메뉴 건너뛰기




Volumn 9, Issue 1, 2016, Pages

Production of a functional cell wall-anchored minicellulosome by recombinant Clostridium acetobutylicum ATCC 824

Author keywords

Cellulosome; Clostridium acetobutylicum; Consolidated bioprocessing; Scaffoldin; Sortase anchoring

Indexed keywords

BIOLOGY; CELL MEMBRANES; CELLULOSE; CLOSTRIDIUM; ENZYMES; FERMENTATION; FOSSIL FUELS; GENES; GLOBAL WARMING; LIGNIN; STRAIN;

EID: 84969785089     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/s13068-016-0526-x     Document Type: Article
Times cited : (33)

References (91)
  • 1
  • 2
    • 72049131519 scopus 로고    scopus 로고
    • Production of first and second generation biofuels: A comprehensive review
    • 1:CAS:528:DC%2BD1MXhsF2isbvF
    • Naik S, Goud VV, Rout PK, Dalai AK. Production of first and second generation biofuels: a comprehensive review. Renew Sust Energ Rev. 2010;14(2):578-97.
    • (2010) Renew Sust Energ Rev , vol.14 , Issue.2 , pp. 578-597
    • Naik, S.1    Goud, V.V.2    Rout, P.K.3    Dalai, A.K.4
  • 3
    • 84863782747 scopus 로고    scopus 로고
    • Biomass recalcitrance. Part I: The chemical compositions and physical structures affecting the enzymatic hydrolysis of lignocellulose
    • Zhao X, Zhang L, Liu D. Biomass recalcitrance. Part I: the chemical compositions and physical structures affecting the enzymatic hydrolysis of lignocellulose. Biofuel Bioprod Bior. 2012;6(4):465-82. doi: 10.1002/bbb.1331.
    • (2012) Biofuel Bioprod Bior , vol.6 , Issue.4 , pp. 465-482
    • Zhao, X.1    Zhang, L.2    Liu, D.3
  • 4
    • 77950423986 scopus 로고    scopus 로고
    • Hemicelluloses
    • Scheller HV, Ulvskov P. Hemicelluloses. Annu Rev Plant Biol. 2010;61(1):263-89. doi: 10.1146/annurev-arplant-042809-112315.
    • (2010) Annu Rev Plant Biol , vol.61 , Issue.1 , pp. 263-289
    • Scheller, H.V.1    Ulvskov, P.2
  • 7
    • 84901766332 scopus 로고    scopus 로고
    • An overview of key pretreatment processes employed for bioconversion of lignocellulosic biomass into biofuels and value added products
    • Chaturvedi V, Verma P. An overview of key pretreatment processes employed for bioconversion of lignocellulosic biomass into biofuels and value added products. 3 Biotech. 2013;3(5):415-31. doi: 10.1007/s13205-013-0167-8.
    • (2013) 3 Biotech , vol.3 , Issue.5 , pp. 415-431
    • Chaturvedi, V.1    Verma, P.2
  • 8
    • 84861982164 scopus 로고    scopus 로고
    • Recent progress in consolidated bioprocessing
    • Olson DG, McBride JE, Joe Shaw A, Lynd LR. Recent progress in consolidated bioprocessing. Curr Opin Biotechnol. 2012;23(3):396-405. doi: 10.1016/j.copbio.2011.11.026.
    • (2012) Curr Opin Biotechnol , vol.23 , Issue.3 , pp. 396-405
    • Olson, D.G.1    McBride, J.E.2    Joe Shaw, A.3    Lynd, L.R.4
  • 9
    • 84987623323 scopus 로고    scopus 로고
    • The emergence of Clostridium thermocellum as a high utility candidate for consolidated bioprocessing applications
    • Akinosho H, Yee K, Close D, Ragauskas A. The emergence of Clostridium thermocellum as a high utility candidate for consolidated bioprocessing applications. Front Chem. 2014;2:66. doi: 10.3389/fchem.2014.00066.
    • (2014) Front Chem , vol.2 , pp. 66
    • Akinosho, H.1    Yee, K.2    Close, D.3    Ragauskas, A.4
  • 10
    • 84885176098 scopus 로고    scopus 로고
    • A genomic update on clostridial phylogeny: Gram-negative spore-formers and other misplaced clostridia
    • Yutin N, Galperin MY. A genomic update on clostridial phylogeny: gram-negative spore-formers and other misplaced clostridia. Environ Microbiol. 2013;15(10):2631-41. doi: 10.1111/1462-2920.12173.
    • (2013) Environ Microbiol , vol.15 , Issue.10 , pp. 2631-2641
    • Yutin, N.1    Galperin, M.Y.2
  • 11
    • 84942313615 scopus 로고    scopus 로고
    • Metabolic and process engineering of Clostridium cellulovorans for biofuel production from cellulose
    • Yang X, Xu M, Yang S-T. Metabolic and process engineering of Clostridium cellulovorans for biofuel production from cellulose. Metab Eng. 2015;32:39-48. doi: 10.1016/j.ymben.2015.09.001.
    • (2015) Metab Eng , vol.32 , pp. 39-48
    • Yang, X.1    Xu, M.2    Yang, S.-T.3
  • 12
    • 84865156886 scopus 로고    scopus 로고
    • Self-surface assembly of cellulosomes with two miniscaffoldins on Saccharomyces cerevisiae for cellulosic ethanol production
    • Fan LH, Zhang ZJ, Yu XY, Xue YX, Tan TW. Self-surface assembly of cellulosomes with two miniscaffoldins on Saccharomyces cerevisiae for cellulosic ethanol production. Proc Natl Acad Sci USA. 2012;109(33):13260-5. doi: 10.1073/pnas.1209856109.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.33 , pp. 13260-13265
    • Fan, L.H.1    Zhang, Z.J.2    Yu, X.Y.3    Xue, Y.X.4    Tan, T.W.5
  • 13
    • 70350553584 scopus 로고    scopus 로고
    • Heterologous expression of a Clostridium minicellulosome in Saccharomyces cerevisiae
    • Lilly M, Fierobe H-P, Van Zyl WH, Volschenk H. Heterologous expression of a Clostridium minicellulosome in Saccharomyces cerevisiae. FEMS Yeast Res. 2009;9(8):1236-49. doi: 10.1111/j.1567-1364.2009.00564.x.
    • (2009) FEMS Yeast Res , vol.9 , Issue.8 , pp. 1236-1249
    • Lilly, M.1    Fierobe, H.-P.2    Van Zyl, W.H.3    Volschenk, H.4
  • 14
    • 84873825894 scopus 로고    scopus 로고
    • Recombinant Bacillus subtilis that grows on untreated plant biomass
    • Anderson TD, Miller JI, Fierobe H-P, Clubb RT. Recombinant Bacillus subtilis that grows on untreated plant biomass. Appl Environ Microbiol. 2013;79(3):867-76. doi: 10.1128/aem.02433-12.
    • (2013) Appl Environ Microbiol , vol.79 , Issue.3 , pp. 867-876
    • Anderson, T.D.1    Miller, J.I.2    Fierobe, H.-P.3    Clubb, R.T.4
  • 15
    • 0034902930 scopus 로고    scopus 로고
    • Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum
    • Nölling J, Breton G, Omelchenko MV, Makarova KS, Zeng Q, Gibson R, et al. Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum. J Bacteriol. 2001;183(16):4823-38. doi: 10.1128/jb.183.16.4823-4838.2001.
    • (2001) J Bacteriol , vol.183 , Issue.16 , pp. 4823-4838
    • Nölling, J.1    Breton, G.2    Omelchenko, M.V.3    Makarova, K.S.4    Zeng, Q.5    Gibson, R.6
  • 16
    • 0028126829 scopus 로고
    • The phylogeny of the genus Clostridium: Proposal of five new genera and eleven new species combinations
    • 1:STN:280:DyaK2M%2FntF2jsA%3D%3D
    • Collins M, Lawson P, Willems A, Cordoba J, Fernandez-Garayzabal J, Garcia P, et al. The phylogeny of the genus Clostridium: proposal of five new genera and eleven new species combinations. Int J Syst Bacteriol. 1994;44(4):812-26.
    • (1994) Int J Syst Bacteriol , vol.44 , Issue.4 , pp. 812-826
    • Collins, M.1    Lawson, P.2    Willems, A.3    Cordoba, J.4    Fernandez-Garayzabal, J.5    Garcia, P.6
  • 17
    • 0022970603 scopus 로고
    • Acetone-butanol fermentation revisited
    • 1:CAS:528:DyaL2sXkvVGltg%3D%3D
    • Jones DT, Woods DR. Acetone-butanol fermentation revisited. Microbiol Rev. 1986;50(4):484-524.
    • (1986) Microbiol Rev , vol.50 , Issue.4 , pp. 484-524
    • Jones, D.T.1    Woods, D.R.2
  • 18
    • 78650698659 scopus 로고    scopus 로고
    • An analysis of net energy production and feedstock availability for biobutanol and bioethanol
    • Swana J, Yang Y, Behnam M, Thompson R. An analysis of net energy production and feedstock availability for biobutanol and bioethanol. Bioresour Technol. 2011;102(2):2112-7. doi: 10.1016/j.biortech.2010.08.051.
    • (2011) Bioresour Technol , vol.102 , Issue.2 , pp. 2112-2117
    • Swana, J.1    Yang, Y.2    Behnam, M.3    Thompson, R.4
  • 19
    • 84930631271 scopus 로고    scopus 로고
    • Butanol production from hexoses and pentoses by fermentation of Clostridium acetobutylicum
    • Raganati F, Olivieri G, Götz P, Marzocchella A, Salatino P. Butanol production from hexoses and pentoses by fermentation of Clostridium acetobutylicum. Anaerobe. 2015;34:146-55. doi: 10.1016/j.anaerobe.2015.05.008.
    • (2015) Anaerobe , vol.34 , pp. 146-155
    • Raganati, F.1    Olivieri, G.2    Götz, P.3    Marzocchella, A.4    Salatino, P.5
  • 20
    • 0036714783 scopus 로고    scopus 로고
    • Microbial cellulose utilization: Fundamentals and biotechnology
    • Lynd LR, Weimer PJ, van Zyl WH, Pretorius IS. Microbial cellulose utilization: fundamentals and biotechnology. Microbiol Mol Biol Rev. 2002;66(3):506-77. doi: 10.1128/mmbr.66.3.506-577.2002.
    • (2002) Microbiol Mol Biol Rev , vol.66 , Issue.3 , pp. 506-577
    • Lynd, L.R.1    Weimer, P.J.2    Van Zyl, W.H.3    Pretorius, I.S.4
  • 21
    • 77953631886 scopus 로고    scopus 로고
    • Cellulosomes: Highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates
    • Fontes CMGA, Gilbert HJ. Cellulosomes: highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates. Annu Rev Biochem. 2010;79(1):655-81. doi: 10.1146/annurev-biochem-091208-085603.
    • (2010) Annu Rev Biochem , vol.79 , Issue.1 , pp. 655-681
    • Fontes, C.M.G.A.1    Gilbert, H.J.2
  • 22
    • 0033167973 scopus 로고    scopus 로고
    • The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides
    • Shoham Y, Lamed R, Bayer EA. The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides. Trends Microbiol. 1999;7(7):275-81. doi: 10.1016/S0966-842X(99)01533-4.
    • (1999) Trends Microbiol , vol.7 , Issue.7 , pp. 275-281
    • Shoham, Y.1    Lamed, R.2    Bayer, E.A.3
  • 23
    • 70350455262 scopus 로고    scopus 로고
    • The prospects of cellulase-producing bacteria for the bioconversion of lignocellulosic biomass
    • 1:CAS:528:DC%2BD1MXhtVemtbzM
    • Maki M, Leung KT, Qin W. The prospects of cellulase-producing bacteria for the bioconversion of lignocellulosic biomass. Int J Biol Sci. 2009;5(5):500-16.
    • (2009) Int J Biol Sci , vol.5 , Issue.5 , pp. 500-516
    • Maki, M.1    Leung, K.T.2    Qin, W.3
  • 24
    • 0037137211 scopus 로고    scopus 로고
    • Characterization of the cellulolytic complex (cellulosome) of Clostridium acetobutylicum
    • Sabathé F, Bélaïch A, Soucaille P. Characterization of the cellulolytic complex (cellulosome) of Clostridium acetobutylicum. FEMS Microbiol Lett. 2002;217(1):15-22. doi: 10.1111/j.1574-6968.2002.tb11450.x.
    • (2002) FEMS Microbiol Lett , vol.217 , Issue.1 , pp. 15-22
    • Sabathé, F.1    Bélaïch, A.2    Soucaille, P.3
  • 25
    • 0037309120 scopus 로고    scopus 로고
    • Characterization of the CipA scaffolding protein and in vivo production of a minicellulosome in Clostridium acetobutylicum
    • Sabathé F, Soucaille P. Characterization of the CipA scaffolding protein and in vivo production of a minicellulosome in Clostridium acetobutylicum. J Bacteriol. 2003;185(3):1092-6. doi: 10.1128/jb.185.3.1092-1096.2003.
    • (2003) J Bacteriol , vol.185 , Issue.3 , pp. 1092-1096
    • Sabathé, F.1    Soucaille, P.2
  • 26
    • 15444362204 scopus 로고    scopus 로고
    • Heterologous production, assembly, and secretion of a Minicellulosome by Clostridium acetobutylicum ATCC 824
    • Mingardon F, Perret S, Bélaïch A, Tardif C, Bélaïch JP, Fierobe HP. Heterologous production, assembly, and secretion of a Minicellulosome by Clostridium acetobutylicum ATCC 824. Appl Environ Microbiol. 2005;71(3):1215-22. doi: 10.1128/aem.71.3.1215-1222.2005.
    • (2005) Appl Environ Microbiol , vol.71 , Issue.3 , pp. 1215-1222
    • Mingardon, F.1    Perret, S.2    Bélaïch, A.3    Tardif, C.4    Bélaïch, J.P.5    Fierobe, H.P.6
  • 27
    • 79955578131 scopus 로고    scopus 로고
    • The issue of secretion in heterologous expression of Clostridium cellulolyticum cellulase-encoding genes in Clostridium acetobutylicum ATCC 824
    • Mingardon F, Chanal A, Tardif C, Fierobe H-P. The issue of secretion in heterologous expression of Clostridium cellulolyticum cellulase-encoding genes in Clostridium acetobutylicum ATCC 824. Appl Environ Microbiol. 2011;77(9):2831-8. doi: 10.1128/aem.03012-10.
    • (2011) Appl Environ Microbiol , vol.77 , Issue.9 , pp. 2831-2838
    • Mingardon, F.1    Chanal, A.2    Tardif, C.3    Fierobe, H.-P.4
  • 28
    • 0028174818 scopus 로고
    • Heterologous expression of endo-beta-1,4-D-glucanase from Clostridium cellulovorans in Clostridium acetobutylicum ATCC 824 following transformation of the engB gene
    • 1:CAS:528:DyaK2cXntVCntw%3D%3D
    • Kim AY, Attwood GT, Holt SM, White BA, Blaschek HP. Heterologous expression of endo-beta-1,4-D-glucanase from Clostridium cellulovorans in Clostridium acetobutylicum ATCC 824 following transformation of the engB gene. Appl Environ Microbiol. 1994;60(1):337-40.
    • (1994) Appl Environ Microbiol , vol.60 , Issue.1 , pp. 337-340
    • Kim, A.Y.1    Attwood, G.T.2    Holt, S.M.3    White, B.A.4    Blaschek, H.P.5
  • 29
    • 84883568981 scopus 로고    scopus 로고
    • Secretion and assembly of functional mini-cellulosomes from synthetic chromosomal operons in Clostridium acetobutylicum ATCC 824
    • Kovács K, Willson BJ, Schwarz K, Heap JT, Jackson A, Bolam DN, et al. Secretion and assembly of functional mini-cellulosomes from synthetic chromosomal operons in Clostridium acetobutylicum ATCC 824. Biotechnol Biofuels. 2013;6(1):117.
    • (2013) Biotechnol Biofuels , vol.6 , Issue.1 , pp. 117
    • Kovács, K.1    Willson, B.J.2    Schwarz, K.3    Heap, J.T.4    Jackson, A.5    Bolam, D.N.6
  • 30
    • 0031019865 scopus 로고    scopus 로고
    • The processive endocellulase CelF, a major component of the Clostridium cellulolyticum cellulosome: Purification and characterization of the recombinant form
    • 1:CAS:528:DyaK2sXhsFaktw%3D%3D
    • Reverbel-Leroy C, Pages S, Belaich A, Belaich JP, Tardif C. The processive endocellulase CelF, a major component of the Clostridium cellulolyticum cellulosome: purification and characterization of the recombinant form. J Bacteriol. 1997;179(1):46-52.
    • (1997) J Bacteriol , vol.179 , Issue.1 , pp. 46-52
    • Reverbel-Leroy, C.1    Pages, S.2    Belaich, A.3    Belaich, J.P.4    Tardif, C.5
  • 31
    • 65549102556 scopus 로고    scopus 로고
    • The cellulosomes from Clostridium cellulolyticum
    • Fendri I, Tardif C, Fierobe HP, Lignon S, Valette O, Pagès S, et al. The cellulosomes from Clostridium cellulolyticum. FEBS J. 2009;276(11):3076-86. doi: 10.1111/j.1742-4658.2009.07025.x.
    • (2009) FEBS J , vol.276 , Issue.11 , pp. 3076-3086
    • Fendri, I.1    Tardif, C.2    Fierobe, H.P.3    Lignon, S.4    Valette, O.5    Pagès, S.6
  • 32
    • 0030700658 scopus 로고    scopus 로고
    • CelG from Clostridium cellulolyticum: A multidomain endoglucanase acting efficiently on crystalline cellulose
    • 1:CAS:528:DyaK2sXnt1akur8%3D
    • Gal L, Gaudin C, Belaich A, Pages S, Tardif C, Belaich JP. CelG from Clostridium cellulolyticum: a multidomain endoglucanase acting efficiently on crystalline cellulose. J Bacteriol. 1997;179(21):6595-601.
    • (1997) J Bacteriol , vol.179 , Issue.21 , pp. 6595-6601
    • Gal, L.1    Gaudin, C.2    Belaich, A.3    Pages, S.4    Tardif, C.5    Belaich, J.P.6
  • 33
    • 84896276890 scopus 로고    scopus 로고
    • Characterization of all family-9 glycoside hydrolases synthesized by the cellulosome-producing bacterium Clostridium cellulolyticum
    • Ravachol J, Borne R, Tardif C, de Philip P, Fierobe H-P. Characterization of all family-9 glycoside hydrolases synthesized by the cellulosome-producing bacterium Clostridium cellulolyticum. J Biol Chem. 2014;289(11):7335-48. doi: 10.1074/jbc.M113.545046.
    • (2014) J Biol Chem , vol.289 , Issue.11 , pp. 7335-7348
    • Ravachol, J.1    Borne, R.2    Tardif, C.3    De Philip, P.4    Fierobe, H.-P.5
  • 34
    • 0347579849 scopus 로고    scopus 로고
    • Degradation of cellulose substrates by cellulosome chimeras: Substrate targeting versus proximity of enzyme components
    • Fierobe H-P, Bayer EA, Tardif C, Czjzek M, Mechaly A, Bélaïch A, et al. Degradation of cellulose substrates by cellulosome chimeras: substrate targeting versus proximity of enzyme components. J Biol Chem. 2002;277(51):49621-30. doi: 10.1074/jbc.M207672200.
    • (2002) J Biol Chem , vol.277 , Issue.51 , pp. 49621-49630
    • Fierobe, H.-P.1    Bayer, E.A.2    Tardif, C.3    Czjzek, M.4    Mechaly, A.5    Bélaïch, A.6
  • 35
    • 34249740743 scopus 로고    scopus 로고
    • Processivity, substrate binding, and mechanism of cellulose hydrolysis by Thermobifida fusca Cel9A
    • Li Y, Irwin DC, Wilson DB. Processivity, substrate binding, and mechanism of cellulose hydrolysis by Thermobifida fusca Cel9A. Appl Environ Microbiol. 2007;73(10):3165-72. doi: 10.1128/aem.02960-06.
    • (2007) Appl Environ Microbiol , vol.73 , Issue.10 , pp. 3165-3172
    • Li, Y.1    Irwin, D.C.2    Wilson, D.B.3
  • 36
    • 0037478772 scopus 로고    scopus 로고
    • X-ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides
    • Mandelman D, Belaich A, Belaich JP, Aghajari N, Driguez H, Haser R. X-ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides. J Bacteriol. 2003;185(14):4127-35. doi: 10.1128/jb.185.14.4127-4135.2003.
    • (2003) J Bacteriol , vol.185 , Issue.14 , pp. 4127-4135
    • Mandelman, D.1    Belaich, A.2    Belaich, J.P.3    Aghajari, N.4    Driguez, H.5    Haser, R.6
  • 37
    • 0037371574 scopus 로고    scopus 로고
    • Synergistic effects of cellulosomal xylanase and cellulases from Clostridium cellulovorans on plant cell wall degradation
    • Murashima K, Kosugi A, Doi RH. Synergistic effects of cellulosomal xylanase and cellulases from Clostridium cellulovorans on plant cell wall degradation. J Bacteriol. 2003;185(5):1518-24. doi: 10.1128/JB.185.5.1518-1524.2003.
    • (2003) J Bacteriol , vol.185 , Issue.5 , pp. 1518-1524
    • Murashima, K.1    Kosugi, A.2    Doi, R.H.3
  • 38
    • 0023133272 scopus 로고
    • Purification and characterization of two endoxylanases from Clostridium acetobutylicum ATCC 824
    • 1:CAS:528:DyaL2sXktF2rsrY%3D
    • Lee SF, Forsberg CW, Rattray JB. Purification and characterization of two endoxylanases from Clostridium acetobutylicum ATCC 824. Appl Environ Microbiol. 1987;53(4):644-50.
    • (1987) Appl Environ Microbiol , vol.53 , Issue.4 , pp. 644-650
    • Lee, S.F.1    Forsberg, C.W.2    Rattray, J.B.3
  • 39
    • 0022409935 scopus 로고
    • Xylanolytic activity of Clostridium acetobutylicum
    • 1:CAS:528:DyaL2MXlslGhsrk%3D
    • Lee SF, Forsberg CW, Gibbins LN. Xylanolytic activity of Clostridium acetobutylicum. Appl Environ Microbiol. 1985;50(4):1068-76.
    • (1985) Appl Environ Microbiol , vol.50 , Issue.4 , pp. 1068-1076
    • Lee, S.F.1    Forsberg, C.W.2    Gibbins, L.N.3
  • 40
    • 33947152858 scopus 로고    scopus 로고
    • Enzyme diversity of the cellulolytic system produced by Clostridium cellulolyticum explored by two-dimensional analysis: Identification of seven genes encoding new dockerin-containing proteins
    • Blouzard JC, Bourgeois C, de Philip P, Valette O, Bélaïch A, Tardif C, et al. Enzyme diversity of the cellulolytic system produced by Clostridium cellulolyticum explored by two-dimensional analysis: identification of seven genes encoding new dockerin-containing proteins. J Bacteriol. 2007;189(6):2300-9. doi: 10.1128/jb.00917-06.
    • (2007) J Bacteriol , vol.189 , Issue.6 , pp. 2300-2309
    • Blouzard, J.C.1    Bourgeois, C.2    De Philip, P.3    Valette, O.4    Bélaïch, A.5    Tardif, C.6
  • 41
    • 84878083304 scopus 로고    scopus 로고
    • Structure and regulation of the cellulose degradome in Clostridium cellulolyticum
    • Xu C, Huang R, Teng L, Wang D, Hemme CL, Borovok I, et al. Structure and regulation of the cellulose degradome in Clostridium cellulolyticum. Biotechnol Biofuels. 2013;6(1):1-15. doi: 10.1186/1754-6834-6-73.
    • (2013) Biotechnol Biofuels , vol.6 , Issue.1 , pp. 1-15
    • Xu, C.1    Huang, R.2    Teng, L.3    Wang, D.4    Hemme, C.L.5    Borovok, I.6
  • 42
    • 84860362257 scopus 로고    scopus 로고
    • Integration of DNA into bacterial chromosomes from plasmids without a counter-selection marker
    • Heap JT, Ehsaan M, Cooksley CM, Ng YK, Cartman ST, Winzer K, et al. Integration of DNA into bacterial chromosomes from plasmids without a counter-selection marker. Nucleic Acids Res. 2012;40(8):e59. doi: 10.1093/nar/gkr1321.
    • (2012) Nucleic Acids Res , vol.40 , Issue.8 , pp. e59
    • Heap, J.T.1    Ehsaan, M.2    Cooksley, C.M.3    Ng, Y.K.4    Cartman, S.T.5    Winzer, K.6
  • 44
    • 0026624779 scopus 로고
    • Characterization of the Lactococcus lactis pepN gene encoding an aminopeptidase homologous to mammalian aminopeptidase N
    • Tan PST, van Alen-Boerrigter IJ, Poolman B, Siezen RJ, de Vos WM, Konings WN. Characterization of the Lactococcus lactis pepN gene encoding an aminopeptidase homologous to mammalian aminopeptidase N. FEBS Lett. 1992;306(1):9-16. doi: 10.1016/0014-5793(92)80827-4.
    • (1992) FEBS Lett , vol.306 , Issue.1 , pp. 9-16
    • Tan, P.S.T.1    Van Alen-Boerrigter, I.J.2    Poolman, B.3    Siezen, R.J.4    De Vos, W.M.5    Konings, W.N.6
  • 45
    • 0027495916 scopus 로고
    • S-layer protein of Lactobacillus acidophilus ATCC 4356: Purification, expression in Escherichia coli, and nucleotide sequence of the corresponding gene
    • 1:CAS:528:DyaK2cXkslSitw%3D%3D
    • Boot HJ, Kolen CP, van Noort JM, Pouwels PH. S-layer protein of Lactobacillus acidophilus ATCC 4356: purification, expression in Escherichia coli, and nucleotide sequence of the corresponding gene. J Bacteriol. 1993;175(19):6089-96.
    • (1993) J Bacteriol , vol.175 , Issue.19 , pp. 6089-6096
    • Boot, H.J.1    Kolen, C.P.2    Van Noort, J.M.3    Pouwels, P.H.4
  • 46
    • 29744441162 scopus 로고    scopus 로고
    • Sequence and phylogenetic analysis of the gene for surface layer protein, slpA, from 14 PCR ribotypes of Clostridium difficile
    • Ní Eidhin D, Ryan AW, Doyle RM, Walsh JB, Kelleher D. Sequence and phylogenetic analysis of the gene for surface layer protein, slpA, from 14 PCR ribotypes of Clostridium difficile. J Med Microbiol. 2006;55(1):69-83. doi: 10.1099/jmm.0.46204-0.
    • (2006) J Med Microbiol , vol.55 , Issue.1 , pp. 69-83
    • Ní Eidhin, D.1    Ryan, A.W.2    Doyle, R.M.3    Walsh, J.B.4    Kelleher, D.5
  • 47
    • 0023237183 scopus 로고
    • In vivo transcription of bacteriophage phi 29 DNA: Transcription termination
    • 1:CAS:528:DyaL2sXitVylsrw%3D
    • Barthelemy I, Salas M, Mellado RP. In vivo transcription of bacteriophage phi 29 DNA: transcription termination. J Virol. 1987;61(5):1751-5.
    • (1987) J Virol , vol.61 , Issue.5 , pp. 1751-1755
    • Barthelemy, I.1    Salas, M.2    Mellado, R.P.3
  • 48
    • 0036529579 scopus 로고    scopus 로고
    • Sequence requirements for terminators and antiterminators in the T box transcription antitermination system: Disparity between conservation and functional requirements
    • 1:CAS:528:DC%2BD38XjtFOqtrs%3D
    • Grundy FJ, Moir TR, Haldeman MT, Henkin TM. Sequence requirements for terminators and antiterminators in the T box transcription antitermination system: disparity between conservation and functional requirements. Nucleic Acids Res. 2002;30(7):1646-55.
    • (2002) Nucleic Acids Res , vol.30 , Issue.7 , pp. 1646-1655
    • Grundy, F.J.1    Moir, T.R.2    Haldeman, M.T.3    Henkin, T.M.4
  • 49
    • 0026077462 scopus 로고
    • Analysis of the complex transcription termination region of the Escherichia coli rrnB gene
    • Orosz A, Boros I, Venetianer P. Analysis of the complex transcription termination region of the Escherichia coli rrnB gene. Eur J Biochem. 1991;201(3):653-9. doi: 10.1111/j.1432-1033.1991.tb16326.x.
    • (1991) Eur J Biochem , vol.201 , Issue.3 , pp. 653-659
    • Orosz, A.1    Boros, I.2    Venetianer, P.3
  • 50
    • 84902168071 scopus 로고    scopus 로고
    • Ectopic integration vectors for generating fluorescent promoter fusions in Bacillus subtilis with minimal dark noise
    • Trauth S, Bischofs IB. Ectopic integration vectors for generating fluorescent promoter fusions in Bacillus subtilis with minimal dark noise. PLoS One. 2014;9(5):e98360. doi: 10.1371/journal.pone.0098360.
    • (2014) PLoS One , vol.9 , Issue.5 , pp. e98360
    • Trauth, S.1    Bischofs, I.B.2
  • 52
    • 53649110127 scopus 로고    scopus 로고
    • Functional Secretion of a type 1 antifreeze protein analogue by optimization of promoter, signal peptide, prosequence, and terminator in Lactococcus lactis
    • Yeh CM, Huang XH, Sue CW. Functional Secretion of a type 1 antifreeze protein analogue by optimization of promoter, signal peptide, prosequence, and terminator in Lactococcus lactis. J Agric Food Chem. 2008;56(18):8442-50. doi: 10.1021/jf801580s.
    • (2008) J Agric Food Chem , vol.56 , Issue.18 , pp. 8442-8450
    • Yeh, C.M.1    Huang, X.H.2    Sue, C.W.3
  • 53
    • 0029983647 scopus 로고    scopus 로고
    • Molecular study and overexpression of the Clostridium cellulolyticum celF cellulase gene in Escherichia coli
    • Reverbel-Leroy C, Belaich A, Bernadac A, Gaudin C, Belaich J-P, Tardif C. Molecular study and overexpression of the Clostridium cellulolyticum celF cellulase gene in Escherichia coli. Microbiology. 1996;142(4):1013-23. doi: 10.1099/00221287-142-4-1013.
    • (1996) Microbiology , vol.142 , Issue.4 , pp. 1013-1023
    • Reverbel-Leroy, C.1    Belaich, A.2    Bernadac, A.3    Gaudin, C.4    Belaich, J.-P.5    Tardif, C.6
  • 55
    • 0020425618 scopus 로고
    • Inhibition of Clostridium thermocellum cellulase by end products of cellulolysis
    • 1:CAS:528:DyaL38XlvFGjs7g%3D
    • Johnson EA, Reese ET, Demain AL. Inhibition of Clostridium thermocellum cellulase by end products of cellulolysis. J Appl Biochem. 1982;4:64-71.
    • (1982) J Appl Biochem , vol.4 , pp. 64-71
    • Johnson, E.A.1    Reese, E.T.2    Demain, A.L.3
  • 56
    • 0036157410 scopus 로고    scopus 로고
    • Cell-surface-anchoring role of N-terminal surface layer homology domains of Clostridium cellulovorans EngE
    • Kosugi A, Murashima K, Tamaru Y, Doi RH. Cell-surface-anchoring role of N-terminal surface layer homology domains of Clostridium cellulovorans EngE. J Bacteriol. 2002;184(4):884-8. doi: 10.1128/jb.184.4.884-888.2002.
    • (2002) J Bacteriol , vol.184 , Issue.4 , pp. 884-888
    • Kosugi, A.1    Murashima, K.2    Tamaru, Y.3    Doi, R.H.4
  • 57
    • 23744447992 scopus 로고    scopus 로고
    • Clostridium cellulolyticum: Model organism of mesophilic cellulolytic clostridia
    • Desvaux M. Clostridium cellulolyticum: model organism of mesophilic cellulolytic clostridia. FEMS Microbiol Rev. 2005;29(4):741-64. doi: 10.1016/j.femsre.2004.11.003.
    • (2005) FEMS Microbiol Rev , vol.29 , Issue.4 , pp. 741-764
    • Desvaux, M.1
  • 58
    • 27744600973 scopus 로고    scopus 로고
    • Unconventional mode of attachment of the Ruminococcus flavefaciens cellulosome to the cell surface
    • Rincon MT, Čepeljnik T, Martin JC, Lamed R, Barak Y, Bayer EA, et al. Unconventional mode of attachment of the Ruminococcus flavefaciens cellulosome to the cell surface. J Bacteriol. 2005;187(22):7569-78. doi: 10.1128/jb.187.22.7569-7578.2005.
    • (2005) J Bacteriol , vol.187 , Issue.22 , pp. 7569-7578
    • Rincon, M.T.1    Čepeljnik, T.2    Martin, J.C.3    Lamed, R.4    Barak, Y.5    Bayer, E.A.6
  • 60
    • 82155168216 scopus 로고    scopus 로고
    • Sortase enzymes in gram-positive bacteria
    • Spirig T, Weiner EM, Clubb RT. Sortase enzymes in gram-positive bacteria. Mol Microbiol. 2011;82(5):1044-59. doi: 10.1111/j.1365-2958.2011.07887.x.
    • (2011) Mol Microbiol , vol.82 , Issue.5 , pp. 1044-1059
    • Spirig, T.1    Weiner, E.M.2    Clubb, R.T.3
  • 61
    • 23944493423 scopus 로고    scopus 로고
    • Genomic analysis of the protein secretion systems in Clostridium acetobutylicum ATCC 824
    • Desvaux M, Khan A, Scott-Tucker A, Chaudhuri RR, Pallen MJ, Henderson IR. Genomic analysis of the protein secretion systems in Clostridium acetobutylicum ATCC 824. Biochim Biophys Acta. 2005;1745(2):223-53. doi: 10.1016/j.bbamcr.2005.04.006.
    • (2005) Biochim Biophys Acta , vol.1745 , Issue.2 , pp. 223-253
    • Desvaux, M.1    Khan, A.2    Scott-Tucker, A.3    Chaudhuri, R.R.4    Pallen, M.J.5    Henderson, I.R.6
  • 62
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • 1:CAS:528:DyaE3sXht1Wjsrc%3D
    • Schleifer KH, Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol Rev. 1972;36(4):407.
    • (1972) Bacteriol Rev , vol.36 , Issue.4 , pp. 407
    • Schleifer, K.H.1    Kandler, O.2
  • 63
    • 77956286293 scopus 로고    scopus 로고
    • Sortase transpeptidases: Insights into mechanism, substrate specificity, and inhibition
    • Clancy KW, Melvin JA, McCafferty DG. Sortase transpeptidases: insights into mechanism, substrate specificity, and inhibition. Pept Sci. 2010;94(4):385-96. doi: 10.1002/bip.21472.
    • (2010) Pept Sci , vol.94 , Issue.4 , pp. 385-396
    • Clancy, K.W.1    Melvin, J.A.2    McCafferty, D.G.3
  • 64
    • 23944522769 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase transpeptidase SrtA: Insight into the kinetic mechanism and evidence for a reverse protonation catalytic mechanism
    • Frankel BA, Kruger RG, Robinson DE, Kelleher NL, McCafferty DG. Staphylococcus aureus sortase transpeptidase SrtA: insight into the kinetic mechanism and evidence for a reverse protonation catalytic mechanism. Biochemistry. 2005;44(33):11188-200. doi: 10.1021/bi050141j.
    • (2005) Biochemistry , vol.44 , Issue.33 , pp. 11188-11200
    • Frankel, B.A.1    Kruger, R.G.2    Robinson, D.E.3    Kelleher, N.L.4    McCafferty, D.G.5
  • 65
    • 0036226966 scopus 로고    scopus 로고
    • Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence
    • Bierne H, Mazmanian SK, Trost M, Pucciarelli MG, Liu G, Dehoux P, et al. Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence. Mol Microbiol. 2002;43(4):869-81. doi: 10.1046/j.1365-2958.2002.02798.x.
    • (2002) Mol Microbiol , vol.43 , Issue.4 , pp. 869-881
    • Bierne, H.1    Mazmanian, S.K.2    Trost, M.3    Pucciarelli, M.G.4    Liu, G.5    Dehoux, P.6
  • 66
    • 21144451705 scopus 로고    scopus 로고
    • Bacillus anthracis sortase A (SrtA) anchors LPXTG motif-containing surface proteins to the cell wall envelope
    • Gaspar AH, Marraffini LA, Glass EM, DeBord KL, Ton-That H, Schneewind O. Bacillus anthracis sortase A (SrtA) anchors LPXTG motif-containing surface proteins to the cell wall envelope. J Bacteriol. 2005;187(13):4646-55. doi: 10.1128/JB.187.13.4646-4655.2005.
    • (2005) J Bacteriol , vol.187 , Issue.13 , pp. 4646-4655
    • Gaspar, A.H.1    Marraffini, L.A.2    Glass, E.M.3    DeBord, K.L.4    Ton-That, H.5    Schneewind, O.6
  • 67
    • 0034603801 scopus 로고    scopus 로고
    • Anchor structure of cell wall surface proteins in Listeria monocytogenes
    • 1:CAS:528:DC%2BD3cXhsFags7Y%3D
    • Dhar G, Faull KF, Schneewind O. Anchor structure of cell wall surface proteins in Listeria monocytogenes. Biochemistry. 2000;39(13):3725-33.
    • (2000) Biochemistry , vol.39 , Issue.13 , pp. 3725-3733
    • Dhar, G.1    Faull, K.F.2    Schneewind, O.3
  • 68
    • 0032582680 scopus 로고    scopus 로고
    • Anchor structure of staphylococcal surface proteins: II. COOH-terminal structure of muramidase and amidase-solubilized surface protein
    • Navarre WW, Ton-That H, Faull KF, Schneewind O. Anchor structure of staphylococcal surface proteins: II. COOH-terminal structure of muramidase and amidase-solubilized surface protein. J Biol Chem. 1998;273(44):29135-42. doi: 10.1074/jbc.273.44.29135.
    • (1998) J Biol Chem , vol.273 , Issue.44 , pp. 29135-29142
    • Navarre, W.W.1    Ton-That, H.2    Faull, K.F.3    Schneewind, O.4
  • 69
    • 0027442464 scopus 로고
    • Cell wall sorting signals in surface proteins of gram-positive bacteria
    • 1:CAS:528:DyaK2cXislWjtw%3D%3D
    • Schneewind O, Mihaylova-Petkov D, Model P. Cell wall sorting signals in surface proteins of gram-positive bacteria. EMBO J. 1993;12(12):4803-11.
    • (1993) EMBO J , vol.12 , Issue.12 , pp. 4803-4811
    • Schneewind, O.1    Mihaylova-Petkov, D.2    Model, P.3
  • 70
    • 84862944239 scopus 로고    scopus 로고
    • Functional characterization and localization of a Bacillus subtilis sortase and its substrate and use of this sortase system to covalently anchor a heterologous protein to the B. Subtilis cell wall for surface display
    • Liew PX, Wang CLC, Wong S-L. Functional characterization and localization of a Bacillus subtilis sortase and its substrate and use of this sortase system to covalently anchor a heterologous protein to the B. subtilis cell wall for surface display. J Bacteriol. 2012;194(1):161-75. doi: 10.1128/jb.05711-11.
    • (2012) J Bacteriol , vol.194 , Issue.1 , pp. 161-175
    • Liew, P.X.1    Wang, C.L.C.2    Wong, S.-L.3
  • 71
    • 84952938924 scopus 로고    scopus 로고
    • Mutant generation by allelic exchange and genome resequencing of the biobutanol organism Clostridium acetobutylicum ATCC 824
    • Ehsaan M, Kuit W, Zhang Y, Cartman ST, Heap JT, Winzer K, et al. Mutant generation by allelic exchange and genome resequencing of the biobutanol organism Clostridium acetobutylicum ATCC 824. Biotechnol Biofuels. 2016;9(1):1-20. doi: 10.1186/s13068-015-0410-0.
    • (2016) Biotechnol Biofuels , vol.9 , Issue.1 , pp. 1-20
    • Ehsaan, M.1    Kuit, W.2    Zhang, Y.3    Cartman, S.T.4    Heap, J.T.5    Winzer, K.6
  • 72
    • 0022706425 scopus 로고
    • Fermentation of xylan by Clostridium acetobutylicum
    • Lemmel SA, Datta R, Frankiewicz JR. Fermentation of xylan by Clostridium acetobutylicum. Enzyme Microb Technol. 1986;8(4):217-21. doi: 10.1016/0141-0229(86)90091-8.
    • (1986) Enzyme Microb Technol , vol.8 , Issue.4 , pp. 217-221
    • Lemmel, S.A.1    Datta, R.2    Frankiewicz, J.R.3
  • 73
    • 33745111655 scopus 로고    scopus 로고
    • Butanol production from corn fiber xylan using Clostridium acetobutylicum
    • Qureshi N, Li XL, Hughes S, Saha BC, Cotta MA. Butanol production from corn fiber xylan using Clostridium acetobutylicum. Biotechnol Prog. 2006;22(3):673-80. doi: 10.1021/bp050360w.
    • (2006) Biotechnol Prog , vol.22 , Issue.3 , pp. 673-680
    • Qureshi, N.1    Li, X.L.2    Hughes, S.3    Saha, B.C.4    Cotta, M.A.5
  • 74
    • 84969775936 scopus 로고    scopus 로고
    • Direct conversion of xylan to butanol by a wild-type Clostridium species strain G117
    • Yan Y, Basu A, Li T, He J. Direct conversion of xylan to butanol by a wild-type Clostridium species strain G117. Biotechnol Bioeng. 2016;. doi: 10.1002/bit.25940.
    • (2016) Biotechnol Bioeng
    • Yan, Y.1    Basu, A.2    Li, T.3    He, J.4
  • 75
    • 0021815411 scopus 로고
    • Cellulolytic activity of Clostridium acetobutylicum
    • 1:CAS:528:DyaL2MXlt1Wlt74%3D
    • Lee SF, Forsberg CW, Gibbins LN. Cellulolytic activity of Clostridium acetobutylicum. Appl Environ Microbiol. 1985;50(2):220-8.
    • (1985) Appl Environ Microbiol , vol.50 , Issue.2 , pp. 220-228
    • Lee, S.F.1    Forsberg, C.W.2    Gibbins, L.N.3
  • 76
    • 84870314936 scopus 로고    scopus 로고
    • Sequence, structure, and evolution of cellulases in glycoside hydrolase family 48
    • Sukharnikov LO, Alahuhta M, Brunecky R, Upadhyay A, Himmel ME, Lunin VV, et al. Sequence, structure, and evolution of cellulases in glycoside hydrolase family 48. J Biol Chem. 2012;287(49):41068-77. doi: 10.1074/jbc.M112.405720.
    • (2012) J Biol Chem , vol.287 , Issue.49 , pp. 41068-41077
    • Sukharnikov, L.O.1    Alahuhta, M.2    Brunecky, R.3    Upadhyay, A.4    Himmel, M.E.5    Lunin, V.V.6
  • 77
    • 34948817185 scopus 로고    scopus 로고
    • Global view of the Clostridium thermocellum cellulosome revealed by quantitative proteomic analysis
    • Gold ND, Martin VJJ. Global view of the Clostridium thermocellum cellulosome revealed by quantitative proteomic analysis. J Bacteriol. 2007;189(19):6787-95. doi: 10.1128/jb.00882-07.
    • (2007) J Bacteriol , vol.189 , Issue.19 , pp. 6787-6795
    • Gold, N.D.1    Martin, V.J.J.2
  • 78
    • 0031020492 scopus 로고    scopus 로고
    • Characterization of the cellulolytic complex (cellulosome) produced by Clostridium cellulolyticum
    • 1:CAS:528:DyaK2sXhsV2ju7Y%3D
    • Gal L, Pages S, Gaudin C, Belaich A, Reverbel-Leroy C, Tardif C, et al. Characterization of the cellulolytic complex (cellulosome) produced by Clostridium cellulolyticum. Appl Environ Microbiol. 1997;63(3):903-9.
    • (1997) Appl Environ Microbiol , vol.63 , Issue.3 , pp. 903-909
    • Gal, L.1    Pages, S.2    Gaudin, C.3    Belaich, A.4    Reverbel-Leroy, C.5    Tardif, C.6
  • 79
    • 0036211985 scopus 로고    scopus 로고
    • Determination of subunit composition of Clostridium cellulovorans cellulosomes that degrade plant cell walls
    • Murashima K, Kosugi A, Doi RH. Determination of subunit composition of Clostridium cellulovorans cellulosomes that degrade plant cell walls. Appl Environ Microbiol. 2002;68(4):1610-5. doi: 10.1128/aem.68.4.1610-1615.2002.
    • (2002) Appl Environ Microbiol , vol.68 , Issue.4 , pp. 1610-1615
    • Murashima, K.1    Kosugi, A.2    Doi, R.H.3
  • 80
    • 84936948373 scopus 로고    scopus 로고
    • Clostridium clariflavum key cellulosome players are revealed by proteomic analysis
    • Artzi L, Morag E, Barak Y, Lamed R, Bayer EA. Clostridium clariflavum key cellulosome players are revealed by proteomic analysis. MBio. 2015;6(3):e00411-15. doi: 10.1128/mBio.00411-15.
    • (2015) MBio , vol.6 , Issue.3 , pp. e00411-e004115
    • Artzi, L.1    Morag, E.2    Barak, Y.3    Lamed, R.4    Bayer, E.A.5
  • 81
    • 84911458413 scopus 로고    scopus 로고
    • Biobutanol production by Clostridium acetobutylicum using xylose recovered from birch Kraft black liquor
    • Kudahettige-Nilsson RL, Helmerius J, Nilsson RT, Sjöblom M, Hodge DB, Rova U. Biobutanol production by Clostridium acetobutylicum using xylose recovered from birch Kraft black liquor. Bioresour Technol. 2015;176:71-9. doi: 10.1016/j.biortech.2014.11.012.
    • (2015) Bioresour Technol , vol.176 , pp. 71-79
    • Kudahettige-Nilsson, R.L.1    Helmerius, J.2    Nilsson, R.T.3    Sjöblom, M.4    Hodge, D.B.5    Rova, U.6
  • 82
    • 60749121157 scopus 로고    scopus 로고
    • Hemicellulose biorefineries: A review on biomass pretreatments
    • 1:CAS:528:DC%2BD1cXhsV2ksrvP
    • Carvalheiro F, Duarte LC, Gírio FM. Hemicellulose biorefineries: a review on biomass pretreatments. J Sci Ind Res. 2008;67(11):849-64.
    • (2008) J Sci Ind Res , vol.67 , Issue.11 , pp. 849-864
    • Carvalheiro, F.1    Duarte, L.C.2    Gírio, F.M.3
  • 84
    • 34548124567 scopus 로고    scopus 로고
    • The ClosTron: A universal gene knock-out system for the genus Clostridium
    • Heap JT, Pennington OJ, Cartman ST, Carter GP, Minton NP. The ClosTron: a universal gene knock-out system for the genus Clostridium. J Microbiol Methods. 2007;70(3):452-64. doi: 10.1016/j.mimet.2007.05.021.
    • (2007) J Microbiol Methods , vol.70 , Issue.3 , pp. 452-464
    • Heap, J.T.1    Pennington, O.J.2    Cartman, S.T.3    Carter, G.P.4    Minton, N.P.5
  • 85
    • 0021261020 scopus 로고
    • Intermediary metabolism in Clostridium acetobutylicum: Levels of enzymes involved in the formation of acetate and butyrate
    • 1:CAS:528:DyaL2cXksFWnuro%3D
    • Hartmanis MGN, Gatenbeck S. Intermediary metabolism in Clostridium acetobutylicum: levels of enzymes involved in the formation of acetate and butyrate. Appl Environ Microbiol. 1984;47(6):1277-83.
    • (1984) Appl Environ Microbiol , vol.47 , Issue.6 , pp. 1277-1283
    • Hartmanis, M.G.N.1    Gatenbeck, S.2
  • 86
    • 33846464622 scopus 로고    scopus 로고
    • A standard operating procedure (SOP) for the preparation of intra- and extracellular proteins of Clostridium acetobutylicum for proteome analysis
    • Schwarz K, Fiedler T, Fischer R-J, Bahl H. A standard operating procedure (SOP) for the preparation of intra- and extracellular proteins of Clostridium acetobutylicum for proteome analysis. J Microbiol Methods. 2007;68(2):396-402. doi: 10.1016/j.mimet.2006.09.018.
    • (2007) J Microbiol Methods , vol.68 , Issue.2 , pp. 396-402
    • Schwarz, K.1    Fiedler, T.2    Fischer, R.-J.3    Bahl, H.4
  • 87
    • 0025939528 scopus 로고
    • Variation in the expression of cell envelope proteins of coagulase-negative staphylococci cultured under iron-restricted conditions in human peritoneal dialysate
    • 1:CAS:528:DyaK38XhvVWlsw%3D%3D
    • Wilcox MH, Williams P, Smith DG, Modun B, Finch RG, Denyer SP. Variation in the expression of cell envelope proteins of coagulase-negative staphylococci cultured under iron-restricted conditions in human peritoneal dialysate. J Gen Microbiol. 1991;137(11):2561-70.
    • (1991) J Gen Microbiol , vol.137 , Issue.11 , pp. 2561-2570
    • Wilcox, M.H.1    Williams, P.2    Smith, D.G.3    Modun, B.4    Finch, R.G.5    Denyer, S.P.6
  • 88
    • 0020049955 scopus 로고
    • Clostridium acetobutylicum protoplast formation and regeneration
    • 1:STN:280:DC%2BC3crnvFGjtg%3D%3D
    • Allcock ER, Reid SJ, Jones DT, Woods DR. Clostridium acetobutylicum protoplast formation and regeneration. Appl Environ Microbiol. 1982;43(3):719-21.
    • (1982) Appl Environ Microbiol , vol.43 , Issue.3 , pp. 719-721
    • Allcock, E.R.1    Reid, S.J.2    Jones, D.T.3    Woods, D.R.4
  • 89
    • 0015155688 scopus 로고
    • Oxygen and the growth and metabolism of Clostridium acetobutylicum
    • O'Brien R, Morris J. Oxygen and the growth and metabolism of Clostridium acetobutylicum. J Gen Microbiol. 1971;68(3):307-18.
    • (1971) J Gen Microbiol , vol.68 , Issue.3 , pp. 307-318
    • O'Brien, R.1    Morris, J.2
  • 90
    • 33644633124 scopus 로고    scopus 로고
    • A transition from cellulose swelling to cellulose dissolution by o-phosphoric acid: Evidence from enzymatic hydrolysis and supramolecular structure
    • Zhang YHP, Cui J, Lynd LR, Kuang LR. A transition from cellulose swelling to cellulose dissolution by o-phosphoric acid: evidence from enzymatic hydrolysis and supramolecular structure. Biomacromolecules. 2006;7(2):644-8. doi: 10.1021/bm050799c.
    • (2006) Biomacromolecules , vol.7 , Issue.2 , pp. 644-648
    • Zhang, Y.H.P.1    Cui, J.2    Lynd, L.R.3    Kuang, L.R.4
  • 91
    • 60549104203 scopus 로고    scopus 로고
    • An optimized microplate assay system for quantitative evaluation of plant cell wall-degrading enzyme activity of fungal culture extracts
    • King BC, Donnelly MK, Bergstrom GC, Walker LP, Gibson DM. An optimized microplate assay system for quantitative evaluation of plant cell wall-degrading enzyme activity of fungal culture extracts. Biotechnol Bioeng. 2009;102(4):1033-44. doi: 10.1002/bit.22151.
    • (2009) Biotechnol Bioeng , vol.102 , Issue.4 , pp. 1033-1044
    • King, B.C.1    Donnelly, M.K.2    Bergstrom, G.C.3    Walker, L.P.4    Gibson, D.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.