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Volumn 510, Issue , 2012, Pages 429-452

Designer cellulosomes for enhanced hydrolysis of cellulosic substrates

Author keywords

Carbohydrate binding module (CBM); Chimeric enzyme; Chimeric scaffoldin; Cohesin; Designer cellulosomes; Dockerin

Indexed keywords

CELLOBIOSE; CELLULASE; CELLULOSE 1,4 BETA CELLOBIOSIDASE; CELLULOSOME; COHESIN; DOCKERIN; GENOMIC DNA; GLUCAN SYNTHASE; GLUCOSE; MEMBRANE PROTEIN; REAGENT; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84861168059     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-415931-0.00023-9     Document Type: Chapter
Times cited : (48)

References (28)
  • 1
    • 11244334206 scopus 로고
    • Maximizing the formation of glucose in the enzymatic hydrolysis of insoluble cellulose
    • J.A. Asenjo Maximizing the formation of glucose in the enzymatic hydrolysis of insoluble cellulose Biotechnol. Bioeng. 25 1983 3185 3190
    • (1983) Biotechnol. Bioeng. , vol.25 , pp. 3185-3190
    • Asenjo, J.A.1
  • 2
    • 27744458385 scopus 로고    scopus 로고
    • Matching fusion-protein systems for affinity analysis of two interacting families of proteins: The cohesin-dockerin interaction
    • Y. Barak, T. Handelsman, D. Nakar, A. Mechaly, R. Lamed, Y. Shoham, and E.A. Bayer Matching fusion-protein systems for affinity analysis of two interacting families of proteins: The cohesin-dockerin interaction J. Mol. Recognit. 18 2005 491 501
    • (2005) J. Mol. Recognit. , vol.18 , pp. 491-501
    • Barak, Y.1    Handelsman, T.2    Nakar, D.3    Mechaly, A.4    Lamed, R.5    Shoham, Y.6    Bayer, E.A.7
  • 3
    • 0027984011 scopus 로고
    • The cellulosome - A treasure-trove for biotechnology
    • E.A. Bayer, E. Morag, and R. Lamed The cellulosome - A treasure-trove for biotechnology Trends Biotechnol. 12 1994 378 386
    • (1994) Trends Biotechnol. , vol.12 , pp. 378-386
    • Bayer, E.A.1    Morag, E.2    Lamed, R.3
  • 6
    • 47249125226 scopus 로고    scopus 로고
    • Conversion of noncellulosomal Thermobifida fusca free exoglucanases into cellulosomal components: Comparative impact on cellulose-degrading activity
    • J. Caspi, D. Irwin, R. Lamed, H.-P. Fierobe, D.B. Wilson, and E.A. Bayer Conversion of noncellulosomal Thermobifida fusca free exoglucanases into cellulosomal components: Comparative impact on cellulose-degrading activity J. Biotechnol. 135 2008 351 357
    • (2008) J. Biotechnol. , vol.135 , pp. 351-357
    • Caspi, J.1    Irwin, D.2    Lamed, R.3    Fierobe, H.-P.4    Wilson, D.B.5    Bayer, E.A.6
  • 7
    • 72949119336 scopus 로고    scopus 로고
    • Effect of linker length and dockerin position on conversion of a Thermobifida fusca endoglucanase to the cellulosomal mode
    • J. Caspi, Y. Barak, R. Haimovitz, D. Irwin, R. Lamed, D.B. Wilson, and E.A. Bayer Effect of linker length and dockerin position on conversion of a Thermobifida fusca endoglucanase to the cellulosomal mode Appl. Environ. Microbiol. 75 2009 7335 7342
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 7335-7342
    • Caspi, J.1    Barak, Y.2    Haimovitz, R.3    Irwin, D.4    Lamed, R.5    Wilson, D.B.6    Bayer, E.A.7
  • 8
    • 77958497861 scopus 로고    scopus 로고
    • Thermobifida fusca exoglucanase Cel6B is incompatible with the cellulosomal mode in contrast to endoglucanase Cel6A
    • J. Caspi, Y. Barak, R. Haimovitz, H. Gilary, D. Irwin, R. Lamed, D.B. Wilson, and E.A. Bayer Thermobifida fusca exoglucanase Cel6B is incompatible with the cellulosomal mode in contrast to endoglucanase Cel6A Syst. Synth. Biol. 4 2010 193 201
    • (2010) Syst. Synth. Biol. , vol.4 , pp. 193-201
    • Caspi, J.1    Barak, Y.2    Haimovitz, R.3    Gilary, H.4    Irwin, D.5    Lamed, R.6    Wilson, D.B.7    Bayer, E.A.8
  • 9
    • 0035877619 scopus 로고    scopus 로고
    • Design and production of active cellulosome chimeras: Selective incorporation of dockerin-containing enzymes into defined functional complexes
    • H.-P. Fierobe, A. Mechaly, C. Tardif, A. Belaich, R. Lamed, Y. Shoham, J.-P. Belaich, and E.A. Bayer Design and production of active cellulosome chimeras: Selective incorporation of dockerin-containing enzymes into defined functional complexes J. Biol. Chem. 276 2001 21257 21261
    • (2001) J. Biol. Chem. , vol.276 , pp. 21257-21261
    • Fierobe, H.-P.1    Mechaly, A.2    Tardif, C.3    Belaich, A.4    Lamed, R.5    Shoham, Y.6    Belaich, J.-P.7    Bayer, E.A.8
  • 10
    • 0038382757 scopus 로고    scopus 로고
    • Designer nanosomes: Selective engineering of dockerin-containing enzymes into chimeric scaffoldins to form defined nanoreactors
    • T.T. Teeri, B. Svensson, H.J. Gilbert, T. Feizi, The Royal Society of Chemistry Cambridge
    • H.-P. Fierobe, A. Mechaly, C. Tardif, A. Belaich, R. Lamed, Y. Shoham, J.-P. Belaich, and E.A. Bayer Designer nanosomes: Selective engineering of dockerin-containing enzymes into chimeric scaffoldins to form defined nanoreactors T.T. Teeri, B. Svensson, H.J. Gilbert, T. Feizi, Carbohydrate Bioengineering: Interdisciplinary Approaches 2002 The Royal Society of Chemistry Cambridge 113 123
    • (2002) Carbohydrate Bioengineering: Interdisciplinary Approaches , pp. 113-123
    • Fierobe, H.-P.1    Mechaly, A.2    Tardif, C.3    Belaich, A.4    Lamed, R.5    Shoham, Y.6    Belaich, J.-P.7    Bayer, E.A.8
  • 11
    • 20944438012 scopus 로고    scopus 로고
    • Action of designer cellulosomes on homogeneous versus complex substrates: Controlled incorporation of three distinct enzymes into a defined tri-functional scaffoldin
    • H.-P. Fierobe, F. Mingardon, A. Mechaly, A. Belaich, M.T. Rincon, R. Lamed, C. Tardif, J.-P. Belaich, and E.A. Bayer Action of designer cellulosomes on homogeneous versus complex substrates: Controlled incorporation of three distinct enzymes into a defined tri-functional scaffoldin J. Biol. Chem. 280 2005 16325 16334
    • (2005) J. Biol. Chem. , vol.280 , pp. 16325-16334
    • Fierobe, H.-P.1    Mingardon, F.2    Mechaly, A.3    Belaich, A.4    Rincon, M.T.5    Lamed, R.6    Tardif, C.7    Belaich, J.-P.8    Bayer, E.A.9
  • 12
    • 84943470296 scopus 로고
    • Measurements of cellulase activity
    • T.K. Ghose Measurements of cellulase activity Pure Appl. Chem. 59 1987 257 268
    • (1987) Pure Appl. Chem. , vol.59 , pp. 257-268
    • Ghose, T.K.1
  • 13
    • 41149118473 scopus 로고    scopus 로고
    • Cohesin-dockerin microarray: Diverse specificities between two complementary families of interacting protein modules
    • R. Haimovitz, Y. Barak, E. Morag, M. Voronov-Goldman, R. Lamed, and E.A. Bayer Cohesin-dockerin microarray: Diverse specificities between two complementary families of interacting protein modules Proteomics 8 2008 968 979
    • (2008) Proteomics , vol.8 , pp. 968-979
    • Haimovitz, R.1    Barak, Y.2    Morag, E.3    Voronov-Goldman, M.4    Lamed, R.5    Bayer, E.A.6
  • 14
    • 0021796320 scopus 로고
    • Major characteristics of the cellulolytic system of Clostridium thermocellum coincide with those of the purified cellulosome
    • R. Lamed, R. Kenig, E. Setter, and E.A. Bayer Major characteristics of the cellulolytic system of Clostridium thermocellum coincide with those of the purified cellulosome Enzyme Microb. Technol. 7 1985 37 41
    • (1985) Enzyme Microb. Technol. , vol.7 , pp. 37-41
    • Lamed, R.1    Kenig, R.2    Setter, E.3    Bayer, E.A.4
  • 15
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • G.L. Miller Use of dinitrosalicylic acid reagent for determination of reducing sugar Anal. Biochem. 31 1959 426 428
    • (1959) Anal. Biochem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 16
    • 34250878420 scopus 로고    scopus 로고
    • Incorporation of fungal cellulases in bacterial minicellulosomes yields viable, synergistically acting cellulolytic complexes
    • F. Mingardon, A. Chanal, A.M. López-Contreras, C. Dray, E.A. Bayer, and H.-P. Fierobe Incorporation of fungal cellulases in bacterial minicellulosomes yields viable, synergistically acting cellulolytic complexes Appl. Environ. Microbiol. 73 2007 3822 3832
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 3822-3832
    • Mingardon, F.1    Chanal, A.2    López-Contreras, A.M.3    Dray, C.4    Bayer, E.A.5    Fierobe, H.-P.6
  • 18
    • 79952167181 scopus 로고    scopus 로고
    • Cellulase-xylanase synergy in designer cellulosomes for enhanced degradation of a complex cellulosic substrate
    • S. Moraïs, Y. Barak, J. Caspi, Y. Hadar, R. Lamed, Y. Shoham, D.B. Wilson, and E.A. Bayer Cellulase-xylanase synergy in designer cellulosomes for enhanced degradation of a complex cellulosic substrate MBio 1 2010 e00285 e00310
    • (2010) MBio , vol.1
    • Moraïs, S.1    Barak, Y.2    Caspi, J.3    Hadar, Y.4    Lamed, R.5    Shoham, Y.6    Wilson, D.B.7    Bayer, E.A.8
  • 19
    • 77953636504 scopus 로고    scopus 로고
    • Contribution of a xylan-binding module to the degradation of a complex cellulosic substrate by designer cellulosomes
    • S. Moraïs, Y. Barak, J. Caspi, Y. Hadar, R. Lamed, Y. Shoham, D.B. Wilson, and E.A. Bayer Contribution of a xylan-binding module to the degradation of a complex cellulosic substrate by designer cellulosomes Appl. Environ. Microbiol. 76 2010 3787 3796
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 3787-3796
    • Moraïs, S.1    Barak, Y.2    Caspi, J.3    Hadar, Y.4    Lamed, R.5    Shoham, Y.6    Wilson, D.B.7    Bayer, E.A.8
  • 20
    • 0031569395 scopus 로고    scopus 로고
    • A cohesin domain from Clostridium thermocellum: The crystal structure provides new insights into cellulosome assembly
    • L.J.W. Shimon, E.A. Bayer, E. Morag, R. Lamed, S. Yaron, Y. Shoham, and F. Frolow A cohesin domain from Clostridium thermocellum: The crystal structure provides new insights into cellulosome assembly Structure 5 1997 381 390
    • (1997) Structure , vol.5 , pp. 381-390
    • Shimon, L.J.W.1    Bayer, E.A.2    Morag, E.3    Lamed, R.4    Yaron, S.5    Shoham, Y.6    Frolow, F.7
  • 21
    • 0034711422 scopus 로고    scopus 로고
    • Crystal structure of a cohesin module from Clostridium cellulolyticum: Implications for dockerin recognition
    • S. Spinelli, H.P. Fierobe, A. Belaich, J.P. Belaich, B. Henrissat, and C. Cambillau Crystal structure of a cohesin module from Clostridium cellulolyticum: Implications for dockerin recognition J. Mol. Biol. 304 2000 189 200
    • (2000) J. Mol. Biol. , vol.304 , pp. 189-200
    • Spinelli, S.1    Fierobe, H.P.2    Belaich, A.3    Belaich, J.P.4    Henrissat, B.5    Cambillau, C.6
  • 22
    • 33745194828 scopus 로고    scopus 로고
    • Enzymatic saccharification of wheat straw for bioethanol production by a combined cellulase xylanase and feruloyl esterase treatment
    • M.G. Tabka, I. Herpoël-Gimbert, F. Monod, M. Asther, and J.C. Sigoillot Enzymatic saccharification of wheat straw for bioethanol production by a combined cellulase xylanase and feruloyl esterase treatment Enzyme Microb. Technol. 39 2006 897 902
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 897-902
    • Tabka, M.G.1    Herpoël-Gimbert, I.2    Monod, F.3    Asther, M.4    Sigoillot, J.C.5
  • 23
    • 0031592929 scopus 로고    scopus 로고
    • The crystal structure of a type i cohesin domain at 1.7 Å resolution
    • G.A. Tavares, P. Béguin, and P.M. Alzari The crystal structure of a type I cohesin domain at 1.7 Å resolution J. Mol. Biol. 273 1997 701 713
    • (1997) J. Mol. Biol. , vol.273 , pp. 701-713
    • Tavares, G.A.1    Béguin, P.2    Alzari, P.M.3
  • 24
    • 0034307779 scopus 로고    scopus 로고
    • Affinity electrophoresis for the identification and characterization of soluble sugar binding by carbohydrate-binding modules
    • P. Tomme, A. Boraston, J.M. Kormos, R.A. Warren, and D.G. Kilburn Affinity electrophoresis for the identification and characterization of soluble sugar binding by carbohydrate-binding modules Enzyme Microb. Technol. 27 2000 453 458
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 453-458
    • Tomme, P.1    Boraston, A.2    Kormos, J.M.3    Warren, R.A.4    Kilburn, D.G.5
  • 25
    • 77952267292 scopus 로고    scopus 로고
    • Interplay between Clostridium thermocellum family-48 and family-9 cellulases in the cellulosomal versus non-cellulosomal states
    • Y. Vazana, S. Moraïs, Y. Barak, R. Lamed, and E.A. Bayer Interplay between Clostridium thermocellum family-48 and family-9 cellulases in the cellulosomal versus non-cellulosomal states Appl. Environ. Microbiol. 76 2010 3236 3243
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 3236-3243
    • Vazana, Y.1    Moraïs, S.2    Barak, Y.3    Lamed, R.4    Bayer, E.A.5
  • 26
    • 77957034698 scopus 로고
    • Methods for measuring cellulases activities
    • T.M. Wood, and K.M. Bhat Methods for measuring cellulases activities Methods Enzymol. 160 1988 87 112
    • (1988) Methods Enzymol. , vol.160 , pp. 87-112
    • Wood, T.M.1    Bhat, K.M.2
  • 27
    • 79960216783 scopus 로고    scopus 로고
    • Substrate channeling and enzyme complexes for biotechnological applications
    • Y.H. Zhang Substrate channeling and enzyme complexes for biotechnological applications Biotechnol. Adv. 29 2011 715 725
    • (2011) Biotechnol. Adv. , vol.29 , pp. 715-725
    • Zhang, Y.H.1
  • 28
    • 0033230682 scopus 로고    scopus 로고
    • Substrate heterogeneity causes the nonlinear kinetics of insoluble cellulose hydrolysis
    • S. Zhang, D.E. Wolfgang, and D.B. Wilson Substrate heterogeneity causes the nonlinear kinetics of insoluble cellulose hydrolysis Biotechnol. Bioeng. 66 1999 35 41
    • (1999) Biotechnol. Bioeng. , vol.66 , pp. 35-41
    • Zhang, S.1    Wolfgang, D.E.2    Wilson, D.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.