메뉴 건너뛰기




Volumn 29, Issue 48, 2013, Pages 14997-15005

Direct in situ observation of synergism between cellulolytic enzymes during the biodegradation of crystalline cellulose fibers

Author keywords

[No Author keywords available]

Indexed keywords

AMORPHOUS CELLULOSE; CELLOBIOHYDROLASES; CELLULOLYTIC ENZYME; CRYSTALLINE CELLULOSE; DEGRADATION EFFECT; DIRECT VISUALIZATION; IN-SITU OBSERVATIONS; SYNERGISTIC EFFECT;

EID: 84888985503     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la403401c     Document Type: Article
Times cited : (27)

References (40)
  • 4
    • 20444400628 scopus 로고    scopus 로고
    • Cellulose fascinating niopolymer and sustainable raw material
    • Klemm, D.; Heublein, B.; Fink, H.-P.; Bohn, A. Cellulose fascinating niopolymer and sustainable raw material Angew. Chem., Int. Ed. 2005, 44, 3358-3393
    • (2005) Angew. Chem., Int. Ed. , vol.44 , pp. 3358-3393
    • Klemm, D.1    Heublein, B.2    Fink, H.-P.3    Bohn, A.4
  • 5
    • 84055221845 scopus 로고    scopus 로고
    • Synergistic interactions in cellulose hydrolysis
    • Kostylev, M.; Wilson, D. Synergistic interactions in cellulose hydrolysis Biofuels 2012, 3, 61-70
    • (2012) Biofuels , vol.3 , pp. 61-70
    • Kostylev, M.1    Wilson, D.2
  • 6
    • 84862900169 scopus 로고    scopus 로고
    • Real-time observation of the swelling and hydrolysis of a single crystalline cellulose fiber catalyzed by cellulase 7B from Trichoderma reesei
    • Wang, J.; Quirk, A.; Lipkowski, J.; Dutcher, J. R.; Hill, C.; Mark, A.; Clarke, A. J. Real-time observation of the swelling and hydrolysis of a single crystalline cellulose fiber catalyzed by cellulase 7B from Trichoderma reesei Langmuir 2012, 28, 9664-9672
    • (2012) Langmuir , vol.28 , pp. 9664-9672
    • Wang, J.1    Quirk, A.2    Lipkowski, J.3    Dutcher, J.R.4    Hill, C.5    Mark, A.6    Clarke, A.J.7
  • 7
    • 77950573367 scopus 로고    scopus 로고
    • Direct visualization of the enzymatic digestion of a single fiber of native cellulose in an aqueous environment by atomic force microscopy
    • Quirk, A.; Lipkowski, J.; Vandenende, C.; Cockburn, D.; Clarke, A. J.; Dutcher, J. R.; Roscoe, S. G. Direct visualization of the enzymatic digestion of a single fiber of native cellulose in an aqueous environment by atomic force microscopy Langmuir 2010, 26, 5007-5013
    • (2010) Langmuir , vol.26 , pp. 5007-5013
    • Quirk, A.1    Lipkowski, J.2    Vandenende, C.3    Cockburn, D.4    Clarke, A.J.5    Dutcher, J.R.6    Roscoe, S.G.7
  • 8
    • 84855228527 scopus 로고    scopus 로고
    • Trichoderma reesei RUT-C30 - Thirty years of strain improvement
    • Peterson, R.; Nevalainen, H. Trichoderma reesei RUT-C30 - thirty years of strain improvement Microbiology 2012, 158, 58-68
    • (2012) Microbiology , vol.158 , pp. 58-68
    • Peterson, R.1    Nevalainen, H.2
  • 10
    • 0027372765 scopus 로고
    • Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase i in its interaction with crystalline cellulose
    • Srisodsuk, M.; Reinikainen, T.; Penttila, M.; Teeri, T. T. Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase I in its interaction with crystalline cellulose J. Biol. Chem. 1993, 268, 20756-20761
    • (1993) J. Biol. Chem. , vol.268 , pp. 20756-20761
    • Srisodsuk, M.1    Reinikainen, T.2    Penttila, M.3    Teeri, T.T.4
  • 11
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules. Fine tuning polysaccharide recognition
    • Boraston, A. B.; Bolam, D. N.; Gilbert, H. J.; Davies, G. J. Carbohydrate-binding modules. Fine tuning polysaccharide recognition Biochem. J. 2004, 382, 769-781
    • (2004) Biochem. J. , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 12
    • 0345676498 scopus 로고    scopus 로고
    • High resolution crystal structures reveal how a cellulose chain is bound in the 50-Å-long tunnel of cellobiohydrolase i from Trichoderma reesei
    • Divne, C.; StaÌŠhlberg, J.; Teeri, T. T.; Jones, T. A. High resolution crystal structures reveal how a cellulose chain is bound in the 50-Å-long tunnel of cellobiohydrolase I from Trichoderma reesei J. Mol. Biol. 1998, 275, 309-325
    • (1998) J. Mol. Biol. , vol.275 , pp. 309-325
    • Divne, C.1    Staìšhlberg, J.2    Teeri, T.T.3    Jones, T.A.4
  • 14
    • 77950356429 scopus 로고    scopus 로고
    • Access to cellulose limits the efficiency of enzymatic hydrolysis the role of amorphogenesis
    • Arantes, V.; Saddler, J. N. Access to cellulose limits the efficiency of enzymatic hydrolysis the role of amorphogenesis Biotechnol. Biofuels 2010, 3, 4
    • (2010) Biotechnol. Biofuels , vol.3 , pp. 4
    • Arantes, V.1    Saddler, J.N.2
  • 15
    • 0015377366 scopus 로고
    • The purification and properties of the C1 component of Trichoderma koningii cellulase
    • Wood, T. M.; McCrae, S. I. The purification and properties of the C1 component of Trichoderma koningii cellulase Biochem. J. 1972, 128, 1183-1192
    • (1972) Biochem. J. , vol.128 , pp. 1183-1192
    • Wood, T.M.1    McCrae, S.I.2
  • 16
    • 84865224370 scopus 로고    scopus 로고
    • Endo-exo synergism in cellulose hydrolysis revisited
    • Jalak, J.; Kurasin, M.; Teugjas, H.; Valjamae, P. Endo-exo synergism in cellulose hydrolysis revisited J. Biol. Chem. 2012, 287, 28802-28815
    • (2012) J. Biol. Chem. , vol.287 , pp. 28802-28815
    • Jalak, J.1    Kurasin, M.2    Teugjas, H.3    Valjamae, P.4
  • 17
    • 84954875039 scopus 로고
    • The 1,4-β-glucan cellobiohydrolases of Trichoderma reesei QM 9414. A new type of cellulolytic synergism
    • Fagerstam, L. G.; Pettersson, L. G. The 1,4-β-glucan cellobiohydrolases of Trichoderma reesei QM 9414. A new type of cellulolytic synergism FEBS Lett. 1980, 119, 97-100
    • (1980) FEBS Lett. , vol.119 , pp. 97-100
    • Fagerstam, L.G.1    Pettersson, L.G.2
  • 19
    • 0034029116 scopus 로고    scopus 로고
    • Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A
    • Boisset, C.; Fraschini, C.; Schulein, M.; Henrissat, B.; Chanzy, H. Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A Appl. Environ. Microbiol. 2000, 66, 1444-1452
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1444-1452
    • Boisset, C.1    Fraschini, C.2    Schulein, M.3    Henrissat, B.4    Chanzy, H.5
  • 20
    • 0033556286 scopus 로고    scopus 로고
    • Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution
    • Varrot, A.; Hastrup, S.; Schülein, M.; Davies, G. J. Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution Biochem. J. 1999, 337, 297-304
    • (1999) Biochem. J. , vol.337 , pp. 297-304
    • Varrot, A.1    Hastrup, S.2    Schülein, M.3    Davies, G.J.4
  • 21
    • 33244486953 scopus 로고    scopus 로고
    • The maize primary cell wall microfibril: A new model derived from direct visualization
    • Ding, S.-Y.; Himmel, M. E. The maize primary cell wall microfibril: a new model derived from direct visualization J. Agric. Food Chem. 2006, 54, 597-606
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 597-606
    • Ding, S.-Y.1    Himmel, M.E.2
  • 23
    • 0031194861 scopus 로고    scopus 로고
    • High-resolution atomic force microscopy of native Valonia cellulose i microcrystals
    • Baker, A. A.; Helbert, W.; Sugiyama, J.; Miles, M. J. High-resolution atomic force microscopy of native Valonia cellulose I microcrystals J. Struct. Biol. 1997, 119, 129-138
    • (1997) J. Struct. Biol. , vol.119 , pp. 129-138
    • Baker, A.A.1    Helbert, W.2    Sugiyama, J.3    Miles, M.J.4
  • 26
    • 84871553240 scopus 로고    scopus 로고
    • Dissecting and reconstructing synergism. in situ visualization of cooperativity among cellulases
    • Ganner, T.; Bubner, P.; Elbinger, M.; Mayrhofer, C.; Plank, H.; Nidetzky, B. Dissecting and reconstructing synergism. In situ visualization of cooperativity among cellulases J. Biol. Chem. 2012, 287, 43215-43222
    • (2012) J. Biol. Chem. , vol.287 , pp. 43215-43222
    • Ganner, T.1    Bubner, P.2    Elbinger, M.3    Mayrhofer, C.4    Plank, H.5    Nidetzky, B.6
  • 27
    • 84869854102 scopus 로고    scopus 로고
    • How does plant cell wall nanoscale architecture correlate with enzymatic digestibility?
    • Ding, S.-Y.; Liu, Y.-S.; Zeng, Y.; Himmel, M. E.; Baker, J. O.; Bayer, E. A. How does plant cell wall nanoscale architecture correlate with enzymatic digestibility? Science 2012, 338, 1055-1060
    • (2012) Science , vol.338 , pp. 1055-1060
    • Ding, S.-Y.1    Liu, Y.-S.2    Zeng, Y.3    Himmel, M.E.4    Baker, J.O.5    Bayer, E.A.6
  • 28
    • 0021668869 scopus 로고
    • Isolation of cellulolytic enzymes from Trichoderma reesei QM 9414
    • Bhikhabhai, R.; Johansson, G.; Pettersson, G. Isolation of cellulolytic enzymes from Trichoderma reesei QM 9414 J. Appl. Biochem. 1984, 6, 336-345
    • (1984) J. Appl. Biochem. , vol.6 , pp. 336-345
    • Bhikhabhai, R.1    Johansson, G.2    Pettersson, G.3
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye ninding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye ninding Anal. Biochem. 1976, 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 1970, 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0021971721 scopus 로고
    • Use of monoclonal antibodies to analyse the expression of a multi-yublin family
    • Birkett, C. R.; Foster, K. E.; Johnson, L.; Gull, K. Use of monoclonal antibodies to analyse the expression of a multi-yublin family FEBS Lett. 1985, 187, 211-218
    • (1985) FEBS Lett. , vol.187 , pp. 211-218
    • Birkett, C.R.1    Foster, K.E.2    Johnson, L.3    Gull, K.4
  • 32
    • 77955576397 scopus 로고    scopus 로고
    • Molecular-scale investigations of cellulose microstructure during enzymatic hydrolysis
    • Santa-Maria, M.; Jeoh, T. Molecular-scale investigations of cellulose microstructure during enzymatic hydrolysis Biomacromolecules 2010, 11, 2000-2007
    • (2010) Biomacromolecules , vol.11 , pp. 2000-2007
    • Santa-Maria, M.1    Jeoh, T.2
  • 33
    • 79953223700 scopus 로고    scopus 로고
    • Single molecule study of cellulase hydrolysis of crystalline cellulose
    • Liu, Y.-S.; Baker, J. O.; Zeng, Y.; Himmel, M. E.; Haas, T.; Ding, S.-Y. Single molecule study of cellulase hydrolysis of crystalline cellulose J. Biol. Chem. 2011, 286, 11195-11201
    • (2011) J. Biol. Chem. , vol.286 , pp. 11195-11201
    • Liu, Y.-S.1    Baker, J.O.2    Zeng, Y.3    Himmel, M.E.4    Haas, T.5    Ding, S.-Y.6
  • 36
    • 0036233797 scopus 로고    scopus 로고
    • A model explaining declining rate in hydrolysis of lignocellulose substrates with cellobiohydrolase i (Cel7A) and endoglucanase i (Cel7B) of Trichoderma reesei
    • Eriksson, T.; Karlsson, J.; Tjerneld, F. A model explaining declining rate in hydrolysis of lignocellulose substrates with cellobiohydrolase I (Cel7A) and endoglucanase I (Cel7B) of Trichoderma reesei Appl. Biochem. Biotechnol. 2002, 101, 41-60
    • (2002) Appl. Biochem. Biotechnol. , vol.101 , pp. 41-60
    • Eriksson, T.1    Karlsson, J.2    Tjerneld, F.3
  • 37
    • 0033485705 scopus 로고    scopus 로고
    • Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase i and endoglucanase i
    • Valjamae, P.; Sild, V.; Nutt, A.; Pettersson, G.; Johansson, G. Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I Eur. J. Biochem. 1999, 266, 327-334
    • (1999) Eur. J. Biochem. , vol.266 , pp. 327-334
    • Valjamae, P.1    Sild, V.2    Nutt, A.3    Pettersson, G.4    Johansson, G.5
  • 38
    • 0027651651 scopus 로고
    • Activity studies of eight purified cellulases. Specificity, synergism, and binding domain effects
    • Irwin, D. C.; Spezio, M.; Walker, L. P.; Wilson, D. B. Activity studies of eight purified cellulases. Specificity, synergism, and binding domain effects Biotechnol. Bioeng. 1993, 42, 1002-1013
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 1002-1013
    • Irwin, D.C.1    Spezio, M.2    Walker, L.P.3    Wilson, D.B.4
  • 39
    • 0030065736 scopus 로고    scopus 로고
    • Identification of two functionally different classes of exocellulases
    • Barr, B. K.; Hsieh, Y.-L.; Ganem, B.; Wilson, D. B. Identification of two functionally different classes of exocellulases Biochemistry 1996, 35, 586-592
    • (1996) Biochemistry , vol.35 , pp. 586-592
    • Barr, B.K.1    Hsieh, Y.-L.2    Ganem, B.3    Wilson, D.B.4
  • 40
    • 0031666637 scopus 로고    scopus 로고
    • Unidirectional processive action of cellobiohydrolase Cel7a on Valonia cellulose microcrystals
    • Imai, T.; Boisset, C.; Samejima, M.; Igarashi, K.; Sugiyama, J. Unidirectional processive action of cellobiohydrolase Cel7a on Valonia cellulose microcrystals FEBS Lett. 1998, 432, 113-116
    • (1998) FEBS Lett. , vol.432 , pp. 113-116
    • Imai, T.1    Boisset, C.2    Samejima, M.3    Igarashi, K.4    Sugiyama, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.