메뉴 건너뛰기




Volumn 41, Issue 1-2, 2007, Pages 186-195

Effect of poly(ethylene glycol) on enzymatic hydrolysis and adsorption of cellulase enzymes to pretreated lignocellulose

Author keywords

Adsorption; CBM; Cellulase; Enzymatic hydrolysis; Hypocrea jecorina; Lignin; PEG

Indexed keywords

ADSORPTION; BINDING ENERGY; BIOMASS; CELLULOSE; ENZYME KINETICS; ETHANOL; HYDROLYSIS;

EID: 34248205049     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2007.01.003     Document Type: Article
Times cited : (213)

References (40)
  • 1
    • 0032552220 scopus 로고    scopus 로고
    • Benefits from Tween during enzymic hydrolysis of corn stover
    • Kaar W.E., and Holtzapple M. Benefits from Tween during enzymic hydrolysis of corn stover. Biotechnol Bioeng 59 (1998) 419-427
    • (1998) Biotechnol Bioeng , vol.59 , pp. 419-427
    • Kaar, W.E.1    Holtzapple, M.2
  • 2
    • 0031826976 scopus 로고    scopus 로고
    • Effect of surfactants and zeolites on simultaneous saccharification and fermentation of steam-exploded poplar biomass to ethanol
    • Ballesteros I., Oliva J.M., Carrasco J., Cabanas A., Navarro A.A., and Ballesteros M. Effect of surfactants and zeolites on simultaneous saccharification and fermentation of steam-exploded poplar biomass to ethanol. Appl Biochem Biotechnol 70 (1998) 369-381
    • (1998) Appl Biochem Biotechnol , vol.70 , pp. 369-381
    • Ballesteros, I.1    Oliva, J.M.2    Carrasco, J.3    Cabanas, A.4    Navarro, A.A.5    Ballesteros, M.6
  • 3
    • 0037008410 scopus 로고    scopus 로고
    • Mechanism of surfactant effect in enzymatic hydrolysis of lignocellulose
    • Eriksson T., Börjesson J., and Tjerneld F. Mechanism of surfactant effect in enzymatic hydrolysis of lignocellulose. Enzyme Microb Technol 31 3 (2002) 353-364
    • (2002) Enzyme Microb Technol , vol.31 , Issue.3 , pp. 353-364
    • Eriksson, T.1    Börjesson, J.2    Tjerneld, F.3
  • 4
    • 0028598828 scopus 로고
    • Pretreatment of Bagasse by nonionic surfactant for the enzymatic hydrolysis
    • Kurakake M., Ooshima H., Kato J., and Harano Y. Pretreatment of Bagasse by nonionic surfactant for the enzymatic hydrolysis. Bioresour Technol 49 (1994) 247-251
    • (1994) Bioresour Technol , vol.49 , pp. 247-251
    • Kurakake, M.1    Ooshima, H.2    Kato, J.3    Harano, Y.4
  • 5
    • 33745793410 scopus 로고    scopus 로고
    • BSA treatment to enhance enzymatic hydrolysis of cellulose in lignin containing substrates
    • Yang B., and Wyman C.E. BSA treatment to enhance enzymatic hydrolysis of cellulose in lignin containing substrates. Biotechnol Bioeng 94 4 (2006) 611-617
    • (2006) Biotechnol Bioeng , vol.94 , Issue.4 , pp. 611-617
    • Yang, B.1    Wyman, C.E.2
  • 6
    • 33847325663 scopus 로고    scopus 로고
    • Enhanced enzymatic conversion of softwood lignocellulose by poly(ethylene glycol) addition
    • Börjesson J., Peterson R., and Tjerneld F. Enhanced enzymatic conversion of softwood lignocellulose by poly(ethylene glycol) addition. Enzyme Microb Technol 40 (2007) 754-762
    • (2007) Enzyme Microb Technol , vol.40 , pp. 754-762
    • Börjesson, J.1    Peterson, R.2    Tjerneld, F.3
  • 7
    • 0001259497 scopus 로고    scopus 로고
    • Lignin impact on fiber degradation. 3. Reversal of inhibition of enzymatic hydrolysis by chemical modification of lignin and by additives
    • Sewalt V.J.H., Glasser W.G., and Beauchemin K.A. Lignin impact on fiber degradation. 3. Reversal of inhibition of enzymatic hydrolysis by chemical modification of lignin and by additives. J Agric Food Chem 45 5 (1997) 1823-1828
    • (1997) J Agric Food Chem , vol.45 , Issue.5 , pp. 1823-1828
    • Sewalt, V.J.H.1    Glasser, W.G.2    Beauchemin, K.A.3
  • 9
    • 0346363683 scopus 로고    scopus 로고
    • Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin
    • Palonen H., Tjerneld F., Zacchi G., and Tenkanen M. Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin. J Biotechnol 107 1 (2004) 65-72
    • (2004) J Biotechnol , vol.107 , Issue.1 , pp. 65-72
    • Palonen, H.1    Tjerneld, F.2    Zacchi, G.3    Tenkanen, M.4
  • 10
    • 18844427544 scopus 로고    scopus 로고
    • Weak lignin-binding enzymes-a novel approach to improve activity of cellulases for hydrolysis of lignocellulosics
    • Berlin A., Gilkes N., Kurabi A., Bura R., Tu M.B., Kilburn D., et al. Weak lignin-binding enzymes-a novel approach to improve activity of cellulases for hydrolysis of lignocellulosics. Appl Biochem Biotechnol 121 (2005) 163-170
    • (2005) Appl Biochem Biotechnol , vol.121 , pp. 163-170
    • Berlin, A.1    Gilkes, N.2    Kurabi, A.3    Bura, R.4    Tu, M.B.5    Kilburn, D.6
  • 11
    • 33746901704 scopus 로고    scopus 로고
    • Inhibition of cellulase, xylanase and [beta]-glucosidase activities by softwood lignin preparations
    • Berlin A., Balakshin M., Gilkes N., Kadla J., Maximenko V., Kubo S., et al. Inhibition of cellulase, xylanase and [beta]-glucosidase activities by softwood lignin preparations. J Biotechnol 125 2 (2006) 198-209
    • (2006) J Biotechnol , vol.125 , Issue.2 , pp. 198-209
    • Berlin, A.1    Balakshin, M.2    Gilkes, N.3    Kadla, J.4    Maximenko, V.5    Kubo, S.6
  • 12
    • 0016984999 scopus 로고
    • Upper and lower critical solution temperatures in poly(ethylene glycol) solutions
    • Saeki S., Kuwahara N., Nakata M., and Kaneko M. Upper and lower critical solution temperatures in poly(ethylene glycol) solutions. Polymer 17 8 (1976) 685-689
    • (1976) Polymer , vol.17 , Issue.8 , pp. 685-689
    • Saeki, S.1    Kuwahara, N.2    Nakata, M.3    Kaneko, M.4
  • 13
    • 33845378357 scopus 로고
    • A new model for upper and lower critical solution temperatures in poly(ethylene oxide) solutions
    • Karlstrom G. A new model for upper and lower critical solution temperatures in poly(ethylene oxide) solutions. J Phys Chem 89 23 (1985) 4962-4964
    • (1985) J Phys Chem , vol.89 , Issue.23 , pp. 4962-4964
    • Karlstrom, G.1
  • 14
    • 36448929608 scopus 로고
    • Water-structure and changes in thermal-stability of the system poly(ethylene oxide)-water
    • Kjellander R., and Florin E. Water-structure and changes in thermal-stability of the system poly(ethylene oxide)-water. J Chem Soc Faraday Trans I 77 (1981) 2053-2077
    • (1981) J Chem Soc Faraday Trans I , vol.77 , pp. 2053-2077
    • Kjellander, R.1    Florin, E.2
  • 18
    • 0016219744 scopus 로고
    • Mechanism of enzymatic cellulose degradation-isolation and some properties of a beta-glucosidase from trichoderma-viride
    • Berghem L.E.R., and Pettersson L.G. Mechanism of enzymatic cellulose degradation-isolation and some properties of a beta-glucosidase from trichoderma-viride. Eur J Biochem 46 2 (1974) 295-305
    • (1974) Eur J Biochem , vol.46 , Issue.2 , pp. 295-305
    • Berghem, L.E.R.1    Pettersson, L.G.2
  • 19
    • 0342786339 scopus 로고    scopus 로고
    • Modification of hardwood dissolving pulp with purified Trichoderma reesei cellulases
    • Rahkamo L., Siika-aho M., Vehviläinen M., Dolk M., Viikari L., Nousianen P., et al. Modification of hardwood dissolving pulp with purified Trichoderma reesei cellulases. Cellulose 3 (1996) 153-163
    • (1996) Cellulose , vol.3 , pp. 153-163
    • Rahkamo, L.1    Siika-aho, M.2    Vehviläinen, M.3    Dolk, M.4    Viikari, L.5    Nousianen, P.6
  • 20
    • 0034204550 scopus 로고    scopus 로고
    • Trichoderma reesei cellulases and their core domain in the hydrolysis and modification of chemical pulp
    • Suurnäkki A., Tenkanen M., Siika-aho M., Niku-Pavola M.-L., Viikari L., and Buchert J. Trichoderma reesei cellulases and their core domain in the hydrolysis and modification of chemical pulp. Cellulose 7 (2000) 189-209
    • (2000) Cellulose , vol.7 , pp. 189-209
    • Suurnäkki, A.1    Tenkanen, M.2    Siika-aho, M.3    Niku-Pavola, M.-L.4    Viikari, L.5    Buchert, J.6
  • 21
    • 0035805435 scopus 로고    scopus 로고
    • Genetic engineering of the Trichoderma reesei endoglucanase I (Cel7B) for enhanced partitioning in aqueous two-phase systems containing thermoseparating ethylene oxide-propylene oxide copolymers
    • Collén A., Ward M., Tjerneld F., and Stalbrand H. Genetic engineering of the Trichoderma reesei endoglucanase I (Cel7B) for enhanced partitioning in aqueous two-phase systems containing thermoseparating ethylene oxide-propylene oxide copolymers. J Biotechnol 87 2 (2001) 179-191
    • (2001) J Biotechnol , vol.87 , Issue.2 , pp. 179-191
    • Collén, A.1    Ward, M.2    Tjerneld, F.3    Stalbrand, H.4
  • 22
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric-focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff V., Arold N., Taube D., and Ehrhardt W. Improved staining of proteins in polyacrylamide gels including isoelectric-focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9 6 (1988) 255-262
    • (1988) Electrophoresis , vol.9 , Issue.6 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 23
    • 0032708967 scopus 로고    scopus 로고
    • Dynamic interaction of Trichoderma reesei cellobiohydrolases Cel6A and Cel7A and cellulose at equilibrium and during hydrolysis
    • Palonen H., Tenkanen M., and Linder M. Dynamic interaction of Trichoderma reesei cellobiohydrolases Cel6A and Cel7A and cellulose at equilibrium and during hydrolysis. Appl Environ Microbiol 65 (1999) 5229-5233
    • (1999) Appl Environ Microbiol , vol.65 , pp. 5229-5233
    • Palonen, H.1    Tenkanen, M.2    Linder, M.3
  • 24
    • 0032526793 scopus 로고    scopus 로고
    • Effect of chain density on inhibition of protein adsorption by poly(ethylene glycol) based coatings
    • Malmsten M., Emoto K., and Alstine J.M. Effect of chain density on inhibition of protein adsorption by poly(ethylene glycol) based coatings. J Colloid Interf Sci 202 (1998) 507-517
    • (1998) J Colloid Interf Sci , vol.202 , pp. 507-517
    • Malmsten, M.1    Emoto, K.2    Alstine, J.M.3
  • 25
    • 0026122420 scopus 로고
    • Protein surface interactions in the presence of polyethylene oxide. 1. Simplified theory
    • Jeon S.I., Lee J.H., Andrade J.D., and Degennes P.G. Protein surface interactions in the presence of polyethylene oxide. 1. Simplified theory. J Colloid Interf Sci 142 1 (1991) 149-158
    • (1991) J Colloid Interf Sci , vol.142 , Issue.1 , pp. 149-158
    • Jeon, S.I.1    Lee, J.H.2    Andrade, J.D.3    Degennes, P.G.4
  • 26
    • 0026118420 scopus 로고
    • Protein surface interactions in the presence of polyethylene oxide. 2. Effect of protein size
    • Jeon S.I., and Andrade J.D. Protein surface interactions in the presence of polyethylene oxide. 2. Effect of protein size. J Colloid Interf Sci 142 1 (1991) 159-166
    • (1991) J Colloid Interf Sci , vol.142 , Issue.1 , pp. 159-166
    • Jeon, S.I.1    Andrade, J.D.2
  • 27
    • 0000472757 scopus 로고    scopus 로고
    • Chemistry of lignin
    • Hon D.N.-S., and Shiraishi N. (Eds), Marcel Dekker Inc., New York
    • Sakakibara A., and Sano Y. Chemistry of lignin. In: Hon D.N.-S., and Shiraishi N. (Eds). Wood and cellulosic chemistry. 2nd ed. (2001), Marcel Dekker Inc., New York 109-173
    • (2001) Wood and cellulosic chemistry. 2nd ed. , pp. 109-173
    • Sakakibara, A.1    Sano, Y.2
  • 28
    • 0026923132 scopus 로고
    • Self-assembly in aqueous block copolymer solutions
    • Malmsten M., and Lindman B. Self-assembly in aqueous block copolymer solutions. Macromolecules 25 20 (1992) 5440-5445
    • (1992) Macromolecules , vol.25 , Issue.20 , pp. 5440-5445
    • Malmsten, M.1    Lindman, B.2
  • 29
    • 0002445915 scopus 로고
    • Structure of adsorbed and desorbed proteins
    • Norde W., and Favier J.P. Structure of adsorbed and desorbed proteins. Colloid Surf 64 1 (1992) 87-93
    • (1992) Colloid Surf , vol.64 , Issue.1 , pp. 87-93
    • Norde, W.1    Favier, J.P.2
  • 30
    • 0000293756 scopus 로고
    • Effects of plasma-protein adsorption on protein conformation and activity
    • Andrade J.D., Hlady V.L., and Vanwagenen R.A. Effects of plasma-protein adsorption on protein conformation and activity. Pure Appl Chem 56 10 (1984) 1345-1350
    • (1984) Pure Appl Chem , vol.56 , Issue.10 , pp. 1345-1350
    • Andrade, J.D.1    Hlady, V.L.2    Vanwagenen, R.A.3
  • 31
    • 21844472999 scopus 로고    scopus 로고
    • Reduction of irreversible protein adsorption on solid surfaces by protein engineering for increased stability
    • Karlsson M., Ekeroth J., Elwing H., and Carlsson U. Reduction of irreversible protein adsorption on solid surfaces by protein engineering for increased stability. J Biol Chem 280 27 (2005) 25558-25564
    • (2005) J Biol Chem , vol.280 , Issue.27 , pp. 25558-25564
    • Karlsson, M.1    Ekeroth, J.2    Elwing, H.3    Carlsson, U.4
  • 32
    • 0000288652 scopus 로고
    • Thermal denaturation of Trichoderma reesei cellulases studied by differential scanning calorimetry and tryptophan fluorescence
    • Baker J.O., Tatsumoto K., Grohmann K., Woodward J., Wichert J.M., Shoemaker S.P., et al. Thermal denaturation of Trichoderma reesei cellulases studied by differential scanning calorimetry and tryptophan fluorescence. Appl Biochem Biotechnol 34-5 (1992) 217-231
    • (1992) Appl Biochem Biotechnol , vol.34-5 , pp. 217-231
    • Baker, J.O.1    Tatsumoto, K.2    Grohmann, K.3    Woodward, J.4    Wichert, J.M.5    Shoemaker, S.P.6
  • 33
    • 0027968302 scopus 로고
    • The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei
    • Divne C., Ståhlberg J., Reinikainen T., Ruohonen L., Pettersson G., Knowles J.K.C., et al. The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science 265 (1994) 524-528
    • (1994) Science , vol.265 , pp. 524-528
    • Divne, C.1    Ståhlberg, J.2    Reinikainen, T.3    Ruohonen, L.4    Pettersson, G.5    Knowles, J.K.C.6
  • 34
    • 0343554779 scopus 로고    scopus 로고
    • Trichoderma reesei cellobiohydrolase I with an endoglucanase cellulose-binding domain: action on bacterial microcrystalline cellulose
    • Srisodsuk M., Lehtiö J., Linder M., Margolles-Clark E., Reinikainen T., and Teeri T.T. Trichoderma reesei cellobiohydrolase I with an endoglucanase cellulose-binding domain: action on bacterial microcrystalline cellulose. J Biotechnol 57 (1997) 49-57
    • (1997) J Biotechnol , vol.57 , pp. 49-57
    • Srisodsuk, M.1    Lehtiö, J.2    Linder, M.3    Margolles-Clark, E.4    Reinikainen, T.5    Teeri, T.T.6
  • 35
    • 0024962351 scopus 로고
    • Determination of the 3-dimensional solution structure of the C-terminal domain of cellobiohydrolase-I from Trichoderma reesei-a study using nuclear magnetic resonance and hybrid distance geometry dynamical simulated annealing
    • Kraulis P.J., Clore G.M., Nilges M., Jones T.A., Pettersson G., Knowles J., et al. Determination of the 3-dimensional solution structure of the C-terminal domain of cellobiohydrolase-I from Trichoderma reesei-a study using nuclear magnetic resonance and hybrid distance geometry dynamical simulated annealing. Biochemistry 28 18 (1989) 7241-7257
    • (1989) Biochemistry , vol.28 , Issue.18 , pp. 7241-7257
    • Kraulis, P.J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6
  • 36
    • 0029155995 scopus 로고
    • Molecular dynamics simulation of fungal cellulose-binding domains: differences in molecular rigidity but a preserved cellulose binding surface
    • Hoffrén A.-M., Teeri T.T., and Teleman O. Molecular dynamics simulation of fungal cellulose-binding domains: differences in molecular rigidity but a preserved cellulose binding surface. Protein Eng 8 (1995) 443-450
    • (1995) Protein Eng , vol.8 , pp. 443-450
    • Hoffrén, A.-M.1    Teeri, T.T.2    Teleman, O.3
  • 37
    • 34248164817 scopus 로고    scopus 로고
    • DeLano WL. The PyMOL molecular graphics system. San Carlos, CA, USA: DeLano Scientific; 2002. http://www.pymol.org.
  • 38
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 15 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 39
    • 0029119131 scopus 로고
    • The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution
    • Linder M., Lindeberg G., Reinikainen T., Teeri T.T., and Pettersson G. The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution. FEBS Lett 372 (1995) 96-98
    • (1995) FEBS Lett , vol.372 , pp. 96-98
    • Linder, M.1    Lindeberg, G.2    Reinikainen, T.3    Teeri, T.T.4    Pettersson, G.5
  • 40
    • 0024278357 scopus 로고
    • Hydrophilicity of polar amino-acid side-chains is markedly reduced by flanking peptide-bonds
    • Roseman M.A. Hydrophilicity of polar amino-acid side-chains is markedly reduced by flanking peptide-bonds. J Mol Biol 200 3 (1988) 513-522
    • (1988) J Mol Biol , vol.200 , Issue.3 , pp. 513-522
    • Roseman, M.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.