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Volumn 46, Issue 4, 2013, Pages 395-405

A roadmap to directed enzyme evolution and screening systems for biotechnological applications

Author keywords

Directed evolution; Enzyme engineering; High throughput screening; Random mutagenesis

Indexed keywords

ENZYME;

EID: 84893488236     PISSN: 07169760     EISSN: 07176287     Source Type: Journal    
DOI: 10.4067/S0716-97602013000400011     Document Type: Article
Times cited : (59)

References (70)
  • 1
    • 28844466075 scopus 로고    scopus 로고
    • High-Throughput Screening of Enzyme Libraries: Thiolactonases Evolved by Fluorescence-Activated Sorting of Single Cells in Emulsion Compartments
    • AHARONI, A., G. AMITAI, K. BERNATH, S. MAGDASSI and D. S. TAWFIK (2005). High-Throughput Screening of Enzyme Libraries: Thiolactonases Evolved by Fluorescence-Activated Sorting of Single Cells in Emulsion Compartments. Chem Biol. 12, 1281-1289
    • (2005) Chem Biol , vol.12 , pp. 1281-1289
    • Aharoni, A.1    Amitai, G.2    Bernath, K.3    Magdassi, S.4    Tawfik, D.S.5
  • 2
    • 33645811495 scopus 로고    scopus 로고
    • Protein stability promotes evolvability
    • BLOOM, J. D., S. T. LABTHAVIKUL, C. R. OTEY and F. H. ARNOLD (2006). Protein stability promotes evolvability. PNAS. 103, 5869-5874
    • (2006) PNAS , vol.103 , pp. 5869-5874
    • Bloom, J.D.1    Labthavikul, S.T.2    Otey, C.R.3    Arnold, F.H.4
  • 3
    • 3042531902 scopus 로고    scopus 로고
    • Learning from Directed Evolution: Theoretical Investigations into Cooperative Mutations in Lipase Enantioselectivity
    • BOCOLA, M., N. OTTE, K.-E. JAEGER, M. T. REETZ and W. THIEL (2004). Learning from Directed Evolution: Theoretical Investigations into Cooperative Mutations in Lipase Enantioselectivity. ChemBioChem. 5, 214-223
    • (2004) ChemBioChem , vol.5 , pp. 214-223
    • Bocola, M.1    Otte, N.2    Jaeger, K.-E.3    Reetz, M.T.4    Thiel, W.5
  • 4
    • 46649102519 scopus 로고    scopus 로고
    • A Novel Genetic Selection System for Improved Enantioselectivity of Bacillus subtilis Lipase A
    • BOERSMA, Y. L., M. J. DRÖGE, A. M. VAN DER SLOOT, T. PIJNING, R. H. COOL, B. W. DIJKSTRA and W. J. QUAX (2008). A Novel Genetic Selection System for Improved Enantioselectivity of Bacillus subtilis Lipase A. ChemBioChem. 9, 1110-1115
    • (2008) ChemBioChem , vol.9 , pp. 1110-1115
    • Boersma, Y.L.1    Dröge, M.J.2    Sloot, A.M.3    Pijning, T.R.4    Cool, H.5    Dijkstra, B.W.6    Quax, W.J.7
  • 5
    • 79953318587 scopus 로고    scopus 로고
    • Status of protein engineering for biocatalysts: How to design an industrially useful biocatalyst
    • BOMMARIUS, A. S., J. K. BLUM and M. J. ABRAHAMSON (2011). Status of protein engineering for biocatalysts: how to design an industrially useful biocatalyst. Curr. Opin. Chem. Biol. 15, 194-200
    • (2011) Curr. Opin. Chem. Biol , vol.15 , pp. 194-200
    • Bommarius, A.S.1    Blum, J.K.2    Abrahamson, M.J.3
  • 6
    • 78049263384 scopus 로고    scopus 로고
    • Improving Biocatalyst Performance by Integrating Statistical Methods into Protein Engineering
    • BROUK, M., Y. NOV and A. FISHMAN (2010). Improving Biocatalyst Performance by Integrating Statistical Methods into Protein Engineering. Appl. Environ. Microbiol. 76, 6397-6403
    • (2010) Appl. Environ. Microbiol , vol.76 , pp. 6397-6403
    • Brouk, M.1    Nov, Y.2    Fishman, A.3
  • 7
    • 76549129324 scopus 로고    scopus 로고
    • Adaptive landscapes and protein evolution
    • CARNEIRO, M. and D. L. HARTL (2010). Adaptive landscapes and protein evolution. PNAS. 107, 1747-1751
    • (2010) PNAS , vol.107 , pp. 1747-1751
    • Carneiro, M.1    Hartl, D.L.2
  • 11
    • 21044438456 scopus 로고    scopus 로고
    • A New Embedded Process for Compartmentalized Cell-Free Protein Expression and On-line Detection in Microfluidic Devices
    • DITTRICH, P. S., M. JAHNZ and P. SCHWILLE (2005). A New Embedded Process for Compartmentalized Cell-Free Protein Expression and On-line Detection in Microfluidic Devices. ChemBioChem. 6, 811-814
    • (2005) ChemBioChem , vol.6 , pp. 811-814
    • Dittrich, P.S.1    Jahnz, M.2    Schwille, P.3
  • 12
    • 79953320824 scopus 로고    scopus 로고
    • Ionic liquids in biotransformations: From proof-of-concept to emerging deep-eutectic-solvents
    • DOMÍNGUEZ DE MARÍA, P. and Z. MAUGERI (2011). Ionic liquids in biotransformations: from proof-of-concept to emerging deep-eutectic-solvents. Curr. Opin. Chem. Biol. 15, 220-225
    • (2011) Curr. Opin. Chem. Biol , vol.15 , pp. 220-225
    • De Domínguez, M.P.1    Maugeri, Z.2
  • 13
    • 84857165856 scopus 로고    scopus 로고
    • A completely in vitro ultrahigh-throughput droplet-based microfluidic screening system for protein engineering and directed evolution
    • Fallah-Araghi, A., J.-C. BARET, M. RYCKELYNCK and A. D. GRIFFITHS (2012). A completely in vitro ultrahigh-throughput droplet-based microfluidic screening system for protein engineering and directed evolution. Lab Chip. 12, 882-891
    • (2012) Lab Chip , vol.12 , pp. 882-891
    • Fallah-Araghi, A.1    Baret, J.-C.2    Ryckelynck, M.3    Griffiths, A.D.4
  • 15
    • 53549085133 scopus 로고    scopus 로고
    • Evolutionary History of a Specialized P450 Propane Monooxygenase
    • FASAN, R., Y. T. MEHARENNA, C. D. SNOW, T. L. POULOS and F. H. ARNOLD (2008). Evolutionary History of a Specialized P450 Propane Monooxygenase. J. Mol. Biol. 383, 1069-1080
    • (2008) J. Mol. Biol , vol.383 , pp. 1069-1080
    • Fasan, R.1    Meharenna, Y.T.2    Snow, C.D.3    Poulos, T.L.4    Arnold, F.H.5
  • 16
    • 23944462537 scopus 로고    scopus 로고
    • Statistics of protein library construction
    • FIRTH, A. E. and W. M. PATRICK (2005). Statistics of protein library construction. Bioinformatics. 21, 3314-3315
    • (2005) Bioinformatics , vol.21 , pp. 3314-3315
    • Firth, A.E.1    Patrick, W.M.2
  • 17
    • 2342488258 scopus 로고    scopus 로고
    • White biotechnology
    • FRAZZETTO, G. (2003). White biotechnology. EMBO Rep. 4, 835-837
    • (2003) EMBO Rep , vol.4 , pp. 835-837
    • Frazzetto, G.1
  • 18
    • 84655167596 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of microcrystalline cellulose in concentrated seawater
    • GRANDE, P. M. and P. DOMÍNGUEZ DE MARÍA (2012). Enzymatic hydrolysis of microcrystalline cellulose in concentrated seawater. Bioresour. Technol. 104, 799-802
    • (2012) Bioresour. Technol , vol.104 , pp. 799-802
    • Grande, P.M.1    María, P.2    De Domínguez3
  • 19
    • 33747130345 scopus 로고    scopus 로고
    • Miniaturising the laboratory in emulsion droplets
    • GRIFFITHS, A. D. and D. S. TAWFIK (2006). Miniaturising the laboratory in emulsion droplets. Trends Biotechnol. 24, 395-402
    • (2006) Trends Biotechnol , vol.24 , pp. 395-402
    • Griffiths, A.D.1    Tawfik, D.S.2
  • 20
    • 0037213311 scopus 로고    scopus 로고
    • An overview on fermentation, downstream processing and properties of microbial alkaline proteases
    • GUPTA, R., Q. BEG, S. KHAN and B. CHAUHAN (2002). An overview on fermentation, downstream processing and properties of microbial alkaline proteases. Appl. Microbiol. Biotechnol. 60, 381-395
    • (2002) Appl. Microbiol. Biotechnol , vol.60 , pp. 381-395
    • Gupta, R.1    Beg, Q.2    Khan, S.3    Chauhan, B.4
  • 25
    • 84865492433 scopus 로고    scopus 로고
    • Picoliter Cell Lysate Assays in Microfluidic Droplet Compartments for Directed Enzyme Evolution
    • KINTSES, B., C. HEIN, MARK F. MOHAMED, M. FISCHLECHNER, F. COURTOIS, C. LAINÉ and F. HOLLFELDER (2012). Picoliter Cell Lysate Assays in Microfluidic Droplet Compartments for Directed Enzyme Evolution. Chem Biol. 19, 1001-1009
    • (2012) Chem Biol , vol.19 , pp. 1001-1009
    • Kintses, B.1    Hein, C.2    Mark, F.M.3    Fischlechner, M.F.4    Courtois, L.C.5    Hollfelder, F.6
  • 26
    • 84893518617 scopus 로고    scopus 로고
    • Directed evolution: Tailoring biocatalysts for industrial applications
    • KUMAR, A. and S. SINGH (2012). Directed evolution: tailoring biocatalysts for industrial applications. Crit. Rev. Biotech. 0, 1-14
    • (2012) Crit. Rev. Biotech , vol.0 , pp. 1-14
    • Kumar, A.1    Singh, S.2
  • 27
    • 0034855858 scopus 로고    scopus 로고
    • How do thermophilic proteins deal with heat?
    • KUMAR, S. and R. NUSSINOV (2001). How do thermophilic proteins deal with heat? CMLS, Cell. Mol. Life Sci. 58, 1216-1233
    • (2001) CMLS, Cell. Mol. Life Sci , vol.58 , pp. 1216-1233
    • Kumar, S.1    Nussinov, R.2
  • 28
    • 68049085915 scopus 로고    scopus 로고
    • Directed evolution of enzymes: Library screening strategies
    • LEEMHUIS, H., R. M. KELLY and L. DIJKHUIZEN (2009). Directed evolution of enzymes: Library screening strategies. IUBMB Life. 61, 222-228
    • (2009) IUBMB Life , vol.61 , pp. 222-228
    • Leemhuis, H.1    Kelly, R.M.2    Dijkhuizen, L.3
  • 29
    • 84867029848 scopus 로고    scopus 로고
    • Reengineering CelA2 cellulase for hydrolysis in aqueous solutions of deep eutectic solvents and concentrated seawater
    • LEHMANN, C., F. SIBILLA, Z. MAUGERI, W. R. STREIT, P. DOMÍNGUEZ DE MARIA, R. MARTINEZ and U. SCHWANEBERG (2012). Reengineering CelA2 cellulase for hydrolysis in aqueous solutions of deep eutectic solvents and concentrated seawater. Green Chem. 14, 2719-2726
    • (2012) Green Chem , vol.14 , pp. 2719-2726
    • Lehmann, C.1    Sibilla, F.2    Maugeri, Z.3    Streit, W.R.4    Domínguez, M.D.E.5    Martinez, R.6    Schwaneberg, U.7
  • 30
    • 84889781065 scopus 로고    scopus 로고
    • In vitro selection of proteins via emulsion compartments
    • LU, W.-C. and A. D. ELLINGTON (2012). In vitro selection of proteins via emulsion compartments. Methods.
    • (2012) Methods
    • Lu, W.-C.1    Ellington, A.D.2
  • 31
    • 84872273584 scopus 로고    scopus 로고
    • Phosphorothioate-based DNA recombination: An enzyme-free method for the combinatorial assembly of multiple DNA fragments
    • MARIENHAGEN, J., A. DENNIG and U. SCHWANEBERG (2012). Phosphorothioate-based DNA recombination: an enzyme-free method for the combinatorial assembly of multiple DNA fragments. BioTechniques. 0, 1-6
    • (2012) BioTechniques , vol.0 , pp. 1-6
    • Marienhagen, J.1    Dennig, A.2    Schwaneberg, U.3
  • 32
    • 84872657998 scopus 로고    scopus 로고
    • Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution
    • MARTÍNEZ, R., F. JAKOB, R. TU, P. SIEGERT, K.-H. MAURER and U. SCHWANEBERG (2013). Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution. Biotechnol. Bioeng. 110, 711-720
    • (2013) Biotechnol. Bioeng , vol.110 , pp. 711-720
    • Martínez, R.1    Jakob, F.2    Tu, R.3    Siegert, P.4    Maurer, K.-H.5    Schwaneberg, U.6
  • 33
    • 28844487473 scopus 로고    scopus 로고
    • 2-Galactosidase by Fluorescence-Activated Sorting of Double Emulsions
    • MASTROBATTISTA, E., V. TALY, E. CHANUDET, P. TREACY, B. T. KELLY and A. D. GRIFFITHS (2005). High-Throughput Screening of Enzyme Libraries: In Vitro Evolution of a 2-Galactosidase by Fluorescence-Activated Sorting of Double Emulsions. Chem Biol. 12, 1291-1300
    • (2005) Chem Biol , vol.12 , pp. 1291-1300
    • Mastrobattista, E.1    Taly, V.2    Chanudet, E.3    Treacy, P.4    Kelly, B.T.5    Griffiths, A.D.6
  • 35
    • 27944437517 scopus 로고    scopus 로고
    • Automated design of degenerate codon libraries
    • MENA, M. A. and P. S. DAUGHERTY (2005). Automated design of degenerate codon libraries. Protein Eng. Des. Sel. 18, 559-561
    • (2005) Protein Eng. Des. Sel , vol.18 , pp. 559-561
    • Mena, M.A.1    Daugherty, P.S.2
  • 37
    • 79959708035 scopus 로고    scopus 로고
    • SeSaM-Tv-II Generates a Protein Sequence Space that is Unobtainable by epPCR
    • MUNDHADA, H., J. MARIENHAGEN, A. SCACIOC, A. SCHENK, D. ROCCATANO and U. SCHWANEBERG (2011). SeSaM-Tv-II Generates a Protein Sequence Space that is Unobtainable by epPCR. ChemBioChem. 12, 1595-1601
    • (2011) ChemBioChem , vol.12 , pp. 1595-1601
    • Mundhada, H.1    Marienhagen, J.2    Scacioc, A.3    Schenk, A.D.4    Roccatano, S.U.5
  • 38
    • 84868280186 scopus 로고    scopus 로고
    • Directed Evolution of Proteins through In Vitro Protein Synthesis in Liposomes
    • NISHIKAWA, T., T. SUNAMI, T. MATSUURA and T. YOMO (2012). Directed Evolution of Proteins through In Vitro Protein Synthesis in Liposomes. J. Nucleic Acids. 2012, 11
    • (2012) J. Nucleic Acids , vol.2012 , pp. 11
    • Nishikawa, T.1    Sunami, T.2    Matsuura, T.3    Yomo, T.4
  • 39
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • O'BRIEN, P. J. and D. HERSCHLAG (1999). Catalytic promiscuity and the evolution of new enzymatic activities. Chem Biol. 6, R91-R105
    • (1999) Chem Biol , vol.6
    • O'Brien, P.J.1    Herschlag, D.2
  • 40
    • 0036960601 scopus 로고    scopus 로고
    • Structure-based Combinatorial Protein Engineering (SCOPE)
    • O'MAILLE, P. E., M. BAKHTINA and M.-D. TSAI (2002). Structure-based Combinatorial Protein Engineering (SCOPE). J. Mol. Biol. 321, 677-691
    • (2002) J. Mol. Biol , vol.321 , pp. 677-691
    • O'Maille, P.E.1    Bakhtina, M.2    Tsai, M.-D.3
  • 41
    • 67849130559 scopus 로고    scopus 로고
    • HotSpot Wizard: A web server for identification of hot spots in protein engineering
    • PAVELKA, A., E. CHOVANCOVA and J. DAMBORSKY (2009). HotSpot Wizard: a web server for identification of hot spots in protein engineering. Nucleic Acids Res. 37, W376-W383
    • (2009) Nucleic Acids Res , vol.37
    • Pavelka, A.1    Chovancova, E.2    Damborsky, J.3
  • 42
    • 85148993418 scopus 로고    scopus 로고
    • Directed evolution: Selection of the host organism
    • POURMIR, A. and T. W. JOHANNES (2012). Directed evolution: selection of the host organism. CSBJ. 2
    • (2012) CSBJ , pp. 2
    • Pourmir, A.1    Johannes, T.W.2
  • 44
    • 70349110513 scopus 로고    scopus 로고
    • Directed Evolution of Enantioselective Enzymes: An Unconventional Approach to Asymmetric Catalysis in Organic Chemistry
    • REETZ, M. T. (2009). Directed Evolution of Enantioselective Enzymes: An Unconventional Approach to Asymmetric Catalysis in Organic Chemistry. J. Org. Chem. 74, 5767-5778
    • (2009) J. Org. Chem , vol.74 , pp. 5767-5778
    • Reetz, M.T.1
  • 45
    • 22144485602 scopus 로고    scopus 로고
    • Expanding the Range of Substrate Acceptance of Enzymes: Combinatorial Active-Site Saturation Test
    • REETZ, M. T., M. BOCOLA, J. D. CARBALLEIRA, D. ZHA and A. VOGEL (2005). Expanding the Range of Substrate Acceptance of Enzymes: Combinatorial Active-Site Saturation Test. Angew. Chem. Int. Ed. Engl. 44, 4192-4196
    • (2005) Angew. Chem. Int. Ed. Engl , vol.44 , pp. 4192-4196
    • Reetz, M.T.1    Bocola, M.2    Carballeira, J.D.3    Zha, D.4    Vogel, A.5
  • 46
    • 55849130758 scopus 로고    scopus 로고
    • A genetic selection system for evolving enantioselectivity of enzymes
    • REETZ, M. T., H. HOBENREICH, P. SONI and L. FERNANDEZ (2008). A genetic selection system for evolving enantioselectivity of enzymes. Chem. Commun. 0, 5502-5504
    • (2008) Chem. Commun , vol.0 , pp. 5502-5504
    • Reetz, M.T.1    Hobenreich, H.2    Soni, P.3    Fernandez, L.4
  • 47
    • 54349090614 scopus 로고    scopus 로고
    • Addressing the Numbers Problem in Directed Evolution
    • REETZ, M. T., D. KAHAKEAW and R. LOHMER (2008). Addressing the Numbers Problem in Directed Evolution. ChemBioChem. 9, 1797-1804
    • (2008) ChemBioChem , vol.9 , pp. 1797-1804
    • Reetz, M.T.1    Kahakeaw, D.2    Lohmer, R.3
  • 48
    • 70450242805 scopus 로고    scopus 로고
    • Exploring protein fitness landscapes by directed evolution
    • ROMERO, P. A. and F. H. ARNOLD (2009). Exploring protein fitness landscapes by directed evolution. Nat Rev Mol Cell Biol. 10, 866-876
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 866-876
    • Romero, P.A.1    Arnold, F.H.2
  • 49
    • 84879229500 scopus 로고    scopus 로고
    • To get what we aim for-progress in diversity generation methods
    • RUFF, A. J., A. DENNIG and U. SCHWANEBERG (2013). To get what we aim for-progress in diversity generation methods. FEBS Journal. 280, 2961-2978
    • (2013) FEBS Journal , vol.280 , pp. 2961-2978
    • Ruff, A.J.1    Dennig, A.2    Schwaneberg, U.3
  • 50
    • 84870932945 scopus 로고    scopus 로고
    • Flow Cytometer-Based High-Throughput Screening System for Accelerated Directed Evolution of P450 Monooxygenases
    • RUFF, A. J., A. DENNIG, G. WIRTZ, M. BLANUSA and U. SCHWANEBERG (2012). Flow Cytometer-Based High-Throughput Screening System for Accelerated Directed Evolution of P450 Monooxygenases. ACS Catal. 2, 2724-2728
    • (2012) ACS Catal , vol.2 , pp. 2724-2728
    • Ruff, A.J.1    Dennig, A.2    Wirtz, G.3    Blanusa, M.4    Schwaneberg, U.5
  • 54
    • 34547271956 scopus 로고    scopus 로고
    • The impact of industrial biotechnology
    • SOETAERT, W. and E. VANDAMME (2006). The impact of industrial biotechnology. Biotech. J. 1, 756-769
    • (2006) Biotech. J , vol.1 , pp. 756-769
    • Soetaert, W.1    Vandamme, E.2
  • 55
    • 73849092565 scopus 로고    scopus 로고
    • Industrial biotechnology: Tools and applications
    • TANG, W. L. and H. ZHAO (2009). Industrial biotechnology: Tools and applications. Biotech. J. 4, 1725-1739
    • (2009) Biotech. J , vol.4 , pp. 1725-1739
    • Tang, W.L.1    Zhao, H.2
  • 56
    • 0031854986 scopus 로고    scopus 로고
    • Man-made cell-like compartments for molecular evolution
    • TAWFIK, D. S. and A. D. GRIFFITHS (1998). Man-made cell-like compartments for molecular evolution. Nat Biotech. 16, 652-656
    • (1998) Nat Biotech , vol.16 , pp. 652-656
    • Tawfik, D.S.1    Griffiths, A.D.2
  • 57
    • 33947225610 scopus 로고    scopus 로고
    • Directed Evolution of Oxygenases: Screening Systems, Success Stories and Challenges
    • TEE, K. L. and U. SCHWANEBERG (2007). Directed Evolution of Oxygenases: Screening Systems, Success Stories and Challenges. Comb. Chem. High Throughput Screening. 10, 197-217
    • (2007) Comb. Chem. High Throughput Screening , vol.10 , pp. 197-217
    • Tee, K.L.1    Schwaneberg, U.2
  • 59
    • 79954615462 scopus 로고    scopus 로고
    • A Flow Cytometry-Based Screening System for Directed Evolution of Proteases
    • TU, R., R. MARTINEZ, R. PRODANOVIC, M. KLEIN and U. SCHWANEBERG (2011). A Flow Cytometry-Based Screening System for Directed Evolution of Proteases. J. Biomol. Screen. 16, 285-294
    • (2011) J. Biomol. Screen , vol.16 , pp. 285-294
    • Tu, R.1    Martinez, R.2    Prodanovic, R.3    Klein, M.4    Schwaneberg, U.5
  • 60
    • 84868216091 scopus 로고    scopus 로고
    • MAP2.03D: A Sequence/Structure Based Server for Protein Engineering
    • VERMA, R., U. SCHWANEBERG and D. ROCCATANO (2012). MAP2.03D: A Sequence/Structure Based Server for Protein Engineering. ACS Synthetic Biology. 1, 139-150
    • (2012) ACS Synthetic Biology , vol.1 , pp. 139-150
    • Verma, R.1    Schwaneberg, U.2    Roccatano, D.3
  • 62
    • 62649104324 scopus 로고    scopus 로고
    • Expanding the Genetic Code for Biological Studies
    • WANG, Q., A. R. PARRISH and L. WANG (2009). Expanding the Genetic Code for Biological Studies. Chem Biol. 16, 323-336
    • (2009) Chem Biol , vol.16 , pp. 323-336
    • Wang, Q.1    Parrish, A.R.2    Wang, L.3
  • 63
    • 38849132858 scopus 로고    scopus 로고
    • Transversion-enriched sequence saturation mutagenesis (SeSaM-Tv+): A random mutagenesis method with consecutive nucleotide exchanges that complements the bias of error-prone PCR
    • WONG, T. S., D. ROCCATANO, D. LOAKES, K. L. TEE, A. SCHENK, B. HAUER and U. SCHWANEBERG (2008). Transversion-enriched sequence saturation mutagenesis (SeSaM-Tv+): A random mutagenesis method with consecutive nucleotide exchanges that complements the bias of error-prone PCR. Biotech. J. 3, 74-82
    • (2008) Biotech. J , vol.3 , pp. 74-82
    • Wong, T.S.1    Roccatano, D.2    Loakes, D.3    Tee, K.L.4    Schenk, A.5    Hauer, B.6    Schwaneberg, U.7
  • 64
    • 33847016154 scopus 로고    scopus 로고
    • Are transversion mutations better? A Mutagenesis Assistant Program analysis on P450 BM-3 heme domain
    • WONG, T. S., D. ROCCATANO and U. SCHWANEBERG (2007). Are transversion mutations better? A Mutagenesis Assistant Program analysis on P450 BM-3 heme domain. Biotech. J. 2, 133-142
    • (2007) Biotech. J , vol.2 , pp. 133-142
    • Wong, T.S.1    Roccatano, D.2    Schwaneberg, U.3
  • 65
    • 77952506385 scopus 로고    scopus 로고
    • Challenges of the genetic code for exploring sequence space in directed protein evolution
    • WONG, T. S., D. ROCCATANO and U. SCHWANEBERG (2007). Challenges of the genetic code for exploring sequence space in directed protein evolution. Biocatal. Biotransfor. 25, 229-241
    • (2007) Biocatal. Biotransfor , vol.25 , pp. 229-241
    • Wong, T.S.1    Roccatano, D.2    Schwaneberg, U.3
  • 66
    • 35148850038 scopus 로고    scopus 로고
    • Steering directed protein evolution: Strategies to manage combinatorial complexity of mutant libraries
    • WONG, T. S., D. ROCCATANO and U. SCHWANEBERG (2007). Steering directed protein evolution: strategies to manage combinatorial complexity of mutant libraries. Environ. Microbiol. 9, 2645-2659
    • (2007) Environ. Microbiol , vol.9 , pp. 2645-2659
    • Wong, T.S.1    Roccatano, D.2    Schwaneberg, U.3
  • 67
    • 29144503012 scopus 로고    scopus 로고
    • A Statistical Analysis of Random Mutagenesis Methods Used for Directed Protein Evolution
    • WONG, T. S., D. ROCCATANO, M. ZACHARIAS and U. SCHWANEBERG (2006). A Statistical Analysis of Random Mutagenesis Methods Used for Directed Protein Evolution. J. Mol. Biol. 355, 858-871
    • (2006) J. Mol. Biol , vol.355 , pp. 858-871
    • Wong, T.S.1    Roccatano, D.2    Zacharias, M.3    Schwaneberg, U.4
  • 68
    • 2342535792 scopus 로고    scopus 로고
    • Sequence saturation mutagenesis (SeSaM): A novel method for directed evolution
    • WONG, T. S., K. L. TEE, B. HAUER and U. SCHWANEBERG (2004). Sequence saturation mutagenesis (SeSaM): a novel method for directed evolution. Nucleic Acids Res. 32, e26
    • (2004) Nucleic Acids Res , vol.32
    • Wong, T.S.1    Tee, K.L.2    Hauer, B.3    Schwaneberg, U.4
  • 70
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • ZHAO, H., L. GIVER, Z. SHAO, J. A. AFFHOLTER and F. H. ARNOLD (1998). Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat Biotech. 16, 258-261
    • (1998) Nat Biotech , vol.16 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Shao, Z.3    Affholter, J.A.4    Arnold, F.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.