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Volumn 146, Issue , 2013, Pages 118-125

Effect of temperature on lignin-derived inhibition studied with three structurally different cellobiohydrolases

Author keywords

Adsorption; Cellulase; Enzymatic hydrolysis; Enzyme stability; Lignin

Indexed keywords

ADSORPTION; ENZYMATIC HYDROLYSIS; ENZYME INHIBITION; TEMPERATURE;

EID: 84881225487     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2013.07.069     Document Type: Article
Times cited : (47)

References (35)
  • 1
    • 0019554715 scopus 로고
    • Induction, isolation and testing of stable Trichoderma reesei mutants with improved production of solubilizing cellulase
    • Bailey M.J., Nevalainen K.M.H. Induction, isolation and testing of stable Trichoderma reesei mutants with improved production of solubilizing cellulase. Enzyme Microb. Technol. 1981, 3:153-157.
    • (1981) Enzyme Microb. Technol. , vol.3 , pp. 153-157
    • Bailey, M.J.1    Nevalainen, K.M.H.2
  • 2
    • 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., Kilburn D., Saddler J. Weak lignin-binding enzymes-a novel approach to improve activity of cellulases for hydrolysis of lignocellulosics. Appl. Biochem. Biotechnol. 2005, 121:163-170.
    • (2005) Appl. Biochem. Biotechnol. , vol.121 , pp. 163-170
    • Berlin, A.1    Gilkes, N.2    Kurabi, A.3    Bura, R.4    Tu, M.5    Kilburn, D.6    Saddler, J.7
  • 3
    • 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
  • 4
    • 34248205049 scopus 로고    scopus 로고
    • Effect of poly(ethylene glycol) on enzymatic hydrolysis and adsorption of cellulase enzymes to pretreated lignocelluloses
    • Börjesson J., Engqvist M., Sipos B., Tjerneld F. Effect of poly(ethylene glycol) on enzymatic hydrolysis and adsorption of cellulase enzymes to pretreated lignocelluloses. Enzyme Microb. Technol. 2007, 41:186-195.
    • (2007) Enzyme Microb. Technol. , vol.41 , pp. 186-195
    • Börjesson, J.1    Engqvist, M.2    Sipos, B.3    Tjerneld, F.4
  • 5
    • 0034641715 scopus 로고    scopus 로고
    • Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose
    • Carrard G., Koivula A., Söderlund H., Béguin P. Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose. PNAS 2000, 97:10342-10347.
    • (2000) PNAS , vol.97 , pp. 10342-10347
    • Carrard, G.1    Koivula, A.2    Söderlund, H.3    Béguin, P.4
  • 6
    • 0024060779 scopus 로고
    • Adsorption of high-purity endo-1,4-β-glucanases from Trichoderma reesei on components of lignocellulosic materials: cellulose lignin and xylan
    • Chernoglazov V.M., Ermolova O.V., Klyosov A.A. Adsorption of high-purity endo-1,4-β-glucanases from Trichoderma reesei on components of lignocellulosic materials: cellulose lignin and xylan. Enzyme Microb. Technol. 1988, 10:503-507.
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 503-507
    • Chernoglazov, V.M.1    Ermolova, O.V.2    Klyosov, A.A.3
  • 8
    • 73149101268 scopus 로고    scopus 로고
    • Inhibition performance of lignocellulose degradation products on industrial cellulase enzymes during cellulose hydrolysis
    • Jing X., Zhang X., Bao J. Inhibition performance of lignocellulose degradation products on industrial cellulase enzymes during cellulose hydrolysis. Appl. Biochem. Biotechnol. 2009, 159:696-707.
    • (2009) Appl. Biochem. Biotechnol. , vol.159 , pp. 696-707
    • Jing, X.1    Zhang, X.2    Bao, J.3
  • 9
    • 0024962351 scopus 로고
    • Determination of the three-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 M., Nilges M., Jones T.A., Pettersson G., Knowles J., Gronenborn A.M. Determination of the three-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 1989, 28:7241-7257.
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, P.J.1    Clore, M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 10
    • 0015333650 scopus 로고
    • A new reaction for colorimeric determination of carbohydrates
    • Lever M. A new reaction for colorimeric determination of carbohydrates. Anal. Biochem. 1972, 47:276-279.
    • (1972) Anal. Biochem. , vol.47 , pp. 276-279
    • Lever, M.1
  • 11
    • 0029861144 scopus 로고    scopus 로고
    • The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose
    • Linder M., Teeri T.T. The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose. PNAS 1996, 93:12251-12255.
    • (1996) PNAS , vol.93 , pp. 12251-12255
    • Linder, M.1    Teeri, T.T.2
  • 12
    • 0036240767 scopus 로고    scopus 로고
    • Cellulase adsorption and an evaluation of enzyme recycle during hydrolysis of steam-exploded softwood residues
    • Lu Y.P., Yang B., Gregg D., Saddler J.N., Mansfield S.D. Cellulase adsorption and an evaluation of enzyme recycle during hydrolysis of steam-exploded softwood residues. Appl. Biochem. Biotechnol. 2002, 98-100:641-654.
    • (2002) Appl. Biochem. Biotechnol. , pp. 641-654
    • Lu, Y.P.1    Yang, B.2    Gregg, D.3    Saddler, J.N.4    Mansfield, S.D.5
  • 13
    • 0029270809 scopus 로고
    • Structural stability effects on the adsorption and dodecyltrimethylammonium bromide-mediated elutability of bacteriophage T4 lysozyme at silica surfaces
    • McGuire J., Wahlgren M.C., Arnebrant T. Structural stability effects on the adsorption and dodecyltrimethylammonium bromide-mediated elutability of bacteriophage T4 lysozyme at silica surfaces. J. Colloid Interface Sci. 1995, 170:182-192.
    • (1995) J. Colloid Interface Sci. , vol.170 , pp. 182-192
    • McGuire, J.1    Wahlgren, M.C.2    Arnebrant, T.3
  • 14
    • 0028765765 scopus 로고
    • Adsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline cellulose
    • Medve J., Ståhlberg J., Tjerneld F. Adsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline cellulose. Biotechnol. Bioeng. 1994, 44:1064-1073.
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 1064-1073
    • Medve, J.1    Ståhlberg, J.2    Tjerneld, F.3
  • 15
    • 0032079694 scopus 로고    scopus 로고
    • The effect of initial pore volume and lignin content on the enzymatic hydrolysis of softwoods
    • Mooney C.A., Mansfield S.D., Touhy M.G., Saddler J.N. The effect of initial pore volume and lignin content on the enzymatic hydrolysis of softwoods. Bioresour. Technol. 1998, 64:113-119.
    • (1998) Bioresour. Technol. , vol.64 , pp. 113-119
    • Mooney, C.A.1    Mansfield, S.D.2    Touhy, M.G.3    Saddler, J.N.4
  • 17
    • 78751473033 scopus 로고    scopus 로고
    • Enhancing the enzymatic hydrolysis of lignocellulosic biomass by increasing the carboxylic acid content of the associated lignin
    • Nakagame S., Chandra R.P., Kadla J.F., Saddler J.N. Enhancing the enzymatic hydrolysis of lignocellulosic biomass by increasing the carboxylic acid content of the associated lignin. Biotechnol. Bioeng. 2011, 108:538-548.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 538-548
    • Nakagame, S.1    Chandra, R.P.2    Kadla, J.F.3    Saddler, J.N.4
  • 18
    • 77949370529 scopus 로고    scopus 로고
    • The effect of isolated lignins, obtained from a range of pretreated lignocellulosic substrates, on enzymatic hydrolysis
    • Nakagame S., Chandra R.P., Saddler J.N. The effect of isolated lignins, obtained from a range of pretreated lignocellulosic substrates, on enzymatic hydrolysis. Biotechnol. Bioeng. 2010, 105:871-879.
    • (2010) Biotechnol. Bioeng. , vol.105 , pp. 871-879
    • Nakagame, S.1    Chandra, R.P.2    Saddler, J.N.3
  • 19
    • 44049111617 scopus 로고
    • Adsorption, desorption and re-adsorption of proteins on solid surfaces
    • Norde W., Anusiem A.C.I. Adsorption, desorption and re-adsorption of proteins on solid surfaces. Colloids Surf. 1992, 66:73-80.
    • (1992) Colloids Surf. , vol.66 , pp. 73-80
    • Norde, W.1    Anusiem, A.C.I.2
  • 20
    • 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., Tenkanen M. Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin. J. Biotechnol. 2004, 107:65-72.
    • (2004) J. Biotechnol. , vol.107 , pp. 65-72
    • Palonen, H.1    Tjerneld, F.2    Zacchi, G.3    Tenkanen, M.4
  • 21
    • 63949083111 scopus 로고    scopus 로고
    • Optimization of hydrothermal pretreatment of wheat straw for production of bioethanol at low water consumption without addition of chemicals
    • Petersen Ø.M., Larsen J., Thomsen M.H. Optimization of hydrothermal pretreatment of wheat straw for production of bioethanol at low water consumption without addition of chemicals. Biomass Bioenergy 2009, 33:834-840.
    • (2009) Biomass Bioenergy , vol.33 , pp. 834-840
    • Petersen, O.M.1    Larsen, J.2    Thomsen, M.H.3
  • 22
    • 80054037883 scopus 로고    scopus 로고
    • Inhibition of enzymatic hydrolysis by residual lignins from softwood-study of enzyme binding and inactivation on lignin-rich surface
    • Rahikainen J., Mikander S., Marjamaa K., Tamminen T., Lappas A., Viikari L., Kruus K. Inhibition of enzymatic hydrolysis by residual lignins from softwood-study of enzyme binding and inactivation on lignin-rich surface. Biotechnol. Bioeng. 2011, 108:2823-2834.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 2823-2834
    • Rahikainen, J.1    Mikander, S.2    Marjamaa, K.3    Tamminen, T.4    Lappas, A.5    Viikari, L.6    Kruus, K.7
  • 25
    • 0022944447 scopus 로고
    • The role of lignin in the adsorption of cellulases during enzymatic treatment of lignocellulosic material
    • Sutcliffe R., Saddler J.N. The role of lignin in the adsorption of cellulases during enzymatic treatment of lignocellulosic material. Biotechnol. Bioeng. Symp. 1986, 17:749-762.
    • (1986) Biotechnol. Bioeng. Symp. , vol.17 , pp. 749-762
    • Sutcliffe, R.1    Saddler, J.N.2
  • 26
    • 0034629241 scopus 로고    scopus 로고
    • An α-glucuronidase of Schizophyllum commune acting on polymeric xylan
    • Tenkanen M., Siika-aho M. An α-glucuronidase of Schizophyllum commune acting on polymeric xylan. J. Biotechnol. 2000, 78:149-161.
    • (2000) J. Biotechnol. , vol.78 , pp. 149-161
    • Tenkanen, M.1    Siika-aho, M.2
  • 27
    • 0029955959 scopus 로고    scopus 로고
    • Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose
    • Tormo J., Lamed R., Chirino A.J., Morag E., Bayer E.A., Shoham Y., Steitz T.A. Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J. 1996, 15:5739-5751.
    • (1996) EMBO J. , vol.15 , pp. 5739-5751
    • Tormo, J.1    Lamed, R.2    Chirino, A.J.3    Morag, E.4    Bayer, E.A.5    Shoham, Y.6    Steitz, T.A.7
  • 28
    • 69949161629 scopus 로고    scopus 로고
    • Adsorption of cellulase on cellulolytic enzyme lignin from lodgepole pine
    • Tu M., Pan X., Saddler J.N. Adsorption of cellulase on cellulolytic enzyme lignin from lodgepole pine. J. Agric. Food Chem. 2009, 57:7771-7778.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 7771-7778
    • Tu, M.1    Pan, X.2    Saddler, J.N.3
  • 30
    • 74149088159 scopus 로고    scopus 로고
    • Restriction of the enzymatic hydrolysis of steam-pretreated spruce by lignin and hemicellulose
    • Várnai A., Siika-aho M., Viikari L. Restriction of the enzymatic hydrolysis of steam-pretreated spruce by lignin and hemicellulose. Enzyme Microb. Technol. 2010, 46:185-193.
    • (2010) Enzyme Microb. Technol. , vol.46 , pp. 185-193
    • Várnai, A.1    Siika-aho, M.2    Viikari, L.3
  • 31
    • 78650714894 scopus 로고    scopus 로고
    • Adsorption of monocomponent enzymes in enzyme mixture analyzed quantitatively during hydrolysis of lignocellulose substrates
    • Várnai A., Viikari L., Marjamaa K., Siika-aho M. Adsorption of monocomponent enzymes in enzyme mixture analyzed quantitatively during hydrolysis of lignocellulose substrates. Bioresour. Technol. 2011, 102:1220-1227.
    • (2011) Bioresour. Technol. , vol.102 , pp. 1220-1227
    • Várnai, A.1    Viikari, L.2    Marjamaa, K.3    Siika-aho, M.4
  • 33
    • 84881222591 scopus 로고    scopus 로고
    • Fungal thermostable cellobiohydrolases: characterization and protein engineering studies
    • Ph.D. Thesis. VTT Publications 754, Espoo.
    • Voutilainen, S., 2011. Fungal thermostable cellobiohydrolases: characterization and protein engineering studies. Ph.D. Thesis. VTT Publications 754, Espoo.
    • (2011)
    • Voutilainen, S.1
  • 34
    • 75649132219 scopus 로고    scopus 로고
    • Expression of Talaromyces emersonii cellobiohydrolase Cel7A in Saccharomyces cerevisiae and rational mutagenesis to improve its thermostability and activity
    • Voutilainen S., Murray P.G., Tuohy M.G., Koivula A. Expression of Talaromyces emersonii cellobiohydrolase Cel7A in Saccharomyces cerevisiae and rational mutagenesis to improve its thermostability and activity. Protein Eng. Des. Sel. 2010, 23:69-79.
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 69-79
    • Voutilainen, S.1    Murray, P.G.2    Tuohy, M.G.3    Koivula, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.