메뉴 건너뛰기




Volumn 8, Issue 11, 2013, Pages

Improved activity of a thermophilic cellulase, Cel5A, from Thermotoga maritima on ionic liquid pretreated switchgrass

Author keywords

[No Author keywords available]

Indexed keywords

CELLULASE; ENDOGLUCANASE CEL5A; IONIC LIQUID;

EID: 84893660324     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0079725     Document Type: Article
Times cited : (28)

References (57)
  • 1
    • 70349281876 scopus 로고    scopus 로고
    • Engineering for biofuels: Exploiting innate microbial capacity or importing biosynthetic potential?
    • doi:10.1038/nrmicro2186
    • Alper H, Stephanopoulos G (2009) Engineering for biofuels: exploiting innate microbial capacity or importing biosynthetic potential? Nat Rev Micro 7: 715-723. doi:10.1038/nrmicro2186.
    • (2009) Nat Rev Micro , vol.7 , pp. 715-723
    • Alper, H.1    Stephanopoulos, G.2
  • 2
    • 79952128475 scopus 로고    scopus 로고
    • Climate change and evolutionary adaptation
    • doi:10.1038/nature09670
    • Hoffmann AA, Sgrò CM (2011) Climate change and evolutionary adaptation. Nature 470: 479-485. doi:10.1038/nature09670.
    • (2011) Nature , vol.470 , pp. 479-485
    • Hoffmann, A.A.1    Sgrò, C.M.2
  • 3
    • 77956299931 scopus 로고    scopus 로고
    • Deep-sea oil plume enriches indigenous oil-degrading bacteria
    • doi:10.1126/science.1195979
    • Hazen TC, Dubinsky EA, DeSantis TZ, Andersen GL, Piceno YM, et al. (2010) Deep-sea oil plume enriches indigenous oil-degrading bacteria. Science 330: 204-208. doi:10.1126/science.1195979.
    • (2010) Science , vol.330 , pp. 204-208
    • Hazen, T.C.1    Dubinsky, E.A.2    DeSantis, T.Z.3    Andersen, G.L.4    Piceno, Y.M.5
  • 4
    • 78650155069 scopus 로고    scopus 로고
    • Biofuels: Biomolecular engineering fundamentals and advances
    • doi:10.1146/annurev-chembioeng-073009-100938
    • Li H, Cann AF, Liao JC (2010) Biofuels: biomolecular engineering fundamentals and advances. Annu Rev Chem Biomol Eng 1: 19-36. doi:10.1146/annurev-chembioeng-073009-100938.
    • (2010) Annu Rev Chem Biomol Eng , vol.1 , pp. 19-36
    • Li, H.1    Cann, A.F.2    Liao, J.C.3
  • 5
    • 75749125061 scopus 로고    scopus 로고
    • Microbial production of fatty-acid-derived fuels and chemicals from plant biomass
    • doi:10.1038/nature08721
    • Steen EJ, Kang Y, Bokinsky G, Hu Z, Schirmer A, et al. (2010) Microbial production of fatty-acid-derived fuels and chemicals from plant biomass. Nature 463: 559-562. doi:10.1038/nature08721.
    • (2010) Nature , vol.463 , pp. 559-562
    • Steen, E.J.1    Kang, Y.2    Bokinsky, G.3    Hu, Z.4    Schirmer, A.5
  • 6
    • 31544452808 scopus 로고    scopus 로고
    • The Path Forward for Biofuels and Biomaterials
    • doi:10.1126/science.1114736
    • Ragauskas AJ (2006) The Path Forward for Biofuels and Biomaterials. Science 311: 484-489. doi:10.1126/science.1114736.
    • (2006) Science , vol.311 , pp. 484-489
    • Ragauskas, A.J.1
  • 7
    • 77949519739 scopus 로고    scopus 로고
    • Fermentable sugars by chemical hydrolysis of biomass
    • doi:10.1073/pnas.0912073107
    • Binder JB, Raines RT (2010) Fermentable sugars by chemical hydrolysis of biomass. Proceedings of the National Academy of Sciences 107: 4516-4521. doi:10.1073/pnas.0912073107.
    • (2010) Proceedings of the National Academy of Sciences , vol.107 , pp. 4516-4521
    • Binder, J.B.1    Raines, R.T.2
  • 9
    • 23844474092 scopus 로고    scopus 로고
    • Combined sugar yields for dilute sulfuric acid pretreatment of corn stover followed by enzymatic hydrolysis of the remaining solids
    • DOI 10.1016/j.biortech.2005.01.011, PII S0960852405000647
    • Lloyd TA, Wyman CE (2005) Combined sugar yields for dilute sulfuric acid pretreatment of corn stover followed by enzymatic hydrolysis of the remaining solids. Bioresour Technol 96: 1967-1977. doi:10.1016/j.biortech.2005.01.011. (Pubitemid 41174566)
    • (2005) Bioresource Technology , vol.96 , Issue.18 SPEC. ISS. , pp. 1967-1977
    • Lloyd, T.A.1    Wyman, C.E.2
  • 10
    • 23844533296 scopus 로고    scopus 로고
    • Optimization of the ammonia fiber explosion (AFEX) treatment parameters for enzymatic hydrolysis of corn stover
    • DOI 10.1016/j.biortech.2005.01.016, PII S0960852405000696
    • Teymouri F, Laureano-Perez L, Alizadeh H, Dale BE (2005) Optimization of the ammonia fiber explosion (AFEX) treatment parameters for enzymatic hydrolysis of corn stover. Bioresour Technol 96: 2014-2018. doi:10.1016/j.biortech.2005. 01.016. (Pubitemid 41174571)
    • (2005) Bioresource Technology , vol.96 , Issue.18 SPEC. ISS. , pp. 2014-2018
    • Teymouri, F.1    Laureano-Perez, L.2    Alizadeh, H.3    Dale, B.E.4
  • 11
    • 23844499442 scopus 로고    scopus 로고
    • Optimization of pH controlled liquid hot water pretreatment of corn stover
    • DOI 10.1016/j.biortech.2005.01.013, PII S0960852405000660
    • Mosier N, Hendrickson R, Ho N, Sedlak M, Ladisch MR (2005) Optimization of pH controlled liquid hot water pretreatment of corn stover. Bioresour Technol 96: 1986-1993. doi:10.1016/j.biortech.2005.01.013. (Pubitemid 41174568)
    • (2005) Bioresource Technology , vol.96 , Issue.18 SPEC. ISS. , pp. 1986-1993
    • Mosier, N.1    Hendrickson, R.2    Ho, N.3    Sedlak, M.4    Ladisch, M.R.5
  • 12
    • 33947430562 scopus 로고    scopus 로고
    • Effect of hemicellulose and lignin removal on enzymatic hydrolysis of steam pretreated corn stover
    • DOI 10.1016/j.biortech.2006.09.003, PII S0960852406004573
    • Ohgren K, Bura R, Saddler J, Zacchi G (2007) Effect of hemicellulose and lignin removal on enzymatic hydrolysis of steam pretreated corn stover. Bioresour Technol 98: 2503-2510. doi:10.1016/j.biortech.2006.09.003. (Pubitemid 46453471)
    • (2007) Bioresource Technology , vol.98 , Issue.13 , pp. 2503-2510
    • Ohgren, K.1    Bura, R.2    Saddler, J.3    Zacchi, G.4
  • 13
    • 79956347286 scopus 로고    scopus 로고
    • Influence of physicochemical changes on enzymatic digestibility of ionic liquid and AFEX pretreated corn stover
    • Li C, Cheng G, Balan V, Kent MS, Ong M, et al. (2011) Influence of physicochemical changes on enzymatic digestibility of ionic liquid and AFEX pretreated corn stover. Bioresour Technol 102: 6928-69286936.
    • (2011) Bioresour Technol , vol.102 , pp. 6928-69286936
    • Li, C.1    Cheng, G.2    Balan, V.3    Kent, M.S.4    Ong, M.5
  • 14
    • 79959386497 scopus 로고    scopus 로고
    • Deconstruction of lignocellulosic biomass to fuels and chemicals
    • doi:10.1146/annurev-chembioeng-061010-114205
    • Chundawat SPS, Beckham GT, Himmel ME, Dale BE (2011) Deconstruction of lignocellulosic biomass to fuels and chemicals. Annu Rev Chem Biomol Eng 2: 121-145. doi:10.1146/annurev-chembioeng-061010-114205.
    • (2011) Annu Rev Chem Biomol Eng , vol.2 , pp. 121-145
    • Chundawat, S.P.S.1    Beckham, G.T.2    Himmel, M.E.3    Dale, B.E.4
  • 15
    • 33846951759 scopus 로고    scopus 로고
    • Biomass Recalcitrance: Engineering Plants and Enzymes for Biofuels Production
    • doi:10.1126/science.1137016
    • Himmel ME, Ding SY, Johnson DK, Adney WS, Nimlos MR, et al. (2007) Biomass Recalcitrance: Engineering Plants and Enzymes for Biofuels Production. Science 315: 804-807. doi:10.1126/science.1137016.
    • (2007) Science , vol.315 , pp. 804-807
    • Himmel, M.E.1    Ding, S.Y.2    Johnson, D.K.3    Adney, W.S.4    Nimlos, M.R.5
  • 16
    • 33746121105 scopus 로고    scopus 로고
    • Outlook for cellulase improvement: Screening and selection strategies
    • DOI 10.1016/j.biotechadv.2006.03.003, PII S0734975006000413
    • Percival Zhang YH, Himmel ME, Mielenz JR (2006) Outlook for cellulase improvement: screening and selection strategies. Biotechnol Adv 24: 452-481. doi:10.1016/j.biotechadv.2006.03.003. (Pubitemid 44082013)
    • (2006) Biotechnology Advances , vol.24 , Issue.5 , pp. 452-481
    • Percival, Z.Y.-H.1    Himmel, M.E.2    Mielenz, J.R.3
  • 18
    • 80052835619 scopus 로고    scopus 로고
    • Techno-economic analysis of a lignocellulosic ethanol biorefinery with ionic liquid pre-treatment. Biofuels
    • Klein Marcuschamer D, Simmons BA, Blanch HW (2011) Techno-economic analysis of a lignocellulosic ethanol biorefinery with ionic liquid pre-treatment. Biofuels, Bioproducts and Biorefining 5: 562-569.
    • (2011) Bioproducts and Biorefining , vol.5 , pp. 562-569
    • Klein Marcuschamer, D.1    Simmons, B.A.2    Blanch, H.W.3
  • 19
    • 76349088995 scopus 로고    scopus 로고
    • Ionic liquid tolerant hyperthermophilic cellulases for biomass pretreatment and hydrolysis
    • Datta S, Holmes B, Park JI, Chen Z, Dibble DC, et al. (2010) Ionic liquid tolerant hyperthermophilic cellulases for biomass pretreatment and hydrolysis. Green Chemistry 12: 338-345.
    • (2010) Green Chemistry , vol.12 , pp. 338-345
    • Datta, S.1    Holmes, B.2    Park, J.I.3    Chen, Z.4    Dibble, D.C.5
  • 20
    • 79955935759 scopus 로고    scopus 로고
    • Correlation between thermostability and stability of glycosidases in ionic liquid
    • doi:10.1007/s10529-011-0560-5
    • Ferdjani S, Ionita M, Roy B, Dion M, Djeghaba Z, et al. (2011) Correlation between thermostability and stability of glycosidases in ionic liquid. Biotechnol Lett 33: 1215-1219. doi:10.1007/s10529-011-0560-5.
    • (2011) Biotechnol Lett , vol.33 , pp. 1215-1219
    • Ferdjani, S.1    Ionita, M.2    Roy, B.3    Dion, M.4    Djeghaba, Z.5
  • 21
    • 70349765870 scopus 로고    scopus 로고
    • Protein engineering in designing tailored enzymes and microorganisms for biofuels production
    • doi:10.1016/j.copbio.2009.07.001
    • Wen F, Nair NU, Zhao H (2009) Protein engineering in designing tailored enzymes and microorganisms for biofuels production. Curr Opin Biotech 20: 412-419. doi:10.1016/j.copbio.2009.07.001.
    • (2009) Curr Opin Biotech , vol.20 , pp. 412-419
    • Wen, F.1    Nair, N.U.2    Zhao, H.3
  • 22
    • 0036372478 scopus 로고    scopus 로고
    • Thermostabilization of cellulosomal endoglucanase EngB from Clostridium cellulovorans by in vitro DNA recombination with non-cellulosomal endoglucanase EngD
    • DOI 10.1046/j.1365-2958.2002.03049.x
    • Murashima K, Kosugi A, Doi RH (2002) Thermostabilization of cellulosomal endoglucanase EngB from Clostridium cellulovorans by in vitro DNA recombination with non-cellulosomal endoglucanase EngD. Mol Microbiol 45: 617-626. (Pubitemid 34989171)
    • (2002) Molecular Microbiology , vol.45 , Issue.3 , pp. 617-626
    • Murashima, K.1    Kosugi, A.2    Doi, R.H.3
  • 23
    • 78650826462 scopus 로고    scopus 로고
    • Introduction of glycine and proline residues onto protein surface increases the thermostability of endoglucanase CelA from Clostridium thermocellum
    • doi:10.1016/j.biortech.2010.11.043
    • Yi ZL, Pei XQ, Wu ZL (2011) Introduction of glycine and proline residues onto protein surface increases the thermostability of endoglucanase CelA from Clostridium thermocellum. Bioresour Technol 102: 3636-3638. doi:10.1016/j. biortech.2010.11.043.
    • (2011) Bioresour Technol , vol.102 , pp. 3636-3638
    • Yi, Z.L.1    Pei, X.Q.2    Wu, Z.L.3
  • 24
    • 77954700415 scopus 로고    scopus 로고
    • Engineering of Clostridium phytofermentans Endoglucanase Cel5A for improved thermostability
    • doi:10.1128/AEM.00958-10
    • Liu W, Zhang XZ, Zhang Z, Zhang YHP (2010) Engineering of Clostridium phytofermentans Endoglucanase Cel5A for improved thermostability. Appl Environ Microbiol 76: 4914-4917. doi:10.1128/AEM.00958-10.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 4914-4917
    • Liu, W.1    Zhang, X.Z.2    Zhang, Z.3    Zhang, Y.H.P.4
  • 25
    • 79957475689 scopus 로고    scopus 로고
    • Directed evolution of a thermophilic endoglucanase (Cel5A) into highly active Cel5A variants with an expanded temperature profile
    • doi:10.1016/j.jbiotec.2011.03.025
    • Liang C, Fioroni M, Rodríguez-Ropero F, Xue Y, Schwaneberg U, et al. (2011) Directed evolution of a thermophilic endoglucanase (Cel5A) into highly active Cel5A variants with an expanded temperature profile. J Biotechnol 154: 46-53. doi:10.1016/j.jbiotec.2011.03.025.
    • (2011) J Biotechnol , vol.154 , pp. 46-53
    • Liang, C.1    Fioroni, M.2    Rodríguez-Ropero, F.3    Xue, Y.4    Schwaneberg, U.5
  • 26
    • 0033961548 scopus 로고    scopus 로고
    • Bacterial cell surface display of an enzyme library for selective screening of improved cellulase variants
    • Kim YS, Jung HC, Pan JG (2000) Bacterial cell surface display of an enzyme library for selective screening of improved cellulase variants. Appl Environ Microbiol 66: 788-793.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 788-793
    • Kim, Y.S.1    Jung, H.C.2    Pan, J.G.3
  • 27
    • 51349085542 scopus 로고    scopus 로고
    • Site-directed mutagenesis and CBM engineering of Cel5A (Thermotoga maritima)
    • doi:10.1111/j.1574-6968.2008.01324.x
    • Arumugam Mahadevan S, Gon Wi S, Lee DS, Bae -J (2008) Site-directed mutagenesis and CBM engineering of Cel5A (Thermotoga maritima). FEMS Microbiol Lett 287: 205-211. doi:10.1111/j.1574-6968.2008.01324.x.
    • (2008) FEMS Microbiol Lett , vol.287 , pp. 205-211
    • Arumugam Mahadevan, S.1    Gon Wi, S.2    Lee, D.S.B.-J.3
  • 28
    • 78449268868 scopus 로고    scopus 로고
    • Microfluidic glycosyl hydrolase screening for biomass-to-biofuel conversion
    • doi:10.1021/ac102243f
    • Bharadwaj R, Chen Z, Datta S, Holmes BM, Sapra R, et al. (2010) Microfluidic glycosyl hydrolase screening for biomass-to-biofuel conversion. Anal Chem 82: 9513-9520. doi:10.1021/ac102243f.
    • (2010) Anal Chem , vol.82 , pp. 9513-9520
    • Bharadwaj, R.1    Chen, Z.2    Datta, S.3    Holmes, B.M.4    Sapra, R.5
  • 29
    • 0036154307 scopus 로고    scopus 로고
    • Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides
    • DOI 10.1128/AEM.68.2.545-554.2002
    • Chhabra SR, Shockley KR, Ward DE, Kelly RM (2002) Regulation of endoacting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides. Appl Environ Microbiol 68: 545-554. (Pubitemid 34113039)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.2 , pp. 545-554
    • Chhabra, S.R.1    Shockley, K.R.2    Ward, D.E.3    Kelly, R.M.4
  • 30
    • 0037470149 scopus 로고    scopus 로고
    • Carbohydrate-induced differential gene expression patterns in the hyperthermophilic bacterium Thermotoga maritima
    • DOI 10.1074/jbc.M211748200
    • Chhabra SR, Shockley KR, Conners SB, Scott KL, Wolfinger RD, et al. (2003) Carbohydrate-induced differential gene expression patterns in the hyperthermophilic bacterium Thermotoga maritima. J Biol Chem 278: 7540-7552. doi:10.1074/jbc.M211748200. (Pubitemid 36800761)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 7540-7552
    • Chhabra, S.R.1    Shockley, K.R.2    Conners, S.B.3    Scott, K.L.4    Wolfinger, R.D.5    Kelly, R.M.6
  • 31
    • 77958177184 scopus 로고    scopus 로고
    • Biochemical characterization and crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima
    • doi:10.1016/j.jsb.2010.06.018
    • Pereira JH, Chen Z, McAndrew RP, Sapra R, Chhabra SR, et al. (2010) Biochemical characterization and crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima. J Struct Biol 172: 372-379. doi:10.1016/j.jsb.2010.06.018.
    • (2010) J Struct Biol , vol.172 , pp. 372-379
    • Pereira, J.H.1    Chen, Z.2    McAndrew, R.P.3    Sapra, R.4    Chhabra, S.R.5
  • 32
    • 84864095374 scopus 로고    scopus 로고
    • Tracing determinants of dual substrate specificity in glycoside hydrolase family 5
    • doi:10.1074/jbc.M112.362640
    • Chen Z, Friedland GD, Pereira JH, Reveco SA, Chan R, et al. (2012) Tracing determinants of dual substrate specificity in glycoside hydrolase family 5. Journal of Biological Chemistry 287: 25335-25343. doi:10.1074/jbc.M112. 362640.
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 25335-25343
    • Chen, Z.1    Friedland, G.D.2    Pereira, J.H.3    Reveco, S.A.4    Chan, R.5
  • 33
    • 1642445607 scopus 로고    scopus 로고
    • Improved Catalytic Efficiency and Active Site Modification of 1,4-beta-D-Glucan Glucohydrolase A from Thermotoga neapolitana by Directed Evolution
    • DOI 10.1074/jbc.M305642200
    • McCarthy JK, Uzelac A, Davis DF, Eveleigh DE (2004) Improved catalytic efficiency and active site modification of 1,4-beta-D-glucan glucohydrolase A from Thermotoga neapolitana by directed evolution. J Biol Chem 279: 11495-11502. doi:10.1074/jbc.M305642200. (Pubitemid 38404277)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.12 , pp. 11495-11502
    • McCarthy, J.K.1    Uzelac, A.2    Davis, D.F.3    Eveleigh, D.E.4
  • 34
    • 33745232328 scopus 로고    scopus 로고
    • High-throughput screening of cellulase F mutants from multiplexed plasmid sets using an automated plate assay on a functional proteomic robotic workcell
    • doi:10.1186/1477-5956-4-10
    • Hughes SR, Riedmuller SB, Mertens JA, Li XL, Bischoff KM, et al. (2006) High-throughput screening of cellulase F mutants from multiplexed plasmid sets using an automated plate assay on a functional proteomic robotic workcell. Proteome Sci 4: 10. doi:10.1186/1477-5956-4-10.
    • (2006) Proteome Sci , vol.4 , pp. 10
    • Hughes, S.R.1    Riedmuller, S.B.2    Mertens, J.A.3    Li, X.L.4    Bischoff, K.M.5
  • 35
    • 77955506096 scopus 로고    scopus 로고
    • Automated assay for screening the enzymatic release of reducing sugars from micronized biomass
    • doi:10.1186/1475-2859-9-58
    • Navarro D, Couturier M, da Silva GGD, Berrin JG, Rouau X, et al. (2010) Automated assay for screening the enzymatic release of reducing sugars from micronized biomass. Microbial Cell Factories 9: 58. doi:10.1186/1475-2859-9-58.
    • (2010) Microbial Cell Factories , vol.9 , pp. 58
    • Navarro, D.1    Couturier, M.2    Da Silva, G.G.D.3    Berrin, J.G.4    Rouau, X.5
  • 36
    • 77958492745 scopus 로고    scopus 로고
    • Automated saccharification assay for determination of digestibility in plant materials
    • doi:10.1186/1754-6834-3-23
    • Gomez LD, Whitehead C, Barakate A, Halpin C, McQueen-Mason SJ (2010) Automated saccharification assay for determination of digestibility in plant materials. Biotechnol Biofuels 3: 23. doi:10.1186/1754-6834-3-23.
    • (2010) Biotechnol Biofuels , vol.3 , pp. 23
    • Gomez, L.D.1    Whitehead, C.2    Barakate, A.3    Halpin, C.4    McQueen-Mason, S.J.5
  • 37
    • 20444401525 scopus 로고    scopus 로고
    • Microplate-based carboxymethylcellulose assay for endoglucanase activity
    • DOI 10.1016/j.ab.2005.01.052, PII S0003269705000965
    • Xiao Z, Storms R, Tsang A (2005) Microplate-based carboxymethylcellulose assay for endoglucanase activity. Anal Biochem 342: 176-178. doi:10.1016/j.ab.2005.01.052. (Pubitemid 40805645)
    • (2005) Analytical Biochemistry , vol.342 , Issue.1 , pp. 176-178
    • Xiao, Z.1    Storms, R.2    Tsang, A.3
  • 38
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41: 207-234.
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 40
    • 79955574923 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System (n.d.) Schrödinger, LLC. Available
    • The PyMOL Molecular Graphics System (n.d.) The PyMOL Molecular Graphics System. Schrödinger, LLC. Available: http://www.pymol.org. Accessed 9 March 2013.
    • The PyMOL Molecular Graphics System
  • 41
    • 0042193601 scopus 로고    scopus 로고
    • Protein aggregation in recombinant bacteria: Biological role of inclusion bodies
    • DOI 10.1023/A:1025024104862
    • Villaverde A, Carrió MM (2003) Protein aggregation in recombinant bacteria: biological role of inclusion bodies. Biotechnol Lett 25: 1385-1395. (Pubitemid 37065286)
    • (2003) Biotechnology Letters , vol.25 , Issue.17 , pp. 1385-1395
    • Villaverde, A.1    Carrio, M.M.2
  • 42
    • 0029670577 scopus 로고    scopus 로고
    • Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents
    • doi:10.1038/nbt0496-458
    • Moore JC, Arnold FH (1996) Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. Nat Biotechnol 14: 458-467. doi:10.1038/nbt0496-458.
    • (1996) Nat Biotechnol , vol.14 , pp. 458-467
    • Moore, J.C.1    Arnold, F.H.2
  • 44
    • 20544449855 scopus 로고    scopus 로고
    • Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins
    • DOI 10.1016/j.jmb.2005.05.023, PII S0022283605005541
    • Drummond DA, Iverson BL, Georgiou G, Arnold FH (2005) Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins. J Mol Biol 350: 806-816. (Pubitemid 40848676)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.4 , pp. 806-816
    • Drummond, D.A.1    Iverson, B.L.2    Georgiou, G.3    Arnold, F.H.4
  • 45
    • 63149152073 scopus 로고    scopus 로고
    • Critical evaluation of random mutagenesis by error-prone polymerase chain reaction protocols, Escherichia coli mutator strain, and hydroxylamine treatment
    • doi:10.1016/j.ab.2009.02.008
    • Rasila TS, Pajunen MI, Savilahti H (2009) Critical evaluation of random mutagenesis by error-prone polymerase chain reaction protocols, Escherichia coli mutator strain, and hydroxylamine treatment. Anal Biochem 388: 71-80. doi:10.1016/j.ab.2009.02.008.
    • (2009) Anal Biochem , vol.388 , pp. 71-80
    • Rasila, T.S.1    Pajunen, M.I.2    Savilahti, H.3
  • 46
    • 69249127947 scopus 로고    scopus 로고
    • Visualization of biomass solubilization and cellulose regeneration during ionic liquid pretreatment of switchgrass
    • Singh S, Simmons BA, Vogel KP (2009) Visualization of biomass solubilization and cellulose regeneration during ionic liquid pretreatment of switchgrass. Biotechnol Bioeng 104: 68-75.
    • (2009) Biotechnol Bioeng , vol.104 , pp. 68-75
    • Singh, S.1    Simmons, B.A.2    Vogel, K.P.3
  • 47
    • 84875074711 scopus 로고    scopus 로고
    • Production and extraction of sugars from switchgrass hydrolyzed in ionic liquids
    • doi:10.1186/1754-6834-6-39
    • Sun N, Liu H, Sathitsuksanoh N, Stavila V, Sawant M, et al. (2013) Production and extraction of sugars from switchgrass hydrolyzed in ionic liquids. Biotechnol Biofuels 6: 39. doi:10.1186/1754-6834-6-39.
    • (2013) Biotechnol Biofuels , vol.6 , pp. 39
    • Sun, N.1    Liu, H.2    Sathitsuksanoh, N.3    Stavila, V.4    Sawant, M.5
  • 51
    • 34249104188 scopus 로고    scopus 로고
    • The catalytic effect of dihydrofolate reductase and its mutants is determined by reorganization energies
    • Warshel A (2007) The catalytic effect of dihydrofolate reductase and its mutants is determined by reorganization energies. Biochemistry.
    • (2007) Biochemistry
    • Warshel, A.1
  • 52
    • 33646935697 scopus 로고    scopus 로고
    • Dynamical contributions to enzyme catalysis: Critical tests of a popular hypothesis
    • DOI 10.1021/cr040427e
    • Olsson MHM, Parson WW, Warshel A (2006) Dynamical contributions to enzyme catalysis: critical tests of a popular hypothesis. Chem Rev 106: 1737-1756. doi:10.1021/cr040427e. (Pubitemid 43792778)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1737-1756
    • Olsson, M.H.M.1    Parson, W.W.2    Warshel, A.3
  • 53
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • DOI 10.1038/nature06407, PII NATURE06407
    • Henzler-Wildman KA, Lei M, Thai V, Kerns SJ, Karplus M, et al. (2007) A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 450: 913-916. doi:10.1038/nature06407. (Pubitemid 350231333)
    • (2007) Nature , vol.450 , Issue.7171 , pp. 913-916
    • Henzler-Wildman, K.A.1    Lei, M.2    Thai, V.3    Kerns, S.J.4    Karplus, M.5    Kern, D.6
  • 55
    • 77955272187 scopus 로고    scopus 로고
    • Molecular simulations provide new insights into the role of the accessory immunoglobulinlike domain of Cel9A
    • doi:10.1016/j.febslet.2010.06.041
    • Liu H, Pereira JH, Adams PD, Sapra R, Simmons BA, et al. (2010) Molecular simulations provide new insights into the role of the accessory immunoglobulinlike domain of Cel9A. FEBS Letters 584: 3431-3435. doi:10.1016/j.febslet.2010.06.041.
    • (2010) FEBS Letters , vol.584 , pp. 3431-3435
    • Liu, H.1    Pereira, J.H.2    Adams, P.D.3    Sapra, R.4    Simmons, B.A.5
  • 56
    • 84864449930 scopus 로고    scopus 로고
    • Protein frustratometer: A tool to localize energetic frustration in protein molecules
    • doi:10.1093/nar/gks447
    • Jenik M, Parra RG, Radusky LG, Turjanski A, Wolynes PG, et al. (2012) Protein frustratometer: a tool to localize energetic frustration in protein molecules. Nucleic Acids Res 40: W348-W351. doi:10.1093/nar/gks447.
    • (2012) Nucleic Acids Res , vol.40
    • Jenik, M.1    Parra, R.G.2    Radusky, L.G.3    Turjanski, A.4    Wolynes, P.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.