three multi-functional catalytic domains with high endoglucanase, cellobiohydrolase and xylanase activities. Journal of General Microbiology 138, 2397-2403.
    • (1992) Journal of General Microbiology , vol.138 , pp. 2397-2403
    • Xue, G.P.1    Gobius, K.S.2    Orpin, C.G.3
  • 203
    • 84947533596 scopus 로고
    • Use of hemicellulolytic enzymes as one stage in bleaching of kraft pulps
    • Yang, J. L. and Eriksson, K. E. L. (1992). Use of hemicellulolytic enzymes as one stage in bleaching of kraft pulps. Holiforschung 46, 481-488.
    • (1992) Holiforschung , vol.46 , pp. 481-488
    • Yang, J.L.1    Eriksson, K.2
  • 204
    • 0026526029 scopus 로고
    • A bifunctional xylanase encoded by the. Vv/m gene of the rumen ceiiuloiytic bacterium ruminococcus flavefaciens 17 comprises two dissimilar domains linked by an asparagine/glutamine-rich sequence
    • Zhang, J. X. and Funt, H. J. (1992). A bifunctional xylanase encoded by the. vv/M gene of the rumen ceiiuloiytic bacterium Ruminococcus flavefaciens 17 comprises two dissimilar domains linked by an asparagine/glutamine-rich sequence. Molecular Microbiology 6, 1013-1023.
    • (1992) Molecular Microbiology , vol.6 , pp. 1013-1023
    • Zhang, J.X.1    Funt, H.J.2
  • 205
    • 0027945130 scopus 로고
    • Identification of non-catalytic conserved regions in xylanases cncoded by the xynb and xynd genes of the ceiiuloiytic rumen anaerobe ruminococcus flavefaciens
    • Zhang, J. X., Martin, J. and Flint, H. J. (1994). Identification of non-catalytic conserved regions in xylanases cncoded by the xynB and xynD genes of the ceiiuloiytic rumen anaerobe Ruminococcus flavefaciens. Molecular and General Genetics 245, 269-274.
    • (1994) Molecular and General Genetics , vol.245 , pp. 269-274
    • Zhang, J.X.1    Martin, J.2    Flint, H.J.3
  • 206
    • 0028953195 scopus 로고
    • Metabolic engineering of a pentose metabolism pathway in ethanologcnic zymomonas mohilis
    • Zhang, M., Eddy, C., Deanda, K., Finkelstein, M. and Picataggio, S. (1995). Metabolic engineering of a pentose metabolism pathway in ethanologcnic Zymomonas mohilis. Science 267, 240-243.
    • (1995) Science , vol.267 , pp. 240-243
    • Zhang, M.1    Eddy, C.2    Deanda, K.3    Finkelstein, M.4    Picataggio, S.5
  • 207
    • 0028332196 scopus 로고
    • Enzymatic specificities and modes of action of the 2 catalytic domains of the xync xylanase from fibrobacter succinogenes-s85
    • Zhu, H., Paradis, F. W., Krell, P. J., Phillips, J. P. and Forsberg, C. W. (1994). Enzymatic specificities and modes of action of the 2 catalytic domains of the xync xylanase from Fibrobacter succinogenes-s85. Journal of Bacteriology 176, 3885-3894.
    • (1994) Journal of Bacteriology , 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.