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Volumn 99, Issue 4, 2015, Pages 1545-1556

Bringing functions together with fusion enzymes—from nature’s inventions to biotechnological applications

Author keywords

Bifunctionality; Biomass degradation; End to end fusion; Multifunctionality; Synergism

Indexed keywords

BIOTECHNOLOGY; CATALYST ACTIVITY; CLONE CELLS; GENES; MOLECULAR BIOLOGY; PATENTS AND INVENTIONS; PLANTS (BOTANY); POLYMERASE CHAIN REACTION; SUBSTRATES;

EID: 84924302954     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-6315-1     Document Type: Review
Times cited : (81)

References (82)
  • 1
    • 79961063240 scopus 로고    scopus 로고
    • Synthesis and characterization of chimeric proteins based on cellulase and xylanase from an insect gut bacterium
    • COI: 1:CAS:528:DC%2BC3MXhtVWlsbrK, PID: 21642416
    • Adlakha N, Rajagopal R, Kumar S, Reddy VS, Yazdani SS (2011) Synthesis and characterization of chimeric proteins based on cellulase and xylanase from an insect gut bacterium. Appl Environ Microbiol 77:4859–4866
    • (2011) Appl Environ Microbiol , vol.77 , pp. 4859-4866
    • Adlakha, N.1    Rajagopal, R.2    Kumar, S.3    Reddy, V.S.4    Yazdani, S.S.5
  • 2
    • 84868369249 scopus 로고    scopus 로고
    • Specific fusion of beta-1,4-endoglucanase and beta-1,4-glucosidase enhances cellulolytic activity and helps in channeling of intermediates
    • COI: 1:CAS:528:DC%2BC38XhsVOnu7vF, PID: 22904050
    • Adlakha N, Sawant S, Anil A, Lali A, Yazdani SS (2012) Specific fusion of beta-1,4-endoglucanase and beta-1,4-glucosidase enhances cellulolytic activity and helps in channeling of intermediates. Appl Environ Microbiol 78:7447–7454
    • (2012) Appl Environ Microbiol , vol.78 , pp. 7447-7454
    • Adlakha, N.1    Sawant, S.2    Anil, A.3    Lali, A.4    Yazdani, S.S.5
  • 3
    • 0037222296 scopus 로고    scopus 로고
    • Distribution and function of new bacterial intein-like protein domains
    • COI: 1:CAS:528:DC%2BD3sXntVKitA%3D%3D, PID: 12492854
    • Amitai G, Belenkiy O, Dassa B, Shainskaya A, Pietrokovski S (2003) Distribution and function of new bacterial intein-like protein domains. Mol Microbiol 47:61–73
    • (2003) Mol Microbiol , vol.47 , pp. 61-73
    • Amitai, G.1    Belenkiy, O.2    Dassa, B.3    Shainskaya, A.4    Pietrokovski, S.5
  • 4
    • 41749092312 scopus 로고    scopus 로고
    • Reversible compartmentalization of de novo purine biosynthetic complexes in living cells
    • COI: 1:CAS:528:DC%2BD1cXktVKhsbk%3D, PID: 18388293
    • An S, Kumar R, Sheets ED, Benkovic SJ (2008) Reversible compartmentalization of de novo purine biosynthetic complexes in living cells. Science 320:103–106
    • (2008) Science , vol.320 , pp. 103-106
    • An, S.1    Kumar, R.2    Sheets, E.D.3    Benkovic, S.J.4
  • 5
    • 0032499716 scopus 로고    scopus 로고
    • Structure and function of the Bacillus hybrid enzyme GluXyn-1: native-like jellyroll fold preserved after insertion of autonomous globular domain
    • COI: 1:CAS:528:DyaK1cXjslynt74%3D, PID: 9618460
    • Ay J, Gotz F, Borriss R, Heinemann U (1998) Structure and function of the Bacillus hybrid enzyme GluXyn-1: native-like jellyroll fold preserved after insertion of autonomous globular domain. Proc Natl Acad Sci U S A 95:6613–6618
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6613-6618
    • Ay, J.1    Gotz, F.2    Borriss, R.3    Heinemann, U.4
  • 6
    • 0030696198 scopus 로고    scopus 로고
    • Creating a bifunctional protein by insertion of beta-lactamase into the maltodextrin-binding protein
    • COI: 1:CAS:528:DyaK2sXntVSlu7Y%3D, PID: 9359111
    • Betton JM, Jacob JP, Hofnung M, Broome-Smith JK (1997) Creating a bifunctional protein by insertion of beta-lactamase into the maltodextrin-binding protein. Nat Biotechnol 15:1276–1279
    • (1997) Nat Biotechnol , vol.15 , pp. 1276-1279
    • Betton, J.M.1    Jacob, J.P.2    Hofnung, M.3    Broome-Smith, J.K.4
  • 7
    • 84873119880 scopus 로고    scopus 로고
    • Improved lignocellulose conversion to biofuels with thermophilic bacteria and thermostable enzymes
    • COI: 1:CAS:528:DC%2BC38XhvVCrsLfF, PID: 23246299
    • Bhalla A, Bansal N, Kumar S, Bischoff KM, Sani RK (2013) Improved lignocellulose conversion to biofuels with thermophilic bacteria and thermostable enzymes. Bioresour Technol 128:751–759
    • (2013) Bioresour Technol , vol.128 , pp. 751-759
    • Bhalla, A.1    Bansal, N.2    Kumar, S.3    Bischoff, K.M.4    Sani, R.K.5
  • 8
    • 84923915273 scopus 로고    scopus 로고
    • Enzymatic degradation of (ligno)cellulose
    • COI: 1:CAS:528:DC%2BC2cXhtlOltrzL, PID: 25136976
    • Bornscheuer U, Buchholz K, Seibel J (2014) Enzymatic degradation of (ligno)cellulose. Angew Chem Int Ed Engl 53:10876–10893
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 10876-10893
    • Bornscheuer, U.1    Buchholz, K.2    Seibel, J.3
  • 9
    • 0023960331 scopus 로고
    • Traffic and assembly of concanavalin A
    • COI: 1:CAS:528:DyaL1cXitVWltrc%3D, PID: 3070848
    • Bowles DJ, Pappin DJ (1988) Traffic and assembly of concanavalin A. Trends Biochem Sci 13:60–64
    • (1988) Trends Biochem Sci , vol.13 , pp. 60-64
    • Bowles, D.J.1    Pappin, D.J.2
  • 10
    • 0029041022 scopus 로고
    • A molecular sensor system based on genetically engineered alkaline phosphatase
    • COI: 1:CAS:528:DyaK2MXmsFWqsbs%3D, PID: 7541135
    • Brennan CA, Christianson K, La Fleur MA, Mandecki W (1995) A molecular sensor system based on genetically engineered alkaline phosphatase. Proc Natl Acad Sci U S A 92:5783–5787
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 5783-5787
    • Brennan, C.A.1    Christianson, K.2    La Fleur, M.A.3    Mandecki, W.4
  • 11
    • 84883033189 scopus 로고    scopus 로고
    • A plasmid toolkit for cloning chimeric cDNAs encoding customized fusion proteins into any Gateway destination expression vector
    • COI: 1:CAS:528:DC%2BC3sXhsVensr7O, PID: 23957834
    • Buj R, Iglesias N, Planas AM, Santalucia T (2013) A plasmid toolkit for cloning chimeric cDNAs encoding customized fusion proteins into any Gateway destination expression vector. BMC Mol Biol 14:18
    • (2013) BMC Mol Biol , vol.14 , pp. 18
    • Buj, R.1    Iglesias, N.2    Planas, A.M.3    Santalucia, T.4
  • 12
    • 13044268636 scopus 로고
    • Preparation of a soluble bifunctional enzyme by gene fusion
    • Bülow L, Ljungcrantz P, Mosbach K (1985) Preparation of a soluble bifunctional enzyme by gene fusion. Bio/Technology 3:821–823
    • (1985) Bio/Technology , vol.3 , pp. 821-823
    • Bülow, L.1    Ljungcrantz, P.2    Mosbach, K.3
  • 13
    • 0022644082 scopus 로고
    • The isolation and nucleotide sequence of the complex AROM locus of Aspergillus nidulans
    • COI: 1:CAS:528:DyaL28XitVWhtbY%3D, PID: 3515316
    • Charles IG, Keyte JW, Brammar WJ, Smith M, Hawkins AR (1986) The isolation and nucleotide sequence of the complex AROM locus of Aspergillus nidulans. Nucleic Acids Res 14:2201–2213
    • (1986) Nucleic Acids Res , vol.14 , pp. 2201-2213
    • Charles, I.G.1    Keyte, J.W.2    Brammar, W.J.3    Smith, M.4    Hawkins, A.R.5
  • 14
    • 0037032419 scopus 로고    scopus 로고
    • Biochemical characterization of Thermotoga maritima endoglucanase Cel74 with and without a carbohydrate binding module (CBM)
    • COI: 1:CAS:528:DC%2BD38Xotl2ms7s%3D, PID: 12417345
    • Chhabra SR, Kelly RM (2002) Biochemical characterization of Thermotoga maritima endoglucanase Cel74 with and without a carbohydrate binding module (CBM). FEBS Lett 531:375–380
    • (2002) FEBS Lett , vol.531 , pp. 375-380
    • Chhabra, S.R.1    Kelly, R.M.2
  • 15
    • 53049107187 scopus 로고    scopus 로고
    • Engineering the spatial organization of metabolic enzymes: mimicking nature’s synergy
    • COI: 1:CAS:528:DC%2BD1cXht1SntL%2FO, PID: 18725290
    • Conrado RJ, Varner JD, DeLisa MP (2008) Engineering the spatial organization of metabolic enzymes: mimicking nature’s synergy. Curr Opin Biotechnol 19:492–499
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 492-499
    • Conrado, R.J.1    Varner, J.D.2    DeLisa, M.P.3
  • 16
    • 67649823734 scopus 로고    scopus 로고
    • ‘Cradle-to-grave’ assessment of existing lignocellulose pretreatment technologies
    • PID: 19481437
    • da Costa Sousa L, Chundawat SP, Balan V, Dale BE (2009) ‘Cradle-to-grave’ assessment of existing lignocellulose pretreatment technologies. Curr Opin Biotechnol 20:339–347
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 339-347
    • da Costa Sousa, L.1    Chundawat, S.P.2    Balan, V.3    Dale, B.E.4
  • 17
    • 3543025094 scopus 로고    scopus 로고
    • Protein splicing and auto-cleavage of bacterial intein-like domains lacking a C′-flanking nucleophilic residue
    • COI: 1:CAS:528:DC%2BD2cXmtVCiur4%3D, PID: 15150275
    • Dassa B, Haviv H, Amitai G, Pietrokovski S (2004) Protein splicing and auto-cleavage of bacterial intein-like domains lacking a C′-flanking nucleophilic residue. J Biol Chem 279:32001–32007
    • (2004) J Biol Chem , vol.279 , pp. 32001-32007
    • Dassa, B.1    Haviv, H.2    Amitai, G.3    Pietrokovski, S.4
  • 19
    • 0032765695 scopus 로고    scopus 로고
    • Insertional gene fusion technology
    • COI: 1:CAS:528:DyaK1MXmtFejs7g%3D, PID: 10486551
    • Doi N, Yanagawa H (1999) Insertional gene fusion technology. FEBS Lett 457:1–4
    • (1999) FEBS Lett , vol.457 , pp. 1-4
    • Doi, N.1    Yanagawa, H.2
  • 20
    • 3142757398 scopus 로고    scopus 로고
    • Cellulosomes: plant-cell-wall-degrading enzyme complexes
    • COI: 1:CAS:528:DC%2BD2cXkvVSru7Y%3D, PID: 15197390
    • Doi RH, Kosugi A (2004) Cellulosomes: plant-cell-wall-degrading enzyme complexes. Nat Rev Microbiol 2:541–551
    • (2004) Nat Rev Microbiol , vol.2 , pp. 541-551
    • Doi, R.H.1    Kosugi, A.2
  • 21
    • 79952252539 scopus 로고    scopus 로고
    • Fusion of the OsmC domain from esterase EstO confers thermolability to the cold-active xylanase Xyn8 from Pseudoalteromonas arctica
    • COI: 1:CAS:528:DC%2BC3MXislOrtb4%3D, PID: 21331632
    • Elleuche S, Piascheck H, Antranikian G (2011) Fusion of the OsmC domain from esterase EstO confers thermolability to the cold-active xylanase Xyn8 from Pseudoalteromonas arctica. Extremophiles 15:311–317
    • (2011) Extremophiles , vol.15 , pp. 311-317
    • Elleuche, S.1    Piascheck, H.2    Antranikian, G.3
  • 22
    • 77953043452 scopus 로고    scopus 로고
    • Inteins, valuable genetic elements in molecular biology and biotechnology
    • COI: 1:CAS:528:DC%2BC3cXmtlGrs7s%3D, PID: 20449740
    • Elleuche S, Pöggeler S (2010) Inteins, valuable genetic elements in molecular biology and biotechnology. Appl Microbiol Biotechnol 87:479–489
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 479-489
    • Elleuche, S.1    Pöggeler, S.2
  • 23
    • 84899789891 scopus 로고    scopus 로고
    • Extremozymes-biocatalysts with unique properties from extremophilic microorganisms
    • Elleuche S, Schröder C, Sahm K, Antranikian G (2014) Extremozymes-biocatalysts with unique properties from extremophilic microorganisms. Curr Opin Biotechnol 29C:116–123
    • (2014) Curr Opin Biotechnol , vol.29C , pp. 116-123
    • Elleuche, S.1    Schröder, C.2    Sahm, K.3    Antranikian, G.4
  • 24
    • 56649114274 scopus 로고    scopus 로고
    • A one pot, one step, precision cloning method with high throughput capability
    • PID: 18985154
    • Engler C, Kandzia R, Marillonnet S (2008) A one pot, one step, precision cloning method with high throughput capability. PLoS One 3:e3647
    • (2008) PLoS One , vol.3 , pp. 3647
    • Engler, C.1    Kandzia, R.2    Marillonnet, S.3
  • 26
    • 0036878154 scopus 로고    scopus 로고
    • An analysis of protein domain linkers: their classification and role in protein folding
    • COI: 1:CAS:528:DC%2BD3sXitlCntLw%3D, PID: 12538906
    • George RA, Heringa J (2002) An analysis of protein domain linkers: their classification and role in protein folding. Protein Eng 15:871–879
    • (2002) Protein Eng , vol.15 , pp. 871-879
    • George, R.A.1    Heringa, J.2
  • 27
  • 28
    • 0033982651 scopus 로고    scopus 로고
    • Role of linkers in communication between protein modules
    • COI: 1:CAS:528:DC%2BD3cXhtlygtrw%3D, PID: 10679375
    • Gokhale RS, Khosla C (2000) Role of linkers in communication between protein modules. Curr Opin Chem Biol 4:22–27
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 22-27
    • Gokhale, R.S.1    Khosla, C.2
  • 29
    • 76649087970 scopus 로고    scopus 로고
    • Carbohydrate-binding domains: multiplicity of biological roles
    • COI: 1:CAS:528:DC%2BC3cXmvVGmsg%3D%3D, PID: 19908036
    • Guillen D, Sanchez S, Rodriguez-Sanoja R (2010) Carbohydrate-binding domains: multiplicity of biological roles. Appl Microbiol Biotechnol 85:1241–1249
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 1241-1249
    • Guillen, D.1    Sanchez, S.2    Rodriguez-Sanoja, R.3
  • 30
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain-reaction
    • COI: 1:CAS:528:DyaL1MXktVaitrk%3D, PID: 2744487
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR (1989) Site-directed mutagenesis by overlap extension using the polymerase chain-reaction. Gene 77:51–59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 31
    • 34247382001 scopus 로고    scopus 로고
    • Construction of the bifunctional enzyme cellulase-beta-glucosidase from the hyperthermophilic bacterium Thermotoga maritima
    • COI: 1:CAS:528:DC%2BD2sXksVOnsbw%3D, PID: 17333463
    • Hong SY, Lee JS, Cho KM, Math RK, Kim YH, Hong SJ, Cho YU, Cho SJ, Kim H, Yun HD (2007) Construction of the bifunctional enzyme cellulase-beta-glucosidase from the hyperthermophilic bacterium Thermotoga maritima. Biotechnol Lett 29:931–936
    • (2007) Biotechnol Lett , vol.29 , pp. 931-936
    • Hong, S.Y.1    Lee, J.S.2    Cho, K.M.3    Math, R.K.4    Kim, Y.H.5    Hong, S.J.6    Cho, Y.U.7    Cho, S.J.8    Kim, H.9    Yun, H.D.10
  • 32
    • 33749643534 scopus 로고    scopus 로고
    • Assembling a novel bifunctional cellulase-xylanase from Thermotoga maritima by end-to-end fusion
    • COI: 1:CAS:528:DC%2BD28XhtVCntbfE, PID: 16988785
    • Hong SY, Lee JS, Cho KM, Math RK, Kim YH, Hong SJ, Cho YU, Kim H, Yun HD (2006) Assembling a novel bifunctional cellulase-xylanase from Thermotoga maritima by end-to-end fusion. Biotechnol Lett 28:1857–1862
    • (2006) Biotechnol Lett , vol.28 , pp. 1857-1862
    • Hong, S.Y.1    Lee, J.S.2    Cho, K.M.3    Math, R.K.4    Kim, Y.H.5    Hong, S.J.6    Cho, Y.U.7    Kim, H.8    Yun, H.D.9
  • 33
    • 84880865578 scopus 로고    scopus 로고
    • The synergistic action of accessory enzymes enhances the hydrolytic potential of a “cellulase mixture” but is highly substrate specific
    • COI: 1:CAS:528:DC%2BC3sXhtlWgtL3K, PID: 23915398
    • Hu J, Arantes V, Pribowo A, Saddler JN (2013) The synergistic action of accessory enzymes enhances the hydrolytic potential of a “cellulase mixture” but is highly substrate specific. Biotechnol Biofuels 6:112
    • (2013) Biotechnol Biofuels , vol.6 , pp. 112
    • Hu, J.1    Arantes, V.2    Pribowo, A.3    Saddler, J.N.4
  • 34
    • 0017697097 scopus 로고
    • Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin
    • COI: 1:CAS:528:DyaE1cXjsVCjtQ%3D%3D, PID: 412251
    • Itakura K, Hirose T, Crea R, Riggs AD, Heyneker HL, Bolivar F, Boyer HW (1977) Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin. Science 198:1056–1063
    • (1977) Science , vol.198 , pp. 1056-1063
    • Itakura, K.1    Hirose, T.2    Crea, R.3    Riggs, A.D.4    Heyneker, H.L.5    Bolivar, F.6    Boyer, H.W.7
  • 35
    • 84896293907 scopus 로고    scopus 로고
    • A universal cloning method based on yeast homologous recombination that is simple, efficient, and versatile
    • COI: 1:CAS:528:DC%2BC2cXmtlSqtbk%3D, PID: 24418681
    • Joska TM, Mashruwala A, Boyd JM, Belden WJ (2014) A universal cloning method based on yeast homologous recombination that is simple, efficient, and versatile. J Microbiol Methods 100:46–51
    • (2014) J Microbiol Methods , vol.100 , pp. 46-51
    • Joska, T.M.1    Mashruwala, A.2    Boyd, J.M.3    Belden, W.J.4
  • 36
    • 84903467154 scopus 로고    scopus 로고
    • Split-gene system for hybrid wheat seed production
    • COI: 1:CAS:528:DC%2BC2cXnsl2nsLk%3D, PID: 24821800
    • Kempe K, Rubtsova M, Gils M (2014) Split-gene system for hybrid wheat seed production. Proc Natl Acad Sci U S A 111:9097–9102
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 9097-9102
    • Kempe, K.1    Rubtsova, M.2    Gils, M.3
  • 37
    • 46949085932 scopus 로고    scopus 로고
    • Bifunctional xylanases and their potential use in biotechnology
    • COI: 1:CAS:528:DC%2BD1cXot1WjurY%3D, PID: 18365260
    • Khandeparker R, Numan MT (2008) Bifunctional xylanases and their potential use in biotechnology. J Ind Microbiol Biotechnol 35:635–644
    • (2008) J Ind Microbiol Biotechnol , vol.35 , pp. 635-644
    • Khandeparker, R.1    Numan, M.T.2
  • 38
    • 84920254305 scopus 로고    scopus 로고
    • Synergistic proteins for the enhanced enzymatic hydrolysis of cellulose by cellulase
    • COI: 1:CAS:528:DC%2BC2cXhtlOrtrjI, PID: 25129610
    • Kim IJ, Lee HJ, Choi IG, Kim KH (2014) Synergistic proteins for the enhanced enzymatic hydrolysis of cellulose by cellulase. Appl Microbiol Biotechnol 98(20):8469–8480
    • (2014) Appl Microbiol Biotechnol , vol.98 , Issue.20 , pp. 8469-8480
    • Kim, I.J.1    Lee, H.J.2    Choi, I.G.3    Kim, K.H.4
  • 39
    • 78149306410 scopus 로고    scopus 로고
    • Binding modules alter the activity of chimeric cellulases: effects of biomass pretreatment and enzyme source
    • COI: 1:CAS:528:DC%2BC3cXht1Kru7%2FN, PID: 20623472
    • Kim TW, Chokhawala HA, Nadler DC, Blanch HW, Clark DS (2010) Binding modules alter the activity of chimeric cellulases: effects of biomass pretreatment and enzyme source. Biotechnol Bioeng 107:601–611
    • (2010) Biotechnol Bioeng , vol.107 , pp. 601-611
    • Kim, T.W.1    Chokhawala, H.A.2    Nadler, D.C.3    Blanch, H.W.4    Clark, D.S.5
  • 40
    • 67649239793 scopus 로고    scopus 로고
    • Construction, expression and characterization of fusion enzyme from Arthrobacter oxydans dextranase and Klebsiella pneumoniae amylase
    • Kim YM, Ko EA, Kang HK, Kim D (2009) Construction, expression and characterization of fusion enzyme from Arthrobacter oxydans dextranase and Klebsiella pneumoniae amylase. Biotechnol Lett 31:1019–1024
    • (2009) Biotechnol Lett , vol.31 , pp. 1019-1024
    • Kim, Y.M.1    Ko, E.A.2    Kang, H.K.3    Kim, D.4
  • 41
    • 84896124264 scopus 로고    scopus 로고
    • Golden GATEway cloning—a combinatorial approach to generate fusion and recombination constructs
    • PID: 24116091
    • Kirchmaier S, Lust K, Wittbrodt J (2013) Golden GATEway cloning—a combinatorial approach to generate fusion and recombination constructs. PLoS One 8:e76117
    • (2013) PLoS One , vol.8 , pp. 76117
    • Kirchmaier, S.1    Lust, K.2    Wittbrodt, J.3
  • 42
    • 84891045920 scopus 로고    scopus 로고
    • A distinct model of synergism between a processive endocellulase (TfCel9A) and an exocellulase (TfCel48A) from Thermobifida fusca
    • COI: 1:CAS:528:DC%2BC2cXltFGhuw%3D%3D, PID: 24162578
    • Kostylev M, Wilson D (2014) A distinct model of synergism between a processive endocellulase (TfCel9A) and an exocellulase (TfCel48A) from Thermobifida fusca. Appl Environ Microbiol 80:339–344
    • (2014) Appl Environ Microbiol , vol.80 , pp. 339-344
    • Kostylev, M.1    Wilson, D.2
  • 43
    • 84876794300 scopus 로고    scopus 로고
    • Construction of a chimeric thermoacidophilic beta-endoglucanase
    • COI: 1:CAS:528:DC%2BC3sXptFygtLo%3D, PID: 23627611
    • Kufner K, Lipps G (2013) Construction of a chimeric thermoacidophilic beta-endoglucanase. BMC Biochem 14:11
    • (2013) BMC Biochem , vol.14 , pp. 11
    • Kufner, K.1    Lipps, G.2
  • 44
    • 78651473740 scopus 로고    scopus 로고
    • Construction and characterization of different fusion proteins between cellulases and beta-glucosidase to improve glucose production and thermostability
    • COI: 1:CAS:528:DC%2BC3MXhtVenurw%3D, PID: 21169014
    • Lee HL, Chang CK, Teng KH, Liang PH (2011) Construction and characterization of different fusion proteins between cellulases and beta-glucosidase to improve glucose production and thermostability. Bioresour Technol 102:3973–3976
    • (2011) Bioresour Technol , vol.102 , pp. 3973-3976
    • Lee, H.L.1    Chang, C.K.2    Teng, K.H.3    Liang, P.H.4
  • 45
    • 29144464941 scopus 로고    scopus 로고
    • Construction of engineered bifunctional enzymes and their overproduction in Aspergillus niger for improved enzymatic tools to degrade agricultural by-products
    • COI: 1:CAS:528:DC%2BD2MXhtlehtLfI, PID: 16332795
    • Levasseur A, Navarro D, Punt PJ, Belaich JP, Asther M, Record E (2005) Construction of engineered bifunctional enzymes and their overproduction in Aspergillus niger for improved enzymatic tools to degrade agricultural by-products. Appl Environ Microbiol 71:8132–8140
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8132-8140
    • Levasseur, A.1    Navarro, D.2    Punt, P.J.3    Belaich, J.P.4    Asther, M.5    Record, E.6
  • 46
    • 84892857908 scopus 로고    scopus 로고
    • Synergism of cellulase, xylanase, and pectinase on hydrolyzing sugarcane bagasse resulting from different pretreatment technologies
    • COI: 1:CAS:528:DC%2BC2cXmslWqtbg%3D, PID: 24457310
    • Li J, Zhou P, Liu H, Xiong C, Lin J, Xiao W, Gong Y, Liu Z (2014) Synergism of cellulase, xylanase, and pectinase on hydrolyzing sugarcane bagasse resulting from different pretreatment technologies. Bioresour Technol 155:258–265
    • (2014) Bioresour Technol , vol.155 , pp. 258-265
    • Li, J.1    Zhou, P.2    Liu, H.3    Xiong, C.4    Lin, J.5    Xiao, W.6    Gong, Y.7    Liu, Z.8
  • 47
    • 84880105717 scopus 로고    scopus 로고
    • Evaluation of immobilized enzymes for industrial applications
    • COI: 1:CAS:528:DC%2BC3sXhtVKhtrrN, PID: 23446771
    • Liese A, Hilterhaus L (2013) Evaluation of immobilized enzymes for industrial applications. Chem Soc Rev 42:6236–6249
    • (2013) Chem Soc Rev , vol.42 , pp. 6236-6249
    • Liese, A.1    Hilterhaus, L.2
  • 48
    • 64549140192 scopus 로고    scopus 로고
    • Production, purification, and characterization of a fusion protein of carbonic anhydrase from Neisseria gonorrhoeae and cellulose binding domain from Clostridium thermocellum
    • PID: 19224556
    • Liu Z, Bartlow P, Dilmore RM, Soong Y, Pan Z, Koepsel R, Ataai M (2009) Production, purification, and characterization of a fusion protein of carbonic anhydrase from Neisseria gonorrhoeae and cellulose binding domain from Clostridium thermocellum. Biotechnol Prog 25:68–74
    • (2009) Biotechnol Prog , vol.25 , pp. 68-74
    • Liu, Z.1    Bartlow, P.2    Dilmore, R.M.3    Soong, Y.4    Pan, Z.5    Koepsel, R.6    Ataai, M.7
  • 49
    • 44649144487 scopus 로고    scopus 로고
    • Bifunctional enhancement of a beta-glucanase-xylanase fusion enzyme by optimization of peptide linkers
    • COI: 1:CAS:528:DC%2BD1cXmsFKgurY%3D, PID: 18415095
    • Lu P, Feng MG (2008) Bifunctional enhancement of a beta-glucanase-xylanase fusion enzyme by optimization of peptide linkers. Appl Microbiol Biotechnol 79:579–587
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 579-587
    • Lu, P.1    Feng, M.G.2
  • 50
    • 33746543618 scopus 로고    scopus 로고
    • Construction and characterization of a bifunctional fusion enzyme of Bacillus-sourced beta-glucanase and xylanase expressed in Escherichia coli
    • COI: 1:CAS:528:DC%2BD28XovFyhsLk%3D, PID: 16907724
    • Lu P, Feng MG, Li WF, Hu CX (2006) Construction and characterization of a bifunctional fusion enzyme of Bacillus-sourced beta-glucanase and xylanase expressed in Escherichia coli. FEMS Microbiol Lett 261:224–230
    • (2006) FEMS Microbiol Lett , vol.261 , pp. 224-230
    • Lu, P.1    Feng, M.G.2    Li, W.F.3    Hu, C.X.4
  • 51
    • 84904860404 scopus 로고    scopus 로고
    • Design and establishment of a vector system that enables production of multifusion proteins and easy purification by a two-step affinity chromatography approach
    • COI: 1:CAS:528:DC%2BC2cXhtlansLjI, PID: 25026273
    • Marquardt T, von der Heyde A, Elleuche S (2014) Design and establishment of a vector system that enables production of multifusion proteins and easy purification by a two-step affinity chromatography approach. J Microbiol Methods 105:47–50
    • (2014) J Microbiol Methods , vol.105 , pp. 47-50
    • Marquardt, T.1    von der Heyde, A.2    Elleuche, S.3
  • 52
    • 70449377156 scopus 로고    scopus 로고
    • Gemini, a bifunctional enzymatic and fluorescent reporter of gene expression
    • PID: 19888458
    • Martin L, Che A, Endy D (2009) Gemini, a bifunctional enzymatic and fluorescent reporter of gene expression. PLoS One 4:e7569
    • (2009) PLoS One , vol.4 , pp. 7569
    • Martin, L.1    Che, A.2    Endy, D.3
  • 54
    • 33847326289 scopus 로고    scopus 로고
    • Evolution of a Saccharomyces cerevisiae metabolic pathway in Escherichia coli
    • COI: 1:CAS:528:DC%2BD2sXhvVyktbw%3D, PID: 17113805
    • Meynial Salles I, Forchhammer N, Croux C, Girbal L, Soucaille P (2007) Evolution of a Saccharomyces cerevisiae metabolic pathway in Escherichia coli. Metab Eng 9:152–159
    • (2007) Metab Eng , vol.9 , pp. 152-159
    • Meynial Salles, I.1    Forchhammer, N.2    Croux, C.3    Girbal, L.4    Soucaille, P.5
  • 56
    • 34547113519 scopus 로고    scopus 로고
    • Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase
    • COI: 1:CAS:528:DC%2BD2sXotVOgsL0%3D, PID: 17520247
    • Orita I, Sakamoto N, Kato N, Yurimoto H, Sakai Y (2007) Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase. Appl Microbiol Biotechnol 76:439–445
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 439-445
    • Orita, I.1    Sakamoto, N.2    Kato, N.3    Yurimoto, H.4    Sakai, Y.5
  • 57
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • COI: 1:CAS:528:DC%2BD3cXnt1ajtbg%3D, PID: 10966466
    • Paulus H (2000) Protein splicing and related forms of protein autoprocessing. Annu Rev Biochem 69:447–496
    • (2000) Annu Rev Biochem , vol.69 , pp. 447-496
    • Paulus, H.1
  • 58
    • 0035909228 scopus 로고    scopus 로고
    • Kinetics of the coupled reaction catalysed by a fusion protein of beta-galactosidase and galactose dehydrogenase
    • COI: 1:CAS:528:DC%2BD3MXnvFCrs74%3D, PID: 11690652
    • Pettersson H, Pettersson G (2001) Kinetics of the coupled reaction catalysed by a fusion protein of beta-galactosidase and galactose dehydrogenase. Biochim Biophys Acta 1549:155–160
    • (2001) Biochim Biophys Acta , vol.1549 , pp. 155-160
    • Pettersson, H.1    Pettersson, G.2
  • 59
    • 79953157902 scopus 로고    scopus 로고
    • Stability of a guest protein depends on stability of a host protein in insertional fusion
    • COI: 1:CAS:528:DC%2BC3MXjvV2qtbk%3D, PID: 21190177
    • Pierre B, Xiong T, Hayles L, Guntaka VR, Kim JR (2011) Stability of a guest protein depends on stability of a host protein in insertional fusion. Biotechnol Bioeng 108:1011–1020
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1011-1020
    • Pierre, B.1    Xiong, T.2    Hayles, L.3    Guntaka, V.R.4    Kim, J.R.5
  • 63
    • 0031831457 scopus 로고    scopus 로고
    • Intramolecular synergism in an engineered exo-endo-1,4-beta-glucanase fusion protein
    • COI: 1:CAS:528:DyaK1cXjsFSgsrk%3D, PID: 9643544
    • Riedel K, Bronnenmeier K (1998) Intramolecular synergism in an engineered exo-endo-1,4-beta-glucanase fusion protein. Mol Microbiol 28:767–775
    • (1998) Mol Microbiol , vol.28 , pp. 767-775
    • Riedel, K.1    Bronnenmeier, K.2
  • 64
    • 84868374454 scopus 로고    scopus 로고
    • End-to-end gene fusions and their impact on the production of multifunctional biomass degrading enzymes
    • COI: 1:CAS:528:DC%2BC38XhsFymtbvM, PID: 23058915
    • Rizk M, Antranikian G, Elleuche S (2012) End-to-end gene fusions and their impact on the production of multifunctional biomass degrading enzymes. Biochem Biophys Res Commun 428:1–5
    • (2012) Biochem Biophys Res Commun , vol.428 , pp. 1-5
    • Rizk, M.1    Antranikian, G.2    Elleuche, S.3
  • 65
    • 84924283158 scopus 로고    scopus 로고
    • Rizk M, Elleuche S, Antranikian G (2015). Generating bifunctional fusion enzymes composed of heat-active endoglucanase (Cel5A) and endoxylanase (XylT). Biotechnol Lett (In press)
    • Rizk M, Elleuche S, Antranikian G (2015). Generating bifunctional fusion enzymes composed of heat-active endoglucanase (Cel5A) and endoxylanase (XylT). Biotechnol Lett (In press)
  • 66
    • 84891412552 scopus 로고    scopus 로고
    • Inteins: nature’s gift to protein chemists
    • COI: 1:CAS:528:DC%2BC3sXitVSqtbzJ, PID: 24634716
    • Shah NH, Muir TW (2014) Inteins: nature’s gift to protein chemists. Chem Sci 5:446–461
    • (2014) Chem Sci , vol.5 , pp. 446-461
    • Shah, N.H.1    Muir, T.W.2
  • 68
    • 70350337095 scopus 로고    scopus 로고
    • Fluorescent proteins: a cell biologist’s user guide
    • COI: 1:CAS:528:DC%2BD1MXhtlChurnF, PID: 19819147
    • Snapp EL (2009) Fluorescent proteins: a cell biologist’s user guide. Trends Cell Biol 19:649–655
    • (2009) Trends Cell Biol , vol.19 , pp. 649-655
    • Snapp, E.L.1
  • 69
    • 79251638276 scopus 로고    scopus 로고
    • Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag
    • Takano K, Okamoto T, Okada J, Tanaka S, Angkawidjaja C, Koga Y, Kanaya S (2011) Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag. PLoS One 6:e16226
    • (2011) PLoS One , vol.e16226 , pp. 6
    • Takano, K.1    Okamoto, T.2    Okada, J.3    Tanaka, S.4    Angkawidjaja, C.5    Koga, Y.6    Kanaya, S.7
  • 70
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems
    • COI: 1:CAS:528:DC%2BD3sXjvFGntQ%3D%3D, PID: 12536251
    • Terpe K (2003) Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biotechnol 60:523–533
    • (2003) Appl Microbiol Biotechnol , vol.60 , pp. 523-533
    • Terpe, K.1
  • 71
    • 84880913078 scopus 로고    scopus 로고
    • Selecting beta-glucosidases to support cellulases in cellulose saccharification
    • COI: 1:CAS:528:DC%2BC3sXhtlWgtLrN, PID: 23883540
    • Teugjas H, Valjamae P (2013) Selecting beta-glucosidases to support cellulases in cellulose saccharification. Biotechnol Biofuels 6:105
    • (2013) Biotechnol Biofuels , vol.6 , pp. 105
    • Teugjas, H.1    Valjamae, P.2
  • 72
    • 84875786949 scopus 로고    scopus 로고
    • Fusion of cellulose binding domain from Trichoderma reesei CBHI to Cryptococcus sp. S-2 cellulase enhances its binding affinity and its cellulolytic activity to insoluble cellulosic substrates
    • Thongekkaew J, Ikeda H, Masaki K, Iefuji H (2013) Fusion of cellulose binding domain from Trichoderma reesei CBHI to Cryptococcus sp. S-2 cellulase enhances its binding affinity and its cellulolytic activity to insoluble cellulosic substrates. Enzyme Microb Technol 52:241–246
    • (2013) Enzyme Microb Technol , vol.52 , pp. 241-246
    • Thongekkaew, J.1    Ikeda, H.2    Masaki, K.3    Iefuji, H.4
  • 73
    • 84876461880 scopus 로고    scopus 로고
    • Recent progress in intein research: from mechanism to directed evolution and applications
    • COI: 1:CAS:528:DC%2BC3sXkt1Khtbg%3D, PID: 22926412
    • Volkmann G, Mootz HD (2013) Recent progress in intein research: from mechanism to directed evolution and applications. Cell Mol Life Sci 70:1185–1206
    • (2013) Cell Mol Life Sci , vol.70 , pp. 1185-1206
    • Volkmann, G.1    Mootz, H.D.2
  • 75
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • COI: 1:CAS:528:DC%2BD2MXks1Cms78%3D, PID: 15922084
    • Waugh DS (2005) Making the most of affinity tags. Trends Biotechnol 23:316–320
    • (2005) Trends Biotechnol , vol.23 , pp. 316-320
    • Waugh, D.S.1
  • 76
    • 67650687073 scopus 로고    scopus 로고
    • You’re one in a googol: optimizing genes for protein expression
    • COI: 1:CAS:528:DC%2BD1MXpslOqtb8%3D, PID: 19324676
    • Welch M, Villalobos A, Gustafsson C, Minshull J (2009) You’re one in a googol: optimizing genes for protein expression. J R Soc Interface 6(Suppl 4):S467–S476
    • (2009) J R Soc Interface , vol.6 , pp. 467-476
    • Welch, M.1    Villalobos, A.2    Gustafsson, C.3    Minshull, J.4
  • 78
    • 0036861615 scopus 로고    scopus 로고
    • Enhanced stress tolerance in Escherichia coli and Nicotiana tabacum expressing a betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein
    • COI: 1:CAS:528:DC%2BD38Xoslarur4%3D, PID: 12467448
    • Yilmaz JL, Bülow L (2002) Enhanced stress tolerance in Escherichia coli and Nicotiana tabacum expressing a betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein. Biotechnol Prog 18:1176–1182
    • (2002) Biotechnol Prog , vol.18 , pp. 1176-1182
    • Yilmaz, J.L.1    Bülow, L.2
  • 79
    • 0014966626 scopus 로고
    • Enzyme evolution: generation of a bifunctional enzyme by fusion of adjacent genes
    • COI: 1:CAS:528:DyaE3MXjvFKntA%3D%3D, PID: 4920435
    • Yourno J, Kohno T, Roth JR (1970) Enzyme evolution: generation of a bifunctional enzyme by fusion of adjacent genes. Nature 228:820–824
    • (1970) Nature , vol.228 , pp. 820-824
    • Yourno, J.1    Kohno, T.2    Roth, J.R.3
  • 80
    • 36248983896 scopus 로고    scopus 로고
    • Rational design of a chimeric endonuclease targeted to NotI recognition site
    • Zhang P, Bao Y, Higgins L, Xu SY (2007) Rational design of a chimeric endonuclease targeted to NotI recognition site. Protein Eng Des Sel 20:497–504
    • (2007) Protein Eng Des Sel , vol.20 , pp. 497-504
    • Zhang, P.1    Bao, Y.2    Higgins, L.3    Xu, S.Y.4
  • 81
    • 84887348704 scopus 로고    scopus 로고
    • Enzymatic properties of Thermoanaerobacterium thermosaccharolyticum beta-glucosidase fused to Clostridium cellulovorans cellulose binding domain and its application in hydrolysis of microcrystalline cellulose
    • COI: 1:CAS:528:DC%2BC3sXhvVKnurnF, PID: 24228818
    • Zhao L, Pang Q, Xie J, Pei J, Wang F, Fan S (2013) Enzymatic properties of Thermoanaerobacterium thermosaccharolyticum beta-glucosidase fused to Clostridium cellulovorans cellulose binding domain and its application in hydrolysis of microcrystalline cellulose. BMC Biotechnol 13:101
    • (2013) BMC Biotechnol , vol.13 , pp. 101
    • Zhao, L.1    Pang, Q.2    Xie, J.3    Pei, J.4    Wang, F.5    Fan, S.6
  • 82
    • 0031889118 scopus 로고    scopus 로고
    • Properties and gene structure of a bifunctional cellulolytic enzyme (CelA) from the extreme thermophile ‘Anaerocellum thermophilum’ with separate glycosyl hydrolase family 9 and 48 catalytic domains
    • COI: 1:CAS:528:DyaK1cXhtlanur0%3D, PID: 9493383
    • Zverlov V, Mahr S, Riedel K, Bronnenmeier K (1998) Properties and gene structure of a bifunctional cellulolytic enzyme (CelA) from the extreme thermophile ‘Anaerocellum thermophilum’ with separate glycosyl hydrolase family 9 and 48 catalytic domains. Microbiology 144(Pt 2):457–465
    • (1998) Microbiology , vol.144 , pp. 457-465
    • Zverlov, V.1    Mahr, S.2    Riedel, K.3    Bronnenmeier, K.4


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