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Volumn 4, Issue , 2011, Pages

Xylan oligosaccharides and cellobiohydrolase i (TrCel7A) interaction and effect on activity

Author keywords

binding; biomass degradation; cellobiohydrolase 1; inhibition; isothermal titration calorimetry; TrCel7A; xylan; xylan oligosaccharide

Indexed keywords

BINDING; CELLOBIOHYDROLASES; ISOTHERMAL TITRATION CALORIMETRY; TRCEL7A; XYLAN;

EID: 80054976342     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/1754-6834-4-45     Document Type: Article
Times cited : (47)

References (24)
  • 1
    • 75949110177 scopus 로고    scopus 로고
    • Enzymatic conversion of lignocellulose into fermentable sugars: Challenges and opportunities
    • 10.1002/bbb.4
    • Enzymatic conversion of lignocellulose into fermentable sugars: challenges and opportunities. Jørgensen H, Kristensen JB, Felby C, Biofuels Bioproducts Biorefining 2007 1 119 134 10.1002/bbb.4
    • (2007) Biofuels Bioproducts Biorefining , vol.1 , pp. 119-134
    • Jørgensen, H.1    Kristensen, J.B.2    Felby, C.3
  • 2
    • 10844286172 scopus 로고    scopus 로고
    • Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems
    • DOI 10.1002/bit.20282
    • Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems. Zhang YHP, Lynd LR, Biotechnol Bioeng 2004 88 797 824 10.1002/bit.20282 15538721 (Pubitemid 40003769)
    • (2004) Biotechnology and Bioengineering , vol.88 , Issue.7 , pp. 797-824
    • Zhang, Y.-H.P.1    Lynd, L.R.2
  • 3
    • 9944252948 scopus 로고    scopus 로고
    • Features of promising technologies for pretreatment of lignocellulosic biomass
    • DOI 10.1016/j.biortech.2004.06.025, PII S0960852404002536
    • Features of promising technologies for pretreatment of lignocellulosic biomass. Mosier N, Wyman C, Dale B, Elander R, Lee YY, Holtzapple M, Ladisch M, Bioresour Technol 2005 96 673 686 10.1016/j.biortech.2004.06.025 15588770 (Pubitemid 39592889)
    • (2005) Bioresource Technology , vol.96 , Issue.6 , pp. 673-686
    • Mosier, N.1    Wyman, C.2    Dale, B.3    Elander, R.4    Lee, Y.Y.5    Holtzapple, M.6    Ladisch, M.7
  • 4
    • 58249083377 scopus 로고    scopus 로고
    • Effect of enzyme supplementation at moderate cellulase loadings on initial glucose and xylose release from corn stover solids pretreated by leading technologies
    • 10.1002/bit.22068 18781688
    • Effect of enzyme supplementation at moderate cellulase loadings on initial glucose and xylose release from corn stover solids pretreated by leading technologies. Kumar R, Wyman CE, Biotechnol Bioeng 2009 102 457 467 10.1002/bit.22068 18781688
    • (2009) Biotechnol Bioeng , vol.102 , pp. 457-467
    • Kumar, R.1    Wyman, C.E.2
  • 5
    • 78650708309 scopus 로고    scopus 로고
    • Hydrolysis of different chain length xylooliogmers by cellulase and hemicellulase
    • 10.1016/j.biortech.2010.09.001 20943381
    • Hydrolysis of different chain length xylooliogmers by cellulase and hemicellulase. Qing Q, Wyman CE, Bioresour Technol 2011 102 1359 1366 10.1016/j.biortech.2010.09.001 20943381
    • (2011) Bioresour Technol , vol.102 , pp. 1359-1366
    • Qing, Q.1    Wyman, C.E.2
  • 6
    • 77956177381 scopus 로고    scopus 로고
    • Xylooligomers are strong inhibitors of cellulose hydrolysis by enzymes
    • 10.1016/j.biortech.2010.06.137 20708404
    • Xylooligomers are strong inhibitors of cellulose hydrolysis by enzymes. Qing Q, Yang B, Wyman CE, Bioresour Technol 2010 101 9624 9630 10.1016/j.biortech.2010.06.137 20708404
    • (2010) Bioresour Technol , vol.101 , pp. 9624-9630
    • Qing, Q.1    Yang, B.2    Wyman, C.E.3
  • 7
    • 79959431147 scopus 로고    scopus 로고
    • Supplementation with xylanase and -xylosidase to reduce xylo-oligomer and xylan inhibition of enzymatic hydrolysis of cellulose and pretreated corn stover
    • 10.1186/1754-6834-4-18 21702938
    • Supplementation with xylanase and -xylosidase to reduce xylo-oligomer and xylan inhibition of enzymatic hydrolysis of cellulose and pretreated corn stover. Qing Q, Wyman C, Biotechnol Biofuels 2011 4 18 10.1186/1754-6834-4-18 21702938
    • (2011) Biotechnol Biofuels , vol.4 , pp. 18
    • Qing, Q.1    Wyman, C.2
  • 8
    • 12844278017 scopus 로고    scopus 로고
    • Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as 'burst' kinetics on fluorescent polymeric model substrates
    • DOI 10.1042/BJ20041144
    • Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as 'burst' kinetics on fluorescent polymeric model substrates. Kipper K, Väljamäe P, Johansson G, Biochem J 2005 385 527 535 10.1042/BJ20041144 15362979 (Pubitemid 40165086)
    • (2005) Biochemical Journal , vol.385 , Issue.2 , pp. 527-535
    • Kipper, K.1    Valjamae, P.2    Johansson, G.3
  • 9
    • 79955071381 scopus 로고    scopus 로고
    • A kinetic model for the burst phase of processive cellulases
    • 10.1111/j.1742-4658.2011.08078.x 21371261
    • A kinetic model for the burst phase of processive cellulases. Praestgaard E, Elmerdahl J, Murphy L, Nymand S, McFarland KC, Borch K, Westh P, FEBS J 2011 278 1547 1560 10.1111/j.1742-4658.2011.08078.x 21371261
    • (2011) FEBS J , vol.278 , pp. 1547-1560
    • Praestgaard, E.1    Elmerdahl, J.2    Murphy, L.3    Nymand, S.4    McFarland, K.C.5    Borch, K.6    Westh, P.7
  • 10
    • 0141839655 scopus 로고    scopus 로고
    • Synergistic cellulose hydrolysis can be described in terms of fractal-like kinetics
    • DOI 10.1002/bit.10775
    • Synergistic cellulose hydrolysis can be described in terms of fractal-like kinetics. Väljamäe P, Kipper K, Pettersson G, Johansson G, Biotechnol Bioeng 2003 84 254 257 10.1002/bit.10775 12966583 (Pubitemid 37176338)
    • (2003) Biotechnology and Bioengineering , vol.84 , Issue.2 , pp. 254-257
    • Valjamae, P.1    Kipper, K.2    Pettersson, G.3    Johansson, G.4
  • 11
    • 78650950110 scopus 로고    scopus 로고
    • Processivity of cellobiohydrolases is limited by the substrate
    • 10.1074/jbc.M110.161059 21051539
    • Processivity of cellobiohydrolases is limited by the substrate. Kurasin M, Väljamäe P, J Biol Chem 2011 286 169 177 10.1074/jbc.M110.161059 21051539
    • (2011) J Biol Chem , vol.286 , pp. 169-177
    • Kurasin, M.1    Väljamäe, P.2
  • 13
    • 0027968302 scopus 로고
    • The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei
    • The 3-dimensional crystal structure of the catalytic core of cellobiohydrolase-1 from Trichoderma reesei. Divne C, Ståhlberg J, Reinikainen T, Ruohonen L, Pettersson G, Knowles JKC, Teeri TT, Jones TA, Science 1994 265 524 528 10.1126/science.8036495 8036495 (Pubitemid 24264997)
    • (1994) Science , vol.265 , Issue.5171 , pp. 524-528
    • Divne, C.1    Stahlberg, J.2    Reinikainen, T.3    Ruohonen, L.4    Pettersson, G.5    Knowles, J.K.C.6    Teeri, T.T.7    Jones, T.A.8
  • 15
    • 0021426650 scopus 로고
    • An assay for selective determination of exo-1,4, - Glucanases in a mixture of cellulolytic enzymes
    • 10.1016/0003-2697(84)90843-1 6430117
    • An assay for selective determination of exo-1,4, - glucanases in a mixture of cellulolytic enzymes. Deshpande MV, Eriksson KE, Pettersson LG, Anal Biochem 1984 138 481 487 10.1016/0003-2697(84)90843-1 6430117
    • (1984) Anal Biochem , vol.138 , pp. 481-487
    • Deshpande, M.V.1    Eriksson, K.E.2    Pettersson, L.G.3
  • 16
    • 77955691535 scopus 로고    scopus 로고
    • Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis
    • 10.1002/bit.22779 20506147
    • Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis. Jalak J, Väljamäe P, Biotechnol Bioeng 2010 106 871 883 10.1002/bit.22779 20506147
    • (2010) Biotechnol Bioeng , vol.106 , pp. 871-883
    • Jalak, J.1    Väljamäe, P.2
  • 17
    • 67650472374 scopus 로고    scopus 로고
    • A thermotolerant -glucosidase isolated from an endophytic fungi, Periconia sp., with a possible use for biomass conversion to sugars
    • 10.1016/j.pep.2008.05.022 18602476
    • A thermotolerant -glucosidase isolated from an endophytic fungi, Periconia sp., with a possible use for biomass conversion to sugars. Harnpicharnchai P, Champreda V, Sornlake W, Eurwilaichitr L, Protein Expr Purif 2009 67 61 69 10.1016/j.pep.2008.05.022 18602476
    • (2009) Protein Expr Purif , vol.67 , pp. 61-69
    • Harnpicharnchai, P.1    Champreda, V.2    Sornlake, W.3    Eurwilaichitr, L.4
  • 18
    • 43249094258 scopus 로고    scopus 로고
    • Purification and characterization of thermostable β-glucosidase from the brown-rot basidiomycete Fomitopsis palustris grown on microcrystalline cellulose
    • DOI 10.1007/s12275-007-0230-4
    • Purification and characterization of thermostable -glucosidase from the brown-rot basidiomycete Fomitopsis palustris grown on microcrystalline cellulose. Yoon JJ, Kim KY, Cha CJ, J Microbiol 2008 46 51 55 10.1007/s12275-007-0230-4 18337693 (Pubitemid 351928074)
    • (2008) Journal of Microbiology , vol.46 , Issue.1 , pp. 51-55
    • Yoon, J.-J.1    Kim, K.-Y.2    Cha, C.-J.3
  • 19
    • 7644238142 scopus 로고    scopus 로고
    • β-Glucosidase activity from the thermophilic fungus Scytalidium thermophilum is stimulated by glucose and xylose
    • DOI 10.1016/j.femsle.2004.09.021, PII S0378109704006846
    • -glucosidase activity from the thermophilic fungus Scytalidium thermophilum is stimulated by glucose and xylose. Zanoelo FF, Polizeli M, Terenzi HF, Jorge JA, FEMS Microbiol Lett 2004 240 137 143 10.1016/j.femsle. 2004.09.021 15522500 (Pubitemid 39457717)
    • (2004) FEMS Microbiology Letters , vol.240 , Issue.2 , pp. 137-143
    • Zanoelo, F.F.1    Polizeli, M.2    Terenzi, H.F.3    Jorge, J.A.4
  • 20
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: New insight into the function of cellobiohydrolases
    • DOI 10.1016/S0167-7799(97)01032-9, PII S0167779997010329
    • Crystalline cellulose degradation: new insight into the function of cellobiohydrolases. Teeri TT, Trends Biotechnol 1997 15 160 167 10.1016/S0167-7799(97)01032-9 (Pubitemid 27219573)
    • (1997) Trends in Biotechnology , vol.15 , Issue.5 , pp. 160-167
    • Teeri, T.T.1
  • 21
    • 2542418037 scopus 로고    scopus 로고
    • Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate
    • DOI 10.1002/bit.10838
    • Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate. Gruno M, Väljamäe P, Pettersson G, Johansson G, Biotechnol Bioeng 2004 86 503 511 10.1002/bit.10838 15129433 (Pubitemid 38679768)
    • (2004) Biotechnology and Bioengineering , vol.86 , Issue.5 , pp. 503-511
    • Gruno, M.1    Valjamae, P.2    Pettersson, G.3    Johansson, G.4
  • 22
    • 0036723835 scopus 로고    scopus 로고
    • Synergistic effects on crystalline cellulose degradation between cellulosomal cellulases from Clostridium cellulovorans
    • DOI 10.1128/JB.184.18.5088-5095.2002
    • Synergistic effects on crystalline cellulose degradation between cellulosomal cellulases from Clostridium cellulovorans. Murashima K, Kosugi A, Doi RH, J Bacteriol 2002 184 5088 5095 10.1128/JB.184.18.5088-5095.2002 12193625 (Pubitemid 34971034)
    • (2002) Journal of Bacteriology , vol.184 , Issue.18 , pp. 5088-5095
    • Murashima, K.1    Kosugi, A.2    Doi, R.H.3
  • 23
    • 41849103104 scopus 로고    scopus 로고
    • Synergistic enhancement of cellobiohydrolase performance on pretreated corn stover by addition of xylanase and esterase activities
    • DOI 10.1016/j.biortech.2007.09.064, PII S0960852407008115
    • Synergistic enhancement of cellobiohydrolase performance on pretreated corn stover by addition of xylanase and esterase activities. Selig MJ, Knoshaug EP, Adney WS, Himmel ME, Decker SR, Bioresour Technol 2008 99 4997 5005 10.1016/j.biortech.2007.09.064 18006303 (Pubitemid 351503850)
    • (2008) Bioresource Technology , vol.99 , Issue.11 , pp. 4997-5005
    • Selig, M.J.1    Knoshaug, E.P.2    Adney, W.S.3    Himmel, M.E.4    Decker, S.R.5
  • 24
    • 78651363174 scopus 로고    scopus 로고
    • Advantages of isothermal titration calorimetry for xylanase kinetics in comparison to chemical-reducing-end assays
    • Advantages of isothermal titration calorimetry for xylanase kinetics in comparison to chemical-reducing-end assays. Baumann MJ, Murphy L, Lei N, Krogh KB, Borch K, Westh P, Anal Biochem 410 19 26
    • Anal Biochem , vol.410 , pp. 19-26
    • Baumann, M.J.1    Murphy, L.2    Lei, N.3    Krogh, K.B.4    Borch, K.5    Westh, P.6


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