메뉴 건너뛰기




Volumn 86, Issue 6, 2010, Pages 1647-1658

Properties and applications of microbial β-D-xylosidases featuring the catalytically efficient enzyme from Selenomonas ruminantium

Author keywords

Xylosidase; Bioenergy; GH43; Glycoside hydrolase; Performance; Protein engineering

Indexed keywords

ANIMAL FEED; BIO-ENERGY; BREAD DOUGH; D-XYLOSE; ENZYMATIC SACCHARIFICATION; GLYCOSIDE HYDROLASES; GLYCOSIDIC BOND; HEMICELLULASES; LIGNOCELLULOSIC BIOMASS; PERFORMANCE PROTEINS; REACTOR CONDITIONS; RECYCLED PAPER; REDUCING ENDS; SELENOMONAS; XYLANASES; XYLOOLIGOSACCHARIDES; XYLOSE RESIDUES; XYLOSIDASE;

EID: 77952881793     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-010-2538-y     Document Type: Short Survey
Times cited : (75)

References (83)
  • 1
    • 4344653896 scopus 로고    scopus 로고
    • Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: Reconstitution of the in vivo system from recombinant enzymes
    • 10.1099/mic.0.27066-0 1:CAS:528:DC%2BD2cXmtFGrtbg%3D
    • H Adelsberger C Hertel E Glawischnig VV Zverlov WH Schwarz 2004 Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes Microbiology 150 2257 2266 10.1099/mic.0.27066-0 1:CAS:528:DC%2BD2cXmtFGrtbg%3D
    • (2004) Microbiology , vol.150 , pp. 2257-2266
    • Adelsberger, H.1    Hertel, C.2    Glawischnig, E.3    Zverlov, V.V.4    Schwarz, W.H.5
  • 2
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • K Arnold L Bordoli J Kopp T Schwede 2006 The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling Bioinformatics 22 195 201 10.1093/bioinformatics/bti770 1:CAS:528:DC%2BD28XovVCltw%3D%3D (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 4
    • 0027292717 scopus 로고
    • Simultaneous high-performance liquid chromatographic determination of both the cleavage pattern and the stereochemical outcome of the hydrolysis reactions catalyzed by various glycosidases
    • DOI 10.1006/abio.1993.1320
    • C Braun A Meinke L Ziser SG Withers 1993 Simultaneous high-performance liquid chromatographic determination of both the cleavage pattern and the stereochemical outcome of the hydrolysis reactions catalyzed by various glycosidases Anal Biochem 212 259 262 10.1006/abio.1993.1320 1:CAS:528:DyaK3sXltFajsLc%3D (Pubitemid 23219482)
    • (1993) Analytical Biochemistry , vol.212 , Issue.1 , pp. 259-262
    • Braun, C.1    Meinke, A.2    Ziser, L.3    Withers, S.G.4
  • 5
    • 0035917899 scopus 로고    scopus 로고
    • Glutamic acid 160 is the acid-base catalyst of β-xylosidase from Bacillus stearothermophilus T-6: A family 39 glycoside hydrolase
    • DOI 10.1016/S0014-5793(01)02371-7, PII S0014579301023717
    • T Bravman A Mechaly S Shulami V Belakhov T Baasov G Shoham Y Shoham 2001 Glutamic acid 160 is the acid-base catalyst of β-xylosidase from Bacillus stearothermophilus T-6: a family 39 glycoside hydrolase FEBS Lett 495 115 119 10.1016/S0014-5793(01)02371-7 1:CAS:528:DC%2BD3MXivFegs70%3D (Pubitemid 32367984)
    • (2001) FEBS Letters , vol.495 , Issue.1-2 , pp. 115-119
    • Bravman, T.1    Mechaly, A.2    Shulami, S.3    Belakhov, V.4    Baasov, T.5    Shoham, G.6    Shoham, Y.7
  • 6
    • 70849107543 scopus 로고    scopus 로고
    • Wheat domestication accelerated evolution and triggered positive selection in the β-xylosidase enzyme of Mycosphaerella graminicola
    • 10.1371/journal.pone.0007884
    • PC Brunner N Keller BA McDonald 2009 Wheat domestication accelerated evolution and triggered positive selection in the β-xylosidase enzyme of Mycosphaerella graminicola PLoS ONE 4 e7884 10.1371/journal.pone.0007884
    • (2009) PLoS ONE , vol.4 , pp. 7884
    • Brunner, P.C.1    Keller, N.2    McDonald, B.A.3
  • 7
    • 43949124808 scopus 로고    scopus 로고
    • Structure of the two-subsite β-d-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane
    • 10.1016/j.abb.2008.03.007 1:CAS:528:DC%2BD1cXmsVaksbw%3D
    • JS Brunzelle DB Jordan DR McCaslin A Olczak Z Wawrzak 2008 Structure of the two-subsite β-d-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane Arch Biochem Biophys 474 157 166 10.1016/j.abb.2008.03.007 1:CAS:528:DC%2BD1cXmsVaksbw%3D
    • (2008) Arch Biochem Biophys , vol.474 , pp. 157-166
    • Brunzelle, J.S.1    Jordan, D.B.2    McCaslin, D.R.3    Olczak, A.4    Wawrzak, Z.5
  • 8
    • 33646165074 scopus 로고    scopus 로고
    • The structure of an inverting GH43 β-xylosidase from Geobacillus stearothermophilus with its substrate reveals the role of the three catalytic residues
    • 10.1016/j.jmb.2006.03.005
    • C Brüx A Ben-David D Shallom-Shezifi M Leon K Niefind G Shoham Y Shoham D Schomburg 2006 The structure of an inverting GH43 β-xylosidase from Geobacillus stearothermophilus with its substrate reveals the role of the three catalytic residues J Mol Biol 359 97 109 10.1016/j.jmb.2006.03.005
    • (2006) J Mol Biol , vol.359 , pp. 97-109
    • Brüx, C.1    Ben-David, A.2    Shallom-Shezifi, D.3    Leon, M.4    Niefind, K.5    Shoham, G.6    Shoham, Y.7    Schomburg, D.8
  • 9
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): An expert resource for Glycogenomics
    • 10.1093/nar/gkn663 1:CAS:528:DC%2BD1cXhsFejtL7K
    • BL Cantarel PM Coutinho C Rancurel T Bernard V Lombard B Henrissat 2009 The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics Nucleic Acids Res 37 D233 D238 10.1093/nar/gkn663 1:CAS:528:DC%2BD1cXhsFejtL7K
    • (2009) Nucleic Acids Res , vol.37
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5    Henrissat, B.6
  • 10
    • 0035723208 scopus 로고    scopus 로고
    • Directed evolution to produce an alkalophilic variant from a neocallimastix patriciarum xylanase
    • DOI 10.1139/cjm-47-12-1088
    • Y-L Chen T-Y Tang K-J Cheng 2001 Directed evolution to produce an alkalophilic variant from Neocallimastix patriciarum xylanase Can J Microbiol 47 1088 1094 10.1139/cjm-47-12-1088 1:CAS:528:DC%2BD38XptVymtA%3D%3D (Pubitemid 34201763)
    • (2001) Canadian Journal of Microbiology , vol.47 , Issue.12 , pp. 1088-1094
    • Chen, Y.-L.1    Tang, T.-Y.2    Cheng, K.-J.3
  • 11
    • 41049111196 scopus 로고    scopus 로고
    • High-throughput microplate technique for enzymatic hydrolysis of lignocellulosic biomass
    • DOI 10.1002/bit.21805
    • SPS Chundawat V Balan BE Dale 2008 High-throughput microplate technique for enzymatic hydrolysis of lignocellulosic biomass Biotechnol Bioeng 99 1281 1294 10.1002/bit.21805 1:CAS:528:DC%2BD1cXktVynt7o%3D (Pubitemid 351548668)
    • (2008) Biotechnology and Bioengineering , vol.99 , Issue.6 , pp. 1281-1294
    • Chundawat, S.P.S.1    Balan, V.2    Dale, B.E.3
  • 12
    • 13244264678 scopus 로고    scopus 로고
    • Improving the alkalophilic performances of the Xy11 xylanase from Streptomyces sp. S38: Structural comparison and mutational analysis
    • DOI 10.1110/ps.04978705
    • F De Lemos Esteves T Gouders J Lamotte-Brasseur S Rigali J-M Frère 2005 Improving the alkalophilic performances of the Xy11 xylanase from Streptomyces sp. S38: structural comparison and mutational analysis Protein Sci 14 292 302 10.1110/ps.04978705 (Pubitemid 40194581)
    • (2005) Protein Science , vol.14 , Issue.2 , pp. 292-302
    • De Lemos Esteves, F.1    Gouders, T.2    Lamotte-Brasseur, J.3    Rigali, S.4    Frere, J.-M.5
  • 13
    • 34548357136 scopus 로고    scopus 로고
    • Impact of wheat flour-associated endoxylanases on arabinoxylan in dough after mixing and resting
    • DOI 10.1021/jf071363m
    • E Dornez K Gebruers S Cuyvers JA Delcour CM Courtin 2007 Impact of wheat flour-associated endoxylanases on arabinoxylan in dough after mixing and resting J Agric Food Chem 55 7149 7155 10.1021/jf071363m 1:CAS:528:DC%2BD2sXot1Gks7g%3D (Pubitemid 47338959)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.17 , pp. 7149-7155
    • Dornez, E.1    Gebruers, K.2    Cuyvers, S.3    Delcour, J.A.4    Courtin, C.M.5
  • 15
    • 0001799213 scopus 로고
    • Conformational analysis of sugars and their derivatives
    • 10.1016/S0065-2318(08)60366-2 1:CAS:528:DyaE38Xos1ShsA%3D%3D
    • PL Durette D Horton 1971 Conformational analysis of sugars and their derivatives Adv Carbohydr Chem Biochem 26 49 125 10.1016/S0065-2318(08)60366-2 1:CAS:528:DyaE38Xos1ShsA%3D%3D
    • (1971) Adv Carbohydr Chem Biochem , vol.26 , pp. 49-125
    • Durette, P.L.1    Horton, D.2
  • 16
    • 60349113795 scopus 로고    scopus 로고
    • The construction and characterization of two xylan-degrading chimeric enzymes
    • 10.1002/bit.22112
    • Z Fan K Wagschal CC Lee Q Kong KA Shen IB Maiti L Yuan 2008 The construction and characterization of two xylan-degrading chimeric enzymes Biotechnol Bioeng 102 684 692 10.1002/bit.22112
    • (2008) Biotechnol Bioeng , vol.102 , pp. 684-692
    • Fan, Z.1    Wagschal, K.2    Lee, C.C.3    Kong, Q.4    Shen, K.A.5    Maiti, I.B.6    Yuan, L.7
  • 17
    • 62149093600 scopus 로고    scopus 로고
    • Multimeric hemicellulases facilitate biomass conversion
    • 10.1128/AEM.02181-08 1:CAS:528:DC%2BD1MXjsFKgtrg%3D
    • Z Fan K Wagschal W Chen MD Montross CC Lee L Yuan 2009 Multimeric hemicellulases facilitate biomass conversion Appl Environ Microbiol 75 1754 1757 10.1128/AEM.02181-08 1:CAS:528:DC%2BD1MXjsFKgtrg%3D
    • (2009) Appl Environ Microbiol , vol.75 , pp. 1754-1757
    • Fan, Z.1    Wagschal, K.2    Chen, W.3    Montross, M.D.4    Lee, C.C.5    Yuan, L.6
  • 18
    • 65249122405 scopus 로고    scopus 로고
    • Engineering of a multifunctional hemicellulase
    • 10.1007/s10529-009-9926-3 1:CAS:528:DC%2BD1MXkt1yisLw%3D
    • Z Fan JR Werkman L Yuan 2009 Engineering of a multifunctional hemicellulase Biotechnol Lett 31 751 757 10.1007/s10529-009-9926-3 1:CAS:528:DC%2BD1MXkt1yisLw%3D
    • (2009) Biotechnol Lett , vol.31 , pp. 751-757
    • Fan, Z.1    Werkman, J.R.2    Yuan, L.3
  • 20
    • 28444448431 scopus 로고    scopus 로고
    • Increased alkali stability in Trichoderma reesei endo-1,4-β-xylanase II by site directed mutagenesis
    • DOI 10.1016/j.jbiotec.2005.07.010, PII S0168165605002919
    • F Fenel A-J Zitting A Kantelinen 2006 Increased alkali stability in Trichoderma reesei endo-1,4-β-xylanase II by site-directed mutagenesis J Biotechnol 121 102 107 10.1016/j.jbiotec.2005.07.010 1:CAS:528: DC%2BD2MXht12ksbvK (Pubitemid 41739669)
    • (2006) Journal of Biotechnology , vol.121 , Issue.1 , pp. 102-107
    • Fenel, F.1    Zitting, A.-J.2    Kantelinen, A.3
  • 21
    • 20444504291 scopus 로고    scopus 로고
    • Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125
    • DOI 10.1074/jbc.M413693200
    • S Fushinobu M Hidaka Y Honda T Wakagi H Shoun M Kitaoka 2005 Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125 J Biol Chem 280 17180 17186 10.1074/jbc. M413693200 1:CAS:528:DC%2BD2MXjsFOgtb4%3D (Pubitemid 41389184)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17180-17186
    • Fushinobu, S.1    Hidaka, M.2    Honda, Y.3    Wakagi, T.4    Shoun, H.5    Kitaoka, M.6
  • 22
    • 73749087300 scopus 로고    scopus 로고
    • Mixture optimization of six core glycosyl hydrolases for maximizing saccharification of ammonia fiber expansion (AFEX) pretreated corn stover
    • 10.1016/j.biortech.2009.10.056 1:CAS:528:DC%2BC3cXjvVegug%3D%3D
    • D Gao SPS Chundawat C Krishnan W Balan BE Dale 2010 Mixture optimization of six core glycosyl hydrolases for maximizing saccharification of ammonia fiber expansion (AFEX) pretreated corn stover Bioresource Technol 101 2770 2781 10.1016/j.biortech.2009.10.056 1:CAS:528:DC%2BC3cXjvVegug%3D%3D
    • (2010) Bioresource Technol , vol.101 , pp. 2770-2781
    • Gao, D.1    Chundawat, S.P.S.2    Krishnan, C.3    Balan, W.4    Dale, B.E.5
  • 23
    • 65249175725 scopus 로고    scopus 로고
    • A family of thermostable fungal cellulases created by structure-guided recombination
    • 10.1073/pnas.0901417106 1:CAS:528:DC%2BD1MXkvFGhtbs%3D
    • P Heinzelman CD Snow I Wu C Nguyen A Villalobos S Govindarajan J Minshull FH Arnold 2009 A family of thermostable fungal cellulases created by structure-guided recombination Proc Nat Acad Sci 106 5610 5615 10.1073/pnas.0901417106 1:CAS:528:DC%2BD1MXkvFGhtbs%3D
    • (2009) Proc Nat Acad Sci , vol.106 , pp. 5610-5615
    • Heinzelman, P.1    Snow, C.D.2    Wu, I.3    Nguyen, C.4    Villalobos, A.5    Govindarajan, S.6    Minshull, J.7    Arnold, F.H.8
  • 24
    • 11244279648 scopus 로고    scopus 로고
    • A family 8 glycoside hydrolase from Bacillus halodurans C-125 (BH2105) is a reducing end xylose-releasing exo-oligoxylanase
    • DOI 10.1074/jbc.M409832200
    • Y Honda M Kitaoka 2004 A family 8 glycoside hydrolase from Bacillus halodurans C-125 (BH2105) is a reducing end xylose-releasing exo-oligoxylanase J Biol Chem 279 55097 55103 10.1074/jbc.M409832200 1:CAS:528:DC%2BD2cXhtFeis7%2FM (Pubitemid 40066502)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55097-55103
    • Honda, Y.1    Kitaoka, M.2
  • 25
    • 43949083068 scopus 로고    scopus 로고
    • β-d-Xylosidase from Selenomonas ruminantium: Catalyzed reactions with natural and artificial substrates
    • 10.1007/s12010-007-8064-4 1:CAS:528:DC%2BD1MXptVGluw%3D%3D
    • DB Jordan 2008 β-d-Xylosidase from Selenomonas ruminantium: catalyzed reactions with natural and artificial substrates Appl Biochem Biotechnol 146 137 149 10.1007/s12010-007-8064-4 1:CAS:528: DC%2BD1MXptVGluw%3D%3D
    • (2008) Appl Biochem Biotechnol , vol.146 , pp. 137-149
    • Jordan, D.B.1
  • 26
    • 34548039761 scopus 로고    scopus 로고
    • Inhibition of the two-subsite β-d-xylosidase from Selenomonas ruminantium by sugars: Competitive, noncompetitive, double binding, and slow binding modes
    • DOI 10.1016/j.abb.2007.05.016, PII S0003986107002743
    • DB Jordan JD Braker 2007 Inhibition of the two-subsite β-d-xylosidase from Selenomonas ruminantium by sugars: competitive, noncompetitive, double binding, and slow binding modes Arch Biochem Biophys 465 231 246 10.1016/j.abb.2007.05.016 1:CAS:528:DC%2BD2sXpsFGhtbY%3D (Pubitemid 47283993)
    • (2007) Archives of Biochemistry and Biophysics , vol.465 , Issue.1 , pp. 231-246
    • Jordan, D.B.1    Braker, J.D.2
  • 27
    • 66349114761 scopus 로고    scopus 로고
    • β-d-Xylosidase from Selenomonas ruminantium: Thermodynamics of enzyme-catalyzed and noncatalyzed reactions
    • 10.1007/s12010-008-8397-7 1:CAS:528:DC%2BD1MXhtlSisbnI
    • DB Jordan JD Braker 2009 β-d-Xylosidase from Selenomonas ruminantium: thermodynamics of enzyme-catalyzed and noncatalyzed reactions Appl Biochem Biotechnol 155 330 346 10.1007/s12010-008-8397-7 1:CAS:528: DC%2BD1MXhtlSisbnI
    • (2009) Appl Biochem Biotechnol , vol.155 , pp. 330-346
    • Jordan, D.B.1    Braker, J.D.2
  • 28
    • 77949658725 scopus 로고    scopus 로고
    • β-d-Xylosidase from Selenomonas ruminantium: Role of glutamate 186 in catalysis revealed by site-directed mutagenesis, alternate substrates, and active-site inhibitor
    • 10.1007/s12010-009-8874-7 10.1007/s12010-009-8874-7 1:CAS:528: DC%2BC3cXkt12msb0%3D
    • DB Jordan JD Braker 2010 β-d-Xylosidase from Selenomonas ruminantium: role of glutamate 186 in catalysis revealed by site-directed mutagenesis, alternate substrates, and active-site inhibitor Appl Biochem Biotechnol 161 395 410 10.1007/s12010-009-8874-7 10.1007/s12010-009-8874-7 1:CAS:528:DC%2BC3cXkt12msb0%3D
    • (2010) Appl Biochem Biotechnol , vol.161 , pp. 395-410
    • Jordan, D.B.1    Braker, J.D.2
  • 29
    • 34548249519 scopus 로고    scopus 로고
    • Variation in relative substrate specificity of bifunctional β-d-xylosidase/α-l-arabinofuranosidase by single-site mutations: Roles of substrate distortion and recognition
    • 1:CAS:528:DC%2BD2sXpvFWlurk%3D
    • DB Jordan X-L Li 2007 Variation in relative substrate specificity of bifunctional β-d-xylosidase/α-l-arabinofuranosidase by single-site mutations: roles of substrate distortion and recognition Biochim Biophys Acta 1774 1192 1198 1:CAS:528:DC%2BD2sXpvFWlurk%3D
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 1192-1198
    • Jordan, D.B.1    Li, X.-L.2
  • 30
    • 34548010301 scopus 로고    scopus 로고
    • β-d-Xylosidase from Selenomonas ruminantium of glycoside hydrolase family 43
    • 10.1007/s12010-007-9042-6
    • DB Jordan X-L Li CA Dunlap TR Whitehead MA Cotta 2007 β-d-Xylosidase from Selenomonas ruminantium of glycoside hydrolase family 43 Appl Biochem Biotechnol 136-140 93 104 10.1007/s12010-007-9042-6
    • (2007) Appl Biochem Biotechnol , vol.136-140 , pp. 93-104
    • Jordan, D.B.1    Li, X.-L.2    Dunlap, C.A.3    Whitehead, T.R.4    Cotta, M.A.5
  • 31
    • 34547512927 scopus 로고    scopus 로고
    • Structure-function relationships of a catalytically efficient β-D-xylosidase
    • DOI 10.1007/s12010-007-9210-8, PII ABAB141151
    • DB Jordan X-L Li CA Dunlap TR Whitehead MA Cotta 2007 Structure-function relationships of a catalytically efficient β-d-xylosidase Appl Biochem Biotechnol 141 51 76 10.1007/s12010-007-9210-8 1:CAS:528:DC%2BD2sXlsFCns7g%3D (Pubitemid 47186940)
    • (2007) Applied Biochemistry and Biotechnology , vol.141 , Issue.1 , pp. 51-76
    • Jordan, D.B.1    Li, X.-L.2    Dunlap, C.A.3    Whitehead, T.R.4    Cotta, M.A.5
  • 32
    • 56449104687 scopus 로고    scopus 로고
    • Aminoalcohols as probes of the two-subsite active site of β-d-xylosidase from Selenomonas ruminantium
    • 1:CAS:528:DC%2BD1cXhsVCmsLbN
    • DB Jordan JA Mertens JD Braker 2009 Aminoalcohols as probes of the two-subsite active site of β-d-xylosidase from Selenomonas ruminantium Biochim Biophys Acta 1794 144 158 1:CAS:528:DC%2BD1cXhsVCmsLbN
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 144-158
    • Jordan, D.B.1    Mertens, J.A.2    Braker, J.D.3
  • 34
    • 28444439172 scopus 로고    scopus 로고
    • Enzymatic transglycosylation of xylose using a glycosynthase
    • DOI 10.1016/j.carres.2005.09.010, PII S0008621505004386
    • YW Kim H Chen SG Withers 2005 Enzymatic transglycosylation of xylose using a glycosynthase Carbohydr Res 340 2735 2741 10.1016/j.carres.2005.09.010 1:CAS:528:DC%2BD2MXht1Oiur%2FJ (Pubitemid 41735360)
    • (2005) Carbohydrate Research , vol.340 , Issue.18 , pp. 2735-2741
    • Kim, Y.-W.1    Chen, H.2    Withers, S.G.3
  • 35
    • 12544249147 scopus 로고    scopus 로고
    • Inhibition of ethanol-producing yeast and bacteria by degradation products produced during pre-treatment of biomass
    • 10.1007/s00253-004-1642-2 1:CAS:528:DC%2BD2cXpsFKrtr0%3D
    • HB Klinke AB Thomsen BK Ahring 2004 Inhibition of ethanol-producing yeast and bacteria by degradation products produced during pre-treatment of biomass Appl Microbiol Biotechnol 66 10 26 10.1007/s00253-004-1642-2 1:CAS:528:DC%2BD2cXpsFKrtr0%3D
    • (2004) Appl Microbiol Biotechnol , vol.66 , pp. 10-26
    • Klinke, H.B.1    Thomsen, A.B.2    Ahring, B.K.3
  • 36
    • 0027300122 scopus 로고
    • Hydrolyses of α- And β-cellobiosyl fluorides by cellobiohydrolases of Trichoderma reesei
    • 1:CAS:528:DyaK3sXksVCjtbY%3D
    • AK Konstantinidis I Marsden ML Sinnott 1993 Hydrolyses of α- and β-cellobiosyl fluorides by cellobiohydrolases of Trichoderma reesei Biochem J 291 883 888 1:CAS:528:DyaK3sXksVCjtbY%3D
    • (1993) Biochem J , vol.291 , pp. 883-888
    • Konstantinidis, A.K.1    Marsden, I.2    Sinnott, M.L.3
  • 37
    • 84979146389 scopus 로고
    • Stereochemistry and mechanism of enzyme reactions
    • 10.1111/j.1469-185X.1953.tb01386.x 1:CAS:528:DyaG2cXhtFCrsQ%3D%3D
    • DE Koshland 1953 Stereochemistry and mechanism of enzyme reactions Biol Rev 28 416 436 10.1111/j.1469-185X.1953.tb01386.x 1:CAS:528:DyaG2cXhtFCrsQ%3D%3D
    • (1953) Biol Rev , vol.28 , pp. 416-436
    • Koshland, D.E.1
  • 38
    • 0035650539 scopus 로고    scopus 로고
    • Degradation of Xylan to D-Xylose by Recombinant Saccharomyces cerevisiae Coexpressing the Aspergillus niger β-Xylosidase (xlnD) and the Trichoderma reesei Xylanase II (xyn2) Genes
    • DOI 10.1128/AEM.67.12.5512-5519.2001
    • DC La Grange IS Pretorius M Claeyssens WH van Zyl 2001 Degradation of xylan to d-xylose by recombinant Saccharomyces cerevisiae coexpressing the Aspergillus niger β-xylosidase (xlnD) and the Trichoderma reesei xylanase II (xyn2) genes Appl Environ Microbiol 67 5512 5519 10.1128/AEM.67.12.5512-5519. 2001 (Pubitemid 33640983)
    • (2001) Applied and Environmental Microbiology , vol.67 , Issue.12 , pp. 5512-5519
    • La Grange, D.C.1    Pretorius, I.S.2    Claeyssens, M.3    Van Zyl, W.H.4
  • 39
  • 40
    • 9144219793 scopus 로고    scopus 로고
    • Mechanistic analogies amongst carbohydrate modifying enzymes
    • DOI 10.1039/b406490a
    • LL Lairson SG Withers 2004 Mechanistic analogies amongst carbohydrate modifying enzymes Chem Commun 2 2243 2248 10.1039/b406490a (Pubitemid 39545881)
    • (2004) Chemical Communications , Issue.20 , pp. 2243-2248
    • Lairson, L.L.1    Withers, S.G.2
  • 41
    • 0034603740 scopus 로고    scopus 로고
    • Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus β-glucosidase CelB by directed evolution
    • DOI 10.1021/bi991483q
    • JHG Lebbink T Kaper P Bron J van der Oost WM de Vos 2000 Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus β-glucosidase CelB by directed evolution Biochemistry 39 3656 3665 10.1021/bi991483q 1:CAS:528:DC%2BD3cXhsFyhsbo%3D (Pubitemid 30183846)
    • (2000) Biochemistry , vol.39 , Issue.13 , pp. 3656-3665
    • Lebbink, J.H.G.1    Kaper, T.2    Bron, P.3    Van Der Oost, J.4    De Vos, W.M.5
  • 42
    • 61449190669 scopus 로고    scopus 로고
    • Improved catalytic efficiency of endo-β-1,4-glucanase from Bacillus subtilis BME-15 by directed evolution
    • 10.1007/s00253-008-1789-3 1:CAS:528:DC%2BD1MXisVWktLc%3D
    • L Lin X Meng P Liu Y Hong G Wu X Huang C Li J Dong L Xiao Z Liu 2009 Improved catalytic efficiency of endo-β-1,4-glucanase from Bacillus subtilis BME-15 by directed evolution Appl Microbiol Biotechnol 82 671 679 10.1007/s00253-008-1789-3 1:CAS:528:DC%2BD1MXisVWktLc%3D
    • (2009) Appl Microbiol Biotechnol , vol.82 , pp. 671-679
    • Lin, L.1    Meng, X.2    Liu, P.3    Hong, Y.4    Wu, G.5    Huang, X.6    Li, C.7    Dong, J.8    Xiao, L.9    Liu, Z.10
  • 43
    • 66049105477 scopus 로고    scopus 로고
    • Rational pH-engineering of the thermostable xylanase based on computational model
    • 10.1016/j.procbio.2009.02.013 1:CAS:528:DC%2BD1MXms1Onurw%3D
    • L Liu B Wang H Chen S Wang M Wang S Zhang A Song J Shen K Wu X Jia 2009 Rational pH-engineering of the thermostable xylanase based on computational model Process Biochem 44 912 915 10.1016/j.procbio.2009.02.013 1:CAS:528:DC%2BD1MXms1Onurw%3D
    • (2009) Process Biochem , vol.44 , pp. 912-915
    • Liu, L.1    Wang, B.2    Chen, H.3    Wang, S.4    Wang, M.5    Zhang, S.6    Song, A.7    Shen, J.8    Wu, K.9    Jia, X.10
  • 44
    • 0029887839 scopus 로고    scopus 로고
    • Amino acid substitutions enhancing the thermostability of Bacillus polymyxa β-glucosidase A
    • 1:CAS:528:DyaK28XhvFyjtrg%3D
    • C Lopez-Camacho J Salgado JL Lequerica A Madarro E Ballestar L Franco J Polaina 1996 Amino acid substitutions enhancing the thermostability of Bacillus polymyxa β-glucosidase A Biochem J 314 833 838 1:CAS:528:DyaK28XhvFyjtrg%3D
    • (1996) Biochem J , vol.314 , pp. 833-838
    • Lopez-Camacho, C.1    Salgado, J.2    Lequerica, J.L.3    Madarro, A.4    Ballestar, E.5    Franco, L.6    Polaina, J.7
  • 45
    • 12544256784 scopus 로고    scopus 로고
    • Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate
    • 10.1074/jbc.M410468200 1:CAS:528:DC%2BD2MXksVWgsQ%3D%3D
    • AL Lovering SS Lee Y-W Kim SG Withers NCJ Strynadka 2005 Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate J Biol Chem 280 2105 2115 10.1074/jbc.M410468200 1:CAS:528:DC%2BD2MXksVWgsQ%3D%3D
    • (2005) J Biol Chem , vol.280 , pp. 2105-2115
    • Lovering, A.L.1    Lee, S.S.2    Kim, Y.-W.3    Withers, S.G.4    Strynadka, N.C.J.5
  • 46
    • 0036008701 scopus 로고    scopus 로고
    • Identification of potential fermentation inhibitors in conversion of hybrid poplar hydrolyzate to ethanol
    • DOI 10.1016/S0961-9534(01)00061-7, PII S0961953401000617
    • CD Luo DL Brink HW Blanch 2002 Identification of potential fermentation inhibitors in conversion of hybrid poplar hydrolyzate to ethanol Biomass Bioenergy 22 125 138 10.1016/S0961-9534(01)00061-7 1:CAS:528: DC%2BD38XhtFGkurs%3D (Pubitemid 34186341)
    • (2002) Biomass and Bioenergy , vol.22 , Issue.2 , pp. 125-138
    • Luo, C.1    Brink, D.L.2    Blanch, H.W.3
  • 47
    • 0033514342 scopus 로고    scopus 로고
    • Screening of non-Saccharomyces wine yeasts for the production of β-D- xylosidase activity
    • DOI 10.1016/S0168-1605(98)00186-X, PII S016816059800186X
    • P Manzanares D Ramon A Querol 1999 Screening of non-Saccharomyces wine yeasts for production of β-xylosidase activity Int J Food Micro 46 105 112 10.1016/S0168-1605(98)00186-X 1:CAS:528:DyaK1MXhs1OrsrY%3D (Pubitemid 29057154)
    • (1999) International Journal of Food Microbiology , vol.46 , Issue.2 , pp. 105-112
    • Manzanares, P.1    Ramon, D.2    Querol, A.3
  • 48
    • 0037434449 scopus 로고    scopus 로고
    • Characterisation and application of glycanases secreted by Aspergillus terreus CCMI 498 and Trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper
    • DOI 10.1016/S0168-1656(02)00247-X, PII S016816560200247X
    • S Marques H Pala L Alves MT Amaral-Collaço FM Gama FM Gírio 2003 Characterisation and application of glycanases secreted by Aspergillus terreus CCMI 498 and Trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper J Biotechnol 100 209 219 10.1016/S0168-1656(02)00247-X 1:CAS:528:DC%2BD38XoslahsL4%3D (Pubitemid 35346531)
    • (2003) Journal of Biotechnology , vol.100 , Issue.3 , pp. 209-219
    • Marques, S.1    Pala, H.2    Alves, L.3    Amaral-Collaco, M.T.4    Gama, F.M.5    Girio, F.M.6
  • 49
    • 33646168883 scopus 로고    scopus 로고
    • Structural elements to convert Escherichia coli α-xylosidase (YicI) into α-glucosidase
    • 10.1016/j.febslet.2006.04.025 1:CAS:528:DC%2BD28XksFaqs7w%3D
    • M Okuyama A Kaneko H Mori S Chiba A Kimura 2006 Structural elements to convert Escherichia coli α-xylosidase (YicI) into α-glucosidase FEBS Lett 580 2707 2711 10.1016/j.febslet.2006.04.025 1:CAS:528:DC%2BD28XksFaqs7w%3D
    • (2006) FEBS Lett , vol.580 , pp. 2707-2711
    • Okuyama, M.1    Kaneko, A.2    Mori, H.3    Chiba, S.4    Kimura, A.5
  • 50
    • 0033585830 scopus 로고    scopus 로고
    • Influence of furfural on anaerobic glycolytic kinetics of saccharomyces cerevisiae in batch culture
    • DOI 10.1002/(SICI)1097-0290(19990220)62:4<447::AID-BIT7>3.0.CO;2-0
    • E Palmqvist JS Almeida B Hahn-Hägerdal 1999 Influence of furfural on anaerobic glycolytic kinetics of Saccharomyces cerevisiae in batch culture Biotechnol Bioeng 62 447 454 10.1002/(SICI)1097-0290(19990220)62:4<447::AID- BIT7>3.0.CO;2-0 1:CAS:528:DyaK1MXns1CisA%3D%3D (Pubitemid 29052879)
    • (1999) Biotechnology and Bioengineering , vol.62 , Issue.4 , pp. 447-454
    • Palmqvist, E.1    Almeida, J.S.2    Hahn-Hagerdal, B.3
  • 52
    • 33746913962 scopus 로고    scopus 로고
    • Mode of action and properties of the β-xylosidases from Talaromyces emersonii and Trichoderma reesei
    • DOI 10.1002/bit.20908
    • LE Rasmussen HR Sørensen J Vind A Viksø-Nielsen 2006 Mode of action and properties of the β-xylosidases from Talaromyces emersonii and Trichoderma reesi Biotechnol Bioengineer 94 869 876 10.1002/bit.20908 1:CAS:528:DC%2BD28XntFGju78%3D (Pubitemid 44186894)
    • (2006) Biotechnology and Bioengineering , vol.94 , Issue.5 , pp. 869-876
    • Rasmussen, L.E.1    Sorensen, H.R.2    Vind, J.3    Vikso-Nielsen, A.4
  • 53
    • 48349138645 scopus 로고    scopus 로고
    • Covalent inhibitors of glycosidases and their applications in biochemistry and biology
    • 10.1093/glycob/cwn041 1:CAS:528:DC%2BD1cXoslGlsL4%3D
    • BP Rempel SG Withers 2008 Covalent inhibitors of glycosidases and their applications in biochemistry and biology Glycobiology 18 570 586 10.1093/glycob/cwn041 1:CAS:528:DC%2BD1cXoslGlsL4%3D
    • (2008) Glycobiology , vol.18 , pp. 570-586
    • Rempel, B.P.1    Withers, S.G.2
  • 54
    • 0033780356 scopus 로고    scopus 로고
    • Glycosidase mechanisms
    • 10.1016/S1367-5931(00)00135-6 1:CAS:528:DC%2BD3cXnsFOrsrs%3D
    • CS Rye SG Withers 2000 Glycosidase mechanisms Curr Opin Chem Biol 4 573 580 10.1016/S1367-5931(00)00135-6 1:CAS:528:DC%2BD3cXnsFOrsrs%3D
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 573-580
    • Rye, C.S.1    Withers, S.G.2
  • 55
    • 42149186349 scopus 로고    scopus 로고
    • Teaching old enzymes new tricks: Engineering and evolution of glycosidases and glycosyl transferases for improved glycoside synthesis
    • DOI 10.1139/O07-149
    • FA Shaikh SG Withers 2008 Teaching old enzymes new tricks: engineering and evolution of glycosidases and glycosyl transferases for improved glycoside synthesis Biochem Cell Biol 86 169 177 10.1139/O07-149 1:CAS:528: DC%2BD1cXlvVCqsLs%3D (Pubitemid 351536497)
    • (2008) Biochemistry and Cell Biology , vol.86 , Issue.2 , pp. 169-177
    • Shaikh, F.A.1    Withers, S.G.2
  • 56
    • 19944427947 scopus 로고    scopus 로고
    • Biochemical characterization and identification of the catalytic residues of a family 43 β-D-xylosidase from Geobacillus stearothermophilus T-6
    • DOI 10.1021/bi048059w
    • D Shallom M Leon T Bravman A Ben-David G Zaide V Belakhov G Shoham D Schomburg T Baasov Y Shoham 2005 Biochemical characterization and identification of the catalytic residues of a family 43 β-d-xylosidase from Geobacillus stearothermophilus T-6 Biochemistry 44 387 397 10.1021/bi048059w 1:CAS:528:DC%2BD2cXhtVegtLjJ (Pubitemid 40095741)
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 387-397
    • Shallom, D.1    Leon, M.2    Bravman, T.3    Ben-David, A.4    Zaide, G.5    Belakhov, V.6    Shoham, G.7    Schomburg, D.8    Baasov, T.9    Shoham, Y.10
  • 58
    • 33847168573 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of wheat arabinoxylan by a recombinant "minimal" enzyme cocktail containing β-xylosidase and novel endo-1,4-β-xylanase and α-L-arabinofuranosidase activities
    • DOI 10.1021/bp0601701
    • HR Sørensen S Pedersen CT Jørgensen AS Meyer 2007 Enzymatic hydrolysis of wheat arabinoxylan by a recombinant "minimal" enzyme cocktail containing β-xylosidase and novel endo-1,4-β-xylanase and α-l-arabinofuranosidase activities Biotechnol Prog 23 100 107 10.1021/bp0601701 (Pubitemid 46293492)
    • (2007) Biotechnology Progress , vol.23 , Issue.1 , pp. 100-107
    • Sorensen, H.R.1    Pedersen, S.2    Jorgensen, C.T.3    Meyer, A.S.4
  • 59
    • 33947654156 scopus 로고    scopus 로고
    • Expression in Escherichia coli and characterization of β-xylosidases GH39 and GH-43 from Bacillus halodurans C-125
    • DOI 10.1007/s00253-006-0512-5
    • I Smaali C Rémond MJ O'Donohue 2006 Expression in Escherichia coli and characterization of β-xylosidases GH39 and GH-43 from Bacillus halodurans C-125 Appl Microbiol Biotechnol 73 582 590 10.1007/s00253-006-0512-5 1:CAS:528:DC%2BD2sXot1Cn (Pubitemid 350262637)
    • (2006) Applied Microbiology and Biotechnology , vol.73 , Issue.3 , pp. 582-590
    • Smaali, I.1    Remond, C.2    O'Donohue, M.J.3
  • 60
    • 47049123955 scopus 로고    scopus 로고
    • Heterologous expression of glycosyl hydrolases in planta: A new departure for biofuels
    • 10.1016/j.tibtech.2008.05.002 1:CAS:528:DC%2BD1cXoslegt7g%3D
    • LE Taylor Z Dai SR Decker R Brunecky WS Adney S-Y Ding ME Himmel 2008 Heterologous expression of glycosyl hydrolases in planta: a new departure for biofuels Trends in Biotechnol 26 413 424 10.1016/j.tibtech.2008.05.002 1:CAS:528:DC%2BD1cXoslegt7g%3D
    • (2008) Trends in Biotechnol , vol.26 , pp. 413-424
    • Taylor, L.E.1    Dai, Z.2    Decker, S.R.3    Brunecky, R.4    Adney, W.S.5    Ding, S.-Y.6    Himmel, M.E.7
  • 61
    • 0035430729 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding an intracellular β-D-xylosidase from Streptomyces thermoviolaceus OPC-520
    • DOI 10.1271/bbb.65.1824
    • H Tsujibo A Takada M Kosaka K Miyamoto Y Inamori 2001 Cloning, sequencing, and expression of the gene encoding an intracellular β-d-xylosidase from Streptomyces thermoviolaceus OPC-520 Biosci Biotech Biochem 65 1824 1831 10.1271/bbb.65.1824 1:CAS:528:DC%2BD3MXmslSltbo%3D (Pubitemid 33617789)
    • (2001) Bioscience, Biotechnology and Biochemistry , vol.65 , Issue.8 , pp. 1824-1831
    • Tsujibo, H.1    Takada, C.2    Tsuji, A.3    Kosaka, M.4    Miyamoto, K.5    Inamori, Y.6
  • 62
    • 37849012558 scopus 로고    scopus 로고
    • Cloning of a novel gene encoding β-1,3-xylosidase from a marine bacterium, Vibrio sp. strain XY-214, and characterization of the gene product
    • 10.1128/AEM.01793-07 1:CAS:528:DC%2BD1cXnsVGqtg%3D%3D
    • Y Umemoto R Onishi T Araki 2008 Cloning of a novel gene encoding β-1,3-xylosidase from a marine bacterium, Vibrio sp. strain XY-214, and characterization of the gene product Appl Environ Microbiol 74 305 308 10.1128/AEM.01793-07 1:CAS:528:DC%2BD1cXnsVGqtg%3D%3D
    • (2008) Appl Environ Microbiol , vol.74 , pp. 305-308
    • Umemoto, Y.1    Onishi, R.2    Araki, T.3
  • 63
    • 67149131557 scopus 로고    scopus 로고
    • Improvement of alkaliphily of Bacillus alkaline xylanase by introducing amino acid substitutions both on catalytic cleft and protein surface
    • 10.1271/bbb.80869 1:CAS:528:DC%2BD1MXlsFCgsrY%3D
    • H Umemoto IM Ihsanawati R Yatsunami T Fukui T Kumasaka N Tanaka S Nakamura 2009 Improvement of alkaliphily of Bacillus alkaline xylanase by introducing amino acid substitutions both on catalytic cleft and protein surface Biosci Biotechnol Biochem 73 965 967 10.1271/bbb.80869 1:CAS:528: DC%2BD1MXlsFCgsrY%3D
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 965-967
    • Umemoto, H.1    Ihsanawati, I.M.2    Yatsunami, R.3    Fukui, T.4    Kumasaka, T.5    Tanaka, N.6    Nakamura, S.7
  • 64
    • 0038780949 scopus 로고
    • Hydrolysis of β-d-xylo-oligosaccharides by β-d-xylosidase from Bacillus pumilus
    • 10.1016/0008-6215(85)85136-3
    • E Van Doorslaer H Kersters-Hilderson CK De Bruyne 1985 Hydrolysis of β-d-xylo-oligosaccharides by β-d-xylosidase from Bacillus pumilus Carbohydr Res 140 342 346 10.1016/0008-6215(85)85136-3
    • (1985) Carbohydr Res , vol.140 , pp. 342-346
    • Van Doorslaer, E.1    Kersters-Hilderson, H.2    De Bruyne, C.K.3
  • 65
    • 0032532593 scopus 로고    scopus 로고
    • Identification of Glu-277 as the catalytic nucleophile of Thermoanaerobacterium saccharolyticum β-xylosidase using electrospray MS
    • DJ Vocadlo LF Mackenzie S He GJ Zeikus SG Withers 1998 Identification of Glu-277 as the catalytic nucleophile of Thermoanaerobacterium saccharolyticum β-xylosidase using electrospray MS Biochem J 335 449 455 1:CAS:528:DyaK1cXntFWnurw%3D (Pubitemid 28491083)
    • (1998) Biochemical Journal , vol.335 , Issue.2 , pp. 449-455
    • Vocadlo, D.J.1    Mackenzie, L.F.2    He, S.3    Zeikus, G.J.4    Withers, S.G.5
  • 66
    • 25144473735 scopus 로고    scopus 로고
    • Enzyme-coupled assay for β-xylosidase hydrolysis of natural substrates
    • DOI 10.1128/AEM.71.9.5318-5323.2005
    • K Wagschal D Franqui-Espiet CC Lee GH Robertson DW Wong 2005 Enzyme-coupled assay for β-xylosidase hydrolysis of natural substrates Appl Environ Microbiol 71 5318 5323 10.1128/AEM.71.9.5318-5323.2005 1:CAS:528:DC%2BD2MXhtVahtr%2FO (Pubitemid 41338264)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.9 , pp. 5318-5323
    • Wagschal, K.1    Franqui-Espiet, D.2    Lee, C.C.3    Robertson, G.H.4    Wong, D.W.S.5
  • 67
    • 33847347613 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of an α-l- arabinofuranosidase isolated from a compost starter mixture
    • DOI 10.1016/j.enzmictec.2006.06.007, PII S0141022906003346
    • K Wagschal C Franqui-Espiet CC Lee RE Kibblewhite-Accinelli GH Robertson DW Wong 2007 Genetic and biochemical characterization of an α-l- arabinofuranosidase isolated from a compost starter mixture Enz Microbial Technol 40 747 753 10.1016/j.enzmictec.2006.06.007 1:CAS:528: DC%2BD2sXit1GksLk%3D (Pubitemid 46331852)
    • (2007) Enzyme and Microbial Technology , vol.40 , Issue.4 , pp. 747-753
    • Wagschal, K.1    Franqui-Espiet, D.2    Lee, C.C.3    Kibblewhite-Accinelli, R.E.4    Robertson, G.H.5    Wong, D.W.S.6
  • 68
    • 49349105229 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a glycoside hydrolase family 39 xylosidase from Bacillus halodurans C-125
    • 10.1007/s12010-007-8055-5 1:CAS:528:DC%2BD1MXptVGlsQ%3D%3D
    • K Wagschal D Franqui-Espiet CC Lee GH Robertson DW Wong 2008 Cloning, expression and characterization of a glycoside hydrolase family 39 xylosidase from Bacillus halodurans C-125 Appl Biochem Biotechnol 146 69 78 10.1007/s12010-007-8055-5 1:CAS:528:DC%2BD1MXptVGlsQ%3D%3D
    • (2008) Appl Biochem Biotechnol , vol.146 , pp. 69-78
    • Wagschal, K.1    Franqui-Espiet, D.2    Lee, C.C.3    Robertson, G.H.4    Wong, D.W.5
  • 69
    • 66349118920 scopus 로고    scopus 로고
    • Purification and characterization of a glycoside hydrolase family 43 β-xylosidase from Geobacillus thermoleovorans IT-08
    • 10.1007/s12010-008-8362-5 1:CAS:528:DC%2BD1MXhtlSisbnN
    • K Wagschal C Heng CC Lee GH Robertson WJ Orts DW Wong 2009 Purification and characterization of a glycoside hydrolase family 43 β-xylosidase from Geobacillus thermoleovorans IT-08 Appl Biochem Biotech 155 304 313 10.1007/s12010-008-8362-5 1:CAS:528:DC%2BD1MXhtlSisbnN
    • (2009) Appl Biochem Biotech , vol.155 , pp. 304-313
    • Wagschal, K.1    Heng, C.2    Lee, C.C.3    Robertson, G.H.4    Orts, W.J.5    Wong, D.W.6
  • 70
    • 58149172062 scopus 로고    scopus 로고
    • Biochemical characterization of a novel dual-function arabinofuranosidase/xylosidase isolated from a compost starter mixture
    • 10.1007/s00253-008-1662-4 1:CAS:528:DC%2BD1cXhsFart77O
    • K Wagschal C Heng CC Lee DW Wong 2009 Biochemical characterization of a novel dual-function arabinofuranosidase/xylosidase isolated from a compost starter mixture Appl Microbiol Biotechnol 81 855 863 10.1007/s00253-008-1662-4 1:CAS:528:DC%2BD1cXhsFart77O
    • (2009) Appl Microbiol Biotechnol , vol.81 , pp. 855-863
    • Wagschal, K.1    Heng, C.2    Lee, C.C.3    Wong, D.W.4
  • 71
    • 70349765870 scopus 로고    scopus 로고
    • Protein engineering in designing tailored enzymes and microorganisms for biofuels production
    • 10.1016/j.copbio.2009.07.001 1:CAS:528:DC%2BD1MXht1OrtLbJ
    • F Wen NU Nair H Zhao 2009 Protein engineering in designing tailored enzymes and microorganisms for biofuels production Curr Opin Biotechnol 20 412 419 10.1016/j.copbio.2009.07.001 1:CAS:528:DC%2BD1MXht1OrtLbJ
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 412-419
    • Wen, F.1    Nair, N.U.2    Zhao, H.3
  • 73
    • 0034654133 scopus 로고    scopus 로고
    • Nanomolar versus millimolar inhibition by xylobiose-derived azasugars: Significant differences between two structurally distinct xylanases
    • DOI 10.1021/ja993805j
    • JS Williams R Hoos SG Withers 2000 Nanomolar versus millimolar inhibition by xylobiose-derived azasugars: significant differences between two structurally distinct xylanases J Am Chem Soc 122 2223 2234 10.1021/ja993805j 1:CAS:528:DC%2BD3cXht1aiu7c%3D (Pubitemid 30164633)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.10 , pp. 2223-2235
    • Williams, S.J.1    Hoos, R.2    Withers, S.G.3
  • 74
    • 0000345418 scopus 로고    scopus 로고
    • Enzymatic cleavage of glycosides: How does it happen?
    • 10.1351/pac199567101673
    • SG Withers 2001 Enzymatic cleavage of glycosides: how does it happen? Pure Appl Chem 67 1673 1682 10.1351/pac199567101673
    • (2001) Pure Appl Chem , vol.67 , pp. 1673-1682
    • Withers, S.G.1
  • 75
    • 0141568787 scopus 로고    scopus 로고
    • Direct screening of libraries of yeast clones for (α-amylase activity on raw starch hydrolysis
    • DOI 10.2174/0929866033478744
    • DWS Wong SB Batt CC Lee GH Robertson 2003 Direct screening of libraries of yeast clones for α-amylase activity on raw starch hydrolysis Protein Pept Lett 10 459 468 10.2174/0929866033478744 1:CAS:528:DC%2BD3sXnslylsL8%3D (Pubitemid 37143545)
    • (2003) Protein and Peptide Letters , vol.10 , Issue.5 , pp. 459-468
    • Wong, D.W.S.1    Batt, S.B.2    Lee, C.C.3    Robertson, G.H.4
  • 76
    • 16244362031 scopus 로고    scopus 로고
    • High-activity barley α-amylase by directed evolution
    • DOI 10.1007/s10930-004-5221-2
    • DWS Wong SB Batt CC Lee GH Robertson 2004 High-activity barley α-amylase by directed evolution Protein J 23 453 460 10.1007/s10930-004- 5221-2 1:CAS:528:DC%2BD2cXhtVSgurbN (Pubitemid 40485965)
    • (2004) Protein Journal , vol.23 , Issue.7 , pp. 453-460
    • Wong, D.W.S.1    Batt, S.B.2    Lee, C.C.3    Robertson, G.H.4
  • 77
    • 11244345992 scopus 로고    scopus 로고
    • Effects of sugar inhibition on cellulases and β-glucosidase during enzymatic hydrolysis of softwood substrates
    • Z Xiao X Zhang DJ Gregg JN Saddler 2004 Effects of sugar inhibition on cellulases and β-glucosidase during enzymatic hydrolysis of softwood substrates Appl Microbiol Biotechnol 115 1115 1126
    • (2004) Appl Microbiol Biotechnol , vol.115 , pp. 1115-1126
    • Xiao, Z.1    Zhang, X.2    Gregg, D.J.3    Saddler, J.N.4
  • 78
    • 0026337930 scopus 로고
    • Sequence and properties of β-xylosidase from Bacillus pumilus IPO. Contradiction of the previous nucleotide sequence
    • 10.1111/j.1432-1033.1991.tb16490.x 1:CAS:528:DyaK38XmsVOlt7k%3D
    • W-W Xu Y Shima S Negoro I Urabe 1991 Sequence and properties of β-xylosidase from Bacillus pumilus IPO. Contradiction of the previous nucleotide sequence Eur J Biochem 202 1197 1203 10.1111/j.1432-1033.1991. tb16490.x 1:CAS:528:DyaK38XmsVOlt7k%3D
    • (1991) Eur J Biochem , vol.202 , pp. 1197-1203
    • Xu, W.-W.1    Shima, Y.2    Negoro, S.3    Urabe, I.4
  • 79
    • 0030221557 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of a β-amylase gene from Bacillus cereus var. mycoides and characterization of its products
    • 10.1271/bbb.60.1255 1:CAS:528:DyaK28XltlektLo%3D
    • T Yamaguchi Y Matsumoto M Shirakawa M Kibe T Hibino S Kozaki Y Takasaki Y Nitta 1996 Cloning, sequencing, and expression of a β-amylase gene from Bacillus cereus var. mycoides and characterization of its products Biosci Biotechnol Biochem 60 1255 1259 10.1271/bbb.60.1255 1:CAS:528:DyaK28XltlektLo%3D
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 1255-1259
    • Yamaguchi, T.1    Matsumoto, Y.2    Shirakawa, M.3    Kibe, M.4    Hibino, T.5    Kozaki, S.6    Takasaki, Y.7    Nitta, Y.8
  • 80
    • 33645213849 scopus 로고    scopus 로고
    • Breakdown of oligosaccharides by the process of elimination
    • 10.1016/j.cbpa.2006.02.005 1:CAS:528:DC%2BD28XjtFagt7k%3D
    • VL Yip SG Withers 2006 Breakdown of oligosaccharides by the process of elimination Curr Opin Chem Biol 10 147 155 10.1016/j.cbpa.2006.02.005 1:CAS:528:DC%2BD28XjtFagt7k%3D
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 147-155
    • Yip, V.L.1    Withers, S.G.2
  • 81
    • 0028042307 scopus 로고
    • Transfer action of α-d-xylosidases from Aspergillus flavus MO-5 on p-nitrophenyl-α-d-xylopyranoside
    • 10.1271/bbb.58.121 1:CAS:528:DyaK2cXhvVGqtL0%3D
    • K Yoshikawa K Yamamoto S Okada 1994 Transfer action of α-d-xylosidases from Aspergillus flavus MO-5 on p-nitrophenyl-α-d- xylopyranoside Biosci Biotechnol Biochem 58 121 125 10.1271/bbb.58.121 1:CAS:528:DyaK2cXhvVGqtL0%3D
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 121-125
    • Yoshikawa, K.1    Yamamoto, K.2    Okada, S.3
  • 82
  • 83
    • 3142674377 scopus 로고    scopus 로고
    • Purification and biochemical properties of a thermostable xylose-tolerant β-d-xylosidase from Scytalidium thermophilum
    • 10.1007/s10295-004-0129-6 1:CAS:528:DC%2BD2cXltVKmtrc%3D
    • FF Zanoelo MLTM Polizeli HF Terenzi JA Jorge 2004 Purification and biochemical properties of a thermostable xylose-tolerant β-d-xylosidase from Scytalidium thermophilum J Ind Microbiol Biotech 31 170 176 10.1007/s10295-004-0129-6 1:CAS:528:DC%2BD2cXltVKmtrc%3D
    • (2004) J Ind Microbiol Biotech , vol.31 , pp. 170-176
    • Zanoelo, F.F.1    Mltm, P.2    Terenzi, H.F.3    Jorge, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.