메뉴 건너뛰기




Volumn 33, Issue 5, 2015, Pages 435-456

Strategies for the one-step immobilization-purification of enzymes as industrial biocatalysts

Author keywords

Chimeric proteins; Controlled immobilization; Covalent attachment; Enzyme stabilization; IMAC; Ionic exchange; Multimeric enzymes

Indexed keywords

ION EXCHANGE; PURIFICATION; SILICATES;

EID: 84931008392     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2015.03.006     Document Type: Review
Times cited : (591)

References (178)
  • 1
    • 84904815258 scopus 로고    scopus 로고
    • Additives enhancing the catalytic properties of lipase from Burkholderia cepacia immobilized on mixed-function-grafted mesoporous silica gel
    • Abaházi E., Boros Z., Poppe L. Additives enhancing the catalytic properties of lipase from Burkholderia cepacia immobilized on mixed-function-grafted mesoporous silica gel. Molecules 2014, 19:9818-9837.
    • (2014) Molecules , vol.19 , pp. 9818-9837
    • Abaházi, E.1    Boros, Z.2    Poppe, L.3
  • 2
    • 2342591293 scopus 로고    scopus 로고
    • Stabilization of penicillin G acylase from Escherichia coli: site-directed mutagenesis of the protein surface to increase multipoint covalent attachment
    • Abian O., Grazú V., Hermoso J., González R., García J.L., Fernández-Lafuente R., et al. Stabilization of penicillin G acylase from Escherichia coli: site-directed mutagenesis of the protein surface to increase multipoint covalent attachment. Appl Environ Microbiol 2004, 70:1249-1251.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 1249-1251
    • Abian, O.1    Grazú, V.2    Hermoso, J.3    González, R.4    García, J.L.5    Fernández-Lafuente, R.6
  • 3
    • 33747755500 scopus 로고    scopus 로고
    • Specific capture of target proteins by oriented antibodies bound to tyrosinase-immobilized Protein A on a polyallylamine affinity membrane surface
    • Ahmed S.R., Lutes A.T., Barbari T.A. Specific capture of target proteins by oriented antibodies bound to tyrosinase-immobilized Protein A on a polyallylamine affinity membrane surface. J Membr Sci 2006, 282:311-321.
    • (2006) J Membr Sci , vol.282 , pp. 311-321
    • Ahmed, S.R.1    Lutes, A.T.2    Barbari, T.A.3
  • 4
    • 80052508281 scopus 로고    scopus 로고
    • Characterization of a novel immobilized biocatalyst obtained by matrix-assisted refolding of recombinant polyhydroxyoctanoate depolymerase from Pseudomonas putida KT2442 isolated from inclusion bodies
    • Arroyo M., García-Hidalgo J., Villalón M., De Eugenio L., Hormigo D., Acebal C., et al. Characterization of a novel immobilized biocatalyst obtained by matrix-assisted refolding of recombinant polyhydroxyoctanoate depolymerase from Pseudomonas putida KT2442 isolated from inclusion bodies. J Ind Microbiol Biotechnol 2011, 38:1203-1209.
    • (2011) J Ind Microbiol Biotechnol , vol.38 , pp. 1203-1209
    • Arroyo, M.1    García-Hidalgo, J.2    Villalón, M.3    De Eugenio, L.4    Hormigo, D.5    Acebal, C.6
  • 5
    • 84859431657 scopus 로고    scopus 로고
    • The slow-down of the CALB immobilization rate permits to control the inter and intra molecular modification produced by glutaraldehyde
    • Barbosa O., Torres R., Ortiz C., Fernandez-Lafuente R. The slow-down of the CALB immobilization rate permits to control the inter and intra molecular modification produced by glutaraldehyde. Process Biochem 2012, 47:766-774.
    • (2012) Process Biochem , vol.47 , pp. 766-774
    • Barbosa, O.1    Torres, R.2    Ortiz, C.3    Fernandez-Lafuente, R.4
  • 6
    • 84881561590 scopus 로고    scopus 로고
    • Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties
    • Barbosa O., Torres R., Ortiz C., Berenguer-Murcia Á., Rodrigues R.C., Fernandez-Lafuente R. Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties. Biomacromolecules 2013, 40:2433-2462.
    • (2013) Biomacromolecules , vol.40 , pp. 2433-2462
    • Barbosa, O.1    Torres, R.2    Ortiz, C.3    Berenguer-Murcia, Á.4    Rodrigues, R.C.5    Fernandez-Lafuente, R.6
  • 7
    • 0032486523 scopus 로고    scopus 로고
    • A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports
    • Bastida A., Sabuquillo P., Armisen P., Fernández-Lafuente R., Huguet J., Guisán J.M. A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports. Biotechnol Bioeng 1998, 58:486-493.
    • (1998) Biotechnol Bioeng , vol.58 , pp. 486-493
    • Bastida, A.1    Sabuquillo, P.2    Armisen, P.3    Fernández-Lafuente, R.4    Huguet, J.5    Guisán, J.M.6
  • 9
    • 52749088977 scopus 로고    scopus 로고
    • Covalent immobilization of antibodies on finally inert support surfaces through their surface regions having the highest densities in carboxyl groups
    • Batalla P., Fuentes M., Mateo C., Grazu V., Fernandez-Lafuente R., Guisan J.M. Covalent immobilization of antibodies on finally inert support surfaces through their surface regions having the highest densities in carboxyl groups. Biomacromolecules 2008, 9:2230-2236.
    • (2008) Biomacromolecules , vol.9 , pp. 2230-2236
    • Batalla, P.1    Fuentes, M.2    Mateo, C.3    Grazu, V.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 10
    • 0032441468 scopus 로고    scopus 로고
    • Indirect immobilization of recombinant proteins to a solid phase using the albumin binding domain of streptococcal protein G and immobilized albumin
    • Baumann S., Grob P., Stuart F., Pertlik D., Ackermann M., Suter M. Indirect immobilization of recombinant proteins to a solid phase using the albumin binding domain of streptococcal protein G and immobilized albumin. J Immunol Methods 1998, 221:95-106.
    • (1998) J Immunol Methods , vol.221 , pp. 95-106
    • Baumann, S.1    Grob, P.2    Stuart, F.3    Pertlik, D.4    Ackermann, M.5    Suter, M.6
  • 11
    • 84900444685 scopus 로고    scopus 로고
    • Specific and reversible immobilization of proteins tagged to the affinity polypeptide C-LytA on functionalized graphite electrodes
    • Bello-Gil D., Maestro B., Fonseca J., Feliu J.M., Climent V., Sanz J.M. Specific and reversible immobilization of proteins tagged to the affinity polypeptide C-LytA on functionalized graphite electrodes. PLoS One 2014, 9.
    • (2014) PLoS One , vol.9
    • Bello-Gil, D.1    Maestro, B.2    Fonseca, J.3    Feliu, J.M.4    Climent, V.5    Sanz, J.M.6
  • 12
    • 63549119129 scopus 로고    scopus 로고
    • Self-renaturing enzymes: design of an enzyme-chaperone chimera as a new approach to enzyme stabilization
    • Bergeron L.M., Gomez L., Whitehead T.A., Clark D.S. Self-renaturing enzymes: design of an enzyme-chaperone chimera as a new approach to enzyme stabilization. Biotechnol Bioeng 2009, 102:1316-1322.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 1316-1322
    • Bergeron, L.M.1    Gomez, L.2    Whitehead, T.A.3    Clark, D.S.4
  • 13
    • 84897517557 scopus 로고    scopus 로고
    • Heterofunctional hydrophilic-hydrophobic porous silica as support for multipoint covalent immobilization of lipases: application to lactulose palmitate synthesis
    • Bernal C., Illanes A., Wilson L. Heterofunctional hydrophilic-hydrophobic porous silica as support for multipoint covalent immobilization of lipases: application to lactulose palmitate synthesis. Langmuir 2014, 30:3557-3566.
    • (2014) Langmuir , vol.30 , pp. 3557-3566
    • Bernal, C.1    Illanes, A.2    Wilson, L.3
  • 14
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • Binz H.K., Amstutz P., Plückthun A. Engineering novel binding proteins from nonimmunoglobulin domains. Nat Biotechnol 2005, 23:1257-1268.
    • (2005) Nat Biotechnol , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Plückthun, A.3
  • 15
    • 0024677047 scopus 로고
    • Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives
    • Blanco R.M., Guisán J. Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives. Enzyme Microb Technol 1989, 11:360-366.
    • (1989) Enzyme Microb Technol , vol.11 , pp. 360-366
    • Blanco, R.M.1    Guisán, J.2
  • 16
    • 84863452401 scopus 로고    scopus 로고
    • Positively charged mini-protein Z basic2 as a highly efficient silica binding module: opportunities for enzyme immobilization on unmodified silica supports
    • Bolivar J.M., Nidetzky B. Positively charged mini-protein Z basic2 as a highly efficient silica binding module: opportunities for enzyme immobilization on unmodified silica supports. Langmuir 2012, 28:10040-10049.
    • (2012) Langmuir , vol.28 , pp. 10040-10049
    • Bolivar, J.M.1    Nidetzky, B.2
  • 17
    • 84859889749 scopus 로고    scopus 로고
    • Oriented and selective enzyme immobilization on functionalized silica carrier using the cationic binding module Z basic2: design of a heterogeneous d-amino acid oxidase catalyst on porous glass
    • Bolivar J.M., Nidetzky B. Oriented and selective enzyme immobilization on functionalized silica carrier using the cationic binding module Z basic2: design of a heterogeneous d-amino acid oxidase catalyst on porous glass. Biotechnol Bioeng 2012, 109:1490-1498.
    • (2012) Biotechnol Bioeng , vol.109 , pp. 1490-1498
    • Bolivar, J.M.1    Nidetzky, B.2
  • 18
  • 19
    • 58149296120 scopus 로고    scopus 로고
    • The adsorption of multimeric enzymes on very lowly activated supports involves more enzyme subunits: stabilization of a glutamate dehydrogenase from Thermus thermophilus by immobilization on heterofunctional supports
    • Bolivar J.M., Mateo C., Rocha-Martin J., Cava F., Berenguer J., Fernandez-Lafuente R., et al. The adsorption of multimeric enzymes on very lowly activated supports involves more enzyme subunits: stabilization of a glutamate dehydrogenase from Thermus thermophilus by immobilization on heterofunctional supports. Enzyme Microb Technol 2009, 44:139-144.
    • (2009) Enzyme Microb Technol , vol.44 , pp. 139-144
    • Bolivar, J.M.1    Mateo, C.2    Rocha-Martin, J.3    Cava, F.4    Berenguer, J.5    Fernandez-Lafuente, R.6
  • 20
    • 63249128248 scopus 로고    scopus 로고
    • Purification and stabilization of a glutamate dehygrogenase from Thermus thermophilus via oriented multisubunit plus multipoint covalent immobilization
    • Bolivar J.M., Rocha-Martin J., Mateo C., Cava F., Berenguer J., Vega D., et al. Purification and stabilization of a glutamate dehygrogenase from Thermus thermophilus via oriented multisubunit plus multipoint covalent immobilization. J Mol Catal B: Enzym 2009, 58:158-163.
    • (2009) J Mol Catal B: Enzym , vol.58 , pp. 158-163
    • Bolivar, J.M.1    Rocha-Martin, J.2    Mateo, C.3    Cava, F.4    Berenguer, J.5    Vega, D.6
  • 21
    • 77956170052 scopus 로고    scopus 로고
    • Heterofunctional supports for the one-step purification, immobilization and stabilization of large multimeric enzymes: amino-glyoxyl versus amino-epoxy supports
    • Bolivar J.M., Mateo C., Grazu V., Carrascosa A.V., Pessela B.C., Guisan J.M. Heterofunctional supports for the one-step purification, immobilization and stabilization of large multimeric enzymes: amino-glyoxyl versus amino-epoxy supports. Process Biochem 2010, 45:1692-1698.
    • (2010) Process Biochem , vol.45 , pp. 1692-1698
    • Bolivar, J.M.1    Mateo, C.2    Grazu, V.3    Carrascosa, A.V.4    Pessela, B.C.5    Guisan, J.M.6
  • 22
    • 70449631056 scopus 로고    scopus 로고
    • Complete reactivation of immobilized derivatives of a trimeric glutamate dehydrogenase from Thermus thermophillus
    • Bolivar J.M., Rocha-Martin J., Godoy C., Rodrigues R.C., Guisan J.M. Complete reactivation of immobilized derivatives of a trimeric glutamate dehydrogenase from Thermus thermophillus. Process Biochem 2010, 45:107-113.
    • (2010) Process Biochem , vol.45 , pp. 107-113
    • Bolivar, J.M.1    Rocha-Martin, J.2    Godoy, C.3    Rodrigues, R.C.4    Guisan, J.M.5
  • 23
    • 84880065854 scopus 로고    scopus 로고
    • Hydrophobic adsorption and covalent immobilization of Candida antarctica lipase B on mixed-function-grafted silica gel supports for continuous-flow biotransformations
    • Boros Z., Weiser D., Márkus M., Abaháziová E., Magyar Á., Tomin A., et al. Hydrophobic adsorption and covalent immobilization of Candida antarctica lipase B on mixed-function-grafted silica gel supports for continuous-flow biotransformations. Process Biochem 2013, 48:1039-1047.
    • (2013) Process Biochem , vol.48 , pp. 1039-1047
    • Boros, Z.1    Weiser, D.2    Márkus, M.3    Abaháziová, E.4    Magyar, Á.5    Tomin, A.6
  • 24
    • 70350257632 scopus 로고    scopus 로고
    • Advances in enzyme immobilisation
    • Brady D., Jordaan J. Advances in enzyme immobilisation. Biotechnol Lett 2009, 31:1639-1650.
    • (2009) Biotechnol Lett , vol.31 , pp. 1639-1650
    • Brady, D.1    Jordaan, J.2
  • 25
    • 0025057072 scopus 로고
    • A serine protease triad forms the catalytic centre of a triacylglycerol lipase
    • Brady L., Brzozowski A.M., Derewenda Z.S., Dodson E., Dodson G., Tolley S., et al. A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 1990, 343:767-770.
    • (1990) Nature , vol.343 , pp. 767-770
    • Brady, L.1    Brzozowski, A.M.2    Derewenda, Z.S.3    Dodson, E.4    Dodson, G.5    Tolley, S.6
  • 26
    • 0026418174 scopus 로고
    • A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex
    • Brzozowski A.M., Derewenda U., Derewenda Z.S., Dodson G.G., Lawson D.M., Turkenburg J.P., et al. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 1991, 351:491-494.
    • (1991) Nature , vol.351 , pp. 491-494
    • Brzozowski, A.M.1    Derewenda, U.2    Derewenda, Z.S.3    Dodson, G.G.4    Lawson, D.M.5    Turkenburg, J.P.6
  • 29
    • 35549010175 scopus 로고    scopus 로고
    • New active site oriented glyoxyl-agarose derivatives of Escherichia coli penicillin G acylase
    • Cecchini D.A., Serra I., Ubiali D., Terreni M., Albertini A.M. New active site oriented glyoxyl-agarose derivatives of Escherichia coli penicillin G acylase. BMC Biotechnol 2007, 7.
    • (2007) BMC Biotechnol , vol.7
    • Cecchini, D.A.1    Serra, I.2    Ubiali, D.3    Terreni, M.4    Albertini, A.M.5
  • 30
    • 84872010935 scopus 로고    scopus 로고
    • Efficient biocatalyst for large-scale synthesis of cephalosporins, obtained by combining immobilization and site-directed mutagenesis of penicillin acylase
    • Cecchini D.A., Pavesi R., Sanna S., Daly S., Xaiz R., Pregnolato M., et al. Efficient biocatalyst for large-scale synthesis of cephalosporins, obtained by combining immobilization and site-directed mutagenesis of penicillin acylase. Appl Microbiol Biotechnol 2012, 95:1491-1500.
    • (2012) Appl Microbiol Biotechnol , vol.95 , pp. 1491-1500
    • Cecchini, D.A.1    Pavesi, R.2    Sanna, S.3    Daly, S.4    Xaiz, R.5    Pregnolato, M.6
  • 31
    • 18144390619 scopus 로고    scopus 로고
    • Chitin-binding domain based immobilization of d-hydantoinase
    • Chern J.T., Chao Y.P. Chitin-binding domain based immobilization of d-hydantoinase. J Biotechnol 2005, 117:267-275.
    • (2005) J Biotechnol , vol.117 , pp. 267-275
    • Chern, J.T.1    Chao, Y.P.2
  • 32
    • 50449093743 scopus 로고    scopus 로고
    • Facile immobilization of evolved Agrobacterium radiobacter carbamoylase with high thermal and oxidative stability
    • Chiang C.J., Chern J.T., Wang J.Y., Chao Y.P. Facile immobilization of evolved Agrobacterium radiobacter carbamoylase with high thermal and oxidative stability. J Agric Food Chem 2008, 56:6348-6354.
    • (2008) J Agric Food Chem , vol.56 , pp. 6348-6354
    • Chiang, C.J.1    Chern, J.T.2    Wang, J.Y.3    Chao, Y.P.4
  • 33
    • 60549105192 scopus 로고    scopus 로고
    • Enhanced levan production using chitin-binding domain fused levansucrase immobilized on chitin beads
    • Chiang C.J., Wang J.Y., Chen P.T., Chao Y.P. Enhanced levan production using chitin-binding domain fused levansucrase immobilized on chitin beads. Appl Microbiol Biotechnol 2009, 82:445-451.
    • (2009) Appl Microbiol Biotechnol , vol.82 , pp. 445-451
    • Chiang, C.J.1    Wang, J.Y.2    Chen, P.T.3    Chao, Y.P.4
  • 34
    • 34247381635 scopus 로고    scopus 로고
    • Site-directed biotinylation of antibodies for controlled immobilization on solid surfaces
    • Cho I.H., Paek E.H., Lee H., Kang J.Y., Kim T.S., Paek S.H. Site-directed biotinylation of antibodies for controlled immobilization on solid surfaces. Anal Biochem 2007, 365:14-23.
    • (2007) Anal Biochem , vol.365 , pp. 14-23
    • Cho, I.H.1    Paek, E.H.2    Lee, H.3    Kang, J.Y.4    Kim, T.S.5    Paek, S.H.6
  • 38
    • 0026786234 scopus 로고
    • The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9Å resolution
    • Derewenda Z.S., Derewenda U., Dodson G.G. The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9Å resolution. J Mol Biol 1992, 227:818-839.
    • (1992) J Mol Biol , vol.227 , pp. 818-839
    • Derewenda, Z.S.1    Derewenda, U.2    Dodson, G.G.3
  • 41
    • 34248534296 scopus 로고    scopus 로고
    • Polyclonal antibodies mediated immobilization of a peroxidase from ammonium sulphate fractionated bitter gourd (Momordica charantia) proteins
    • Fatima A., Husain Q. Polyclonal antibodies mediated immobilization of a peroxidase from ammonium sulphate fractionated bitter gourd (Momordica charantia) proteins. Biomol Eng 2007, 24:223-230.
    • (2007) Biomol Eng , vol.24 , pp. 223-230
    • Fatima, A.1    Husain, Q.2
  • 42
    • 70349782241 scopus 로고    scopus 로고
    • Stabilization of multimeric enzymes: strategies to prevent subunit dissociation
    • Fernandez-Lafuente R. Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb Technol 2009, 45:405-418.
    • (2009) Enzyme Microb Technol , vol.45 , pp. 405-418
    • Fernandez-Lafuente, R.1
  • 46
    • 34547537549 scopus 로고    scopus 로고
    • Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports
    • Fernández-Lorente G., Palomo J.M., Cabrera Z., Guisán J.M., Fernández-Lafuente R. Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports. Enzyme Microb Technol 2007, 41:565-569.
    • (2007) Enzyme Microb Technol , vol.41 , pp. 565-569
    • Fernández-Lorente, G.1    Palomo, J.M.2    Cabrera, Z.3    Guisán, J.M.4    Fernández-Lafuente, R.5
  • 47
    • 50449108577 scopus 로고    scopus 로고
    • Interfacially activated lipases against hydrophobic supports: Effect of the support nature on the biocatalytic properties
    • Fernandez-Lorente G., Cabrera Z., Godoy C., Fernandez-Lafuente R., Palomo J.M., Guisan J.M. Interfacially activated lipases against hydrophobic supports: Effect of the support nature on the biocatalytic properties. Process Biochem 2008, 43:1061-1067.
    • (2008) Process Biochem , vol.43 , pp. 1061-1067
    • Fernandez-Lorente, G.1    Cabrera, Z.2    Godoy, C.3    Fernandez-Lafuente, R.4    Palomo, J.M.5    Guisan, J.M.6
  • 48
    • 84931004943 scopus 로고    scopus 로고
    • Cross-linking of lipases adsorbed on hydrophobic supports: highly selective hydrolysis of fish oil catalyzed by RML
    • Fernandez-Lorente G., Filice M., Lopez-Vela D., Pizarro C., Wilson L., Betancor L., et al. Cross-linking of lipases adsorbed on hydrophobic supports: highly selective hydrolysis of fish oil catalyzed by RML. J Am Oil Chem Soc 2010, 1-7.
    • (2010) J Am Oil Chem Soc , pp. 1-7
    • Fernandez-Lorente, G.1    Filice, M.2    Lopez-Vela, D.3    Pizarro, C.4    Wilson, L.5    Betancor, L.6
  • 49
    • 0037072993 scopus 로고    scopus 로고
    • Stabilization of horseradish peroxidase in aqueous-organic media by immobilization onto cellulose using a cellulose-binding-domain
    • Fishman A., Levy I., Cogan U., Shoseyov O. Stabilization of horseradish peroxidase in aqueous-organic media by immobilization onto cellulose using a cellulose-binding-domain. J Mol Catal B: Enzym 2002, 18:121-131.
    • (2002) J Mol Catal B: Enzym , vol.18 , pp. 121-131
    • Fishman, A.1    Levy, I.2    Cogan, U.3    Shoseyov, O.4
  • 50
    • 22444439952 scopus 로고    scopus 로고
    • Polyarginine as a multifunctional fusion tag
    • Fuchs S.M., Raines R.T. Polyarginine as a multifunctional fusion tag. Protein Sci 2005, 14:1538-1544.
    • (2005) Protein Sci , vol.14 , pp. 1538-1544
    • Fuchs, S.M.1    Raines, R.T.2
  • 51
    • 9144241209 scopus 로고    scopus 로고
    • Detection and purification of two antibody-antigen complexes via selective adsorption on lowly activated anion exchangers
    • Fuentes M., Pessela B.C.C., Mateo C., Munilla R., Guisán J.M., Fernandez-Lafuente R. Detection and purification of two antibody-antigen complexes via selective adsorption on lowly activated anion exchangers. J Chromatogr A 2004, 1059:89-94.
    • (2004) J Chromatogr A , vol.1059 , pp. 89-94
    • Fuentes, M.1    Pessela, B.C.C.2    Mateo, C.3    Munilla, R.4    Guisán, J.M.5    Fernandez-Lafuente, R.6
  • 52
    • 10044261711 scopus 로고    scopus 로고
    • Preparation of inert magnetic nano-particles for the directed immobilization of antibodies
    • Fuentes M., Mateo C., Guisán J.M., Fernández-Lafuente R. Preparation of inert magnetic nano-particles for the directed immobilization of antibodies. Biosens Bioelectron 2005, 20:1380-1387.
    • (2005) Biosens Bioelectron , vol.20 , pp. 1380-1387
    • Fuentes, M.1    Mateo, C.2    Guisán, J.M.3    Fernández-Lafuente, R.4
  • 53
    • 27744538409 scopus 로고    scopus 로고
    • Purification, stabilization, and concentration of very weak protein-protein complexes: shifting the association equilibrium via complex selective adsorption on lowly activated supports
    • Fuentes M., Mateo C., Pessela B.C.C., Guisán J.M., Fernandez-Lafuente R. Purification, stabilization, and concentration of very weak protein-protein complexes: shifting the association equilibrium via complex selective adsorption on lowly activated supports. Proteomics 2005, 5:4062-4069.
    • (2005) Proteomics , vol.5 , pp. 4062-4069
    • Fuentes, M.1    Mateo, C.2    Pessela, B.C.C.3    Guisán, J.M.4    Fernandez-Lafuente, R.5
  • 54
    • 33646360190 scopus 로고    scopus 로고
    • Adsorption behavior of bovine serum albumin on lowly activated anionic exchangers suggests a new strategy for solid-phase proteomics
    • Fuentes M., Pessela B.C.C., Mateo C., Palomo J.M., Batalla P., Fernández-Lafuente R., et al. Adsorption behavior of bovine serum albumin on lowly activated anionic exchangers suggests a new strategy for solid-phase proteomics. Biomacromolecules 2006, 7:1357-1361.
    • (2006) Biomacromolecules , vol.7 , pp. 1357-1361
    • Fuentes, M.1    Pessela, B.C.C.2    Mateo, C.3    Palomo, J.M.4    Batalla, P.5    Fernández-Lafuente, R.6
  • 58
    • 0034536389 scopus 로고    scopus 로고
    • Charge engineering of a protein domain to allow efficient ion-exchange recovery
    • Gräslund T., Lundin G., Uhlén M., Nygren P.-Å., Hober S. Charge engineering of a protein domain to allow efficient ion-exchange recovery. Protein Eng 2000, 13:703-709.
    • (2000) Protein Eng , vol.13 , pp. 703-709
    • Gräslund, T.1    Lundin, G.2    Uhlén, M.3    Nygren, P.-Å.4    Hober, S.5
  • 59
    • 0037016340 scopus 로고    scopus 로고
    • Strategy for highly selective ion-exchange capture using a charge-polarizing fusion partner
    • Gräslund T., Ehn M., Lundin G., Hedhammar M., Uhlén M., Nygren P.Å., et al. Strategy for highly selective ion-exchange capture using a charge-polarizing fusion partner. J Chromatogr A 2002, 942:157-166.
    • (2002) J Chromatogr A , vol.942 , pp. 157-166
    • Gräslund, T.1    Ehn, M.2    Lundin, G.3    Hedhammar, M.4    Uhlén, M.5    Nygren, P.Å.6
  • 60
    • 0037071909 scopus 로고    scopus 로고
    • Integrated strategy for selective expanded bed ion-exchange adsorption and site-specific protein processing using gene fusion technology
    • Gräslund T., Hedhammar M., Uhlén M., Nygren P.Å., Hober S. Integrated strategy for selective expanded bed ion-exchange adsorption and site-specific protein processing using gene fusion technology. J Biotechnol 2002, 96:93-102.
    • (2002) J Biotechnol , vol.96 , pp. 93-102
    • Gräslund, T.1    Hedhammar, M.2    Uhlén, M.3    Nygren, P.Å.4    Hober, S.5
  • 62
    • 84870857894 scopus 로고    scopus 로고
    • Tailor-made design of penicillin G acylase surface enables its site-directed immobilization and stabilization onto commercial mono-functional epoxy supports
    • Grazu V., López-Gallego F., Guisán J.M. Tailor-made design of penicillin G acylase surface enables its site-directed immobilization and stabilization onto commercial mono-functional epoxy supports. Process Biochem 2012, 47:2538-2541.
    • (2012) Process Biochem , vol.47 , pp. 2538-2541
    • Grazu, V.1    López-Gallego, F.2    Guisán, J.M.3
  • 63
    • 84897535679 scopus 로고    scopus 로고
    • Combining the 'two worlds' of chemocatalysis and biocatalysis towards multi-step one-pot processes in aqueous media
    • Gröger H., Hummel W. Combining the 'two worlds' of chemocatalysis and biocatalysis towards multi-step one-pot processes in aqueous media. Curr Opin Chem Biol 2014, 19:171-179.
    • (2014) Curr Opin Chem Biol , vol.19 , pp. 171-179
    • Gröger, H.1    Hummel, W.2
  • 64
    • 84904793107 scopus 로고    scopus 로고
    • Immobilization as a strategy for improving enzyme properties - application to oxidoreductases
    • Guzik U., Hupert-Kocurek K., Wojcieszynska D. Immobilization as a strategy for improving enzyme properties - application to oxidoreductases. Molecules 2014, 19:8995-9018.
    • (2014) Molecules , vol.19 , pp. 8995-9018
    • Guzik, U.1    Hupert-Kocurek, K.2    Wojcieszynska, D.3
  • 65
    • 84873413560 scopus 로고    scopus 로고
    • One-step immobilization and purification of His-tagged enzyme using poly(2-acetamidoacrylic acid) hydrogel
    • Ha E.J., Kim K.K., Park H.S., Lee S.G., Lee J.O., Seong Soo A.A., et al. One-step immobilization and purification of His-tagged enzyme using poly(2-acetamidoacrylic acid) hydrogel. Macromol Res 2013, 21:5-9.
    • (2013) Macromol Res , vol.21 , pp. 5-9
    • Ha, E.J.1    Kim, K.K.2    Park, H.S.3    Lee, S.G.4    Lee, J.O.5    Seong Soo, A.A.6
  • 66
    • 58349118740 scopus 로고    scopus 로고
    • Immobilization of β galactosidase from Aspergillus oryzae via immunoaffinity support
    • Haider T., Husain Q. Immobilization of β galactosidase from Aspergillus oryzae via immunoaffinity support. Biochem Eng J 2009, 43:307-314.
    • (2009) Biochem Eng J , vol.43 , pp. 307-314
    • Haider, T.1    Husain, Q.2
  • 67
    • 34447617851 scopus 로고    scopus 로고
    • Zbasic-A novel purification tag for efficient protein recovery
    • Hedhammar M., Hober S. Zbasic-A novel purification tag for efficient protein recovery. J Chromatogr A 2007, 1161:22-28.
    • (2007) J Chromatogr A , vol.1161 , pp. 22-28
    • Hedhammar, M.1    Hober, S.2
  • 68
    • 14644444571 scopus 로고    scopus 로고
    • Negatively charged purification tags for selective anion-exchange recovery
    • Hedhammar M., Gräslund T., Uhlén M., Hober S. Negatively charged purification tags for selective anion-exchange recovery. Protein Eng Des Sel 2004, 17:779-786.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 779-786
    • Hedhammar, M.1    Gräslund, T.2    Uhlén, M.3    Hober, S.4
  • 69
    • 33750601043 scopus 로고    scopus 로고
    • Single-step recovery and solid-phase refolding of inclusion body proteins using a polycationic purification tag
    • Hedhammar M., Alm T., Gräslund T., Hober S. Single-step recovery and solid-phase refolding of inclusion body proteins using a polycationic purification tag. Biotechnol J 2006, 1:187-196.
    • (2006) Biotechnol J , vol.1 , pp. 187-196
    • Hedhammar, M.1    Alm, T.2    Gräslund, T.3    Hober, S.4
  • 70
    • 78650818528 scopus 로고    scopus 로고
    • Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance
    • Hernandez K., Fernandez-Lafuente R. Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance. Enzyme Microb Technol 2011, 48:107-122.
    • (2011) Enzyme Microb Technol , vol.48 , pp. 107-122
    • Hernandez, K.1    Fernandez-Lafuente, R.2
  • 71
    • 79957560384 scopus 로고    scopus 로고
    • Simple and efficient immobilization of lipase B from Candida antarctica on porous styrene-divinylbenzene beads
    • Hernandez K., Garcia-Galan C., Fernandez-Lafuente R. Simple and efficient immobilization of lipase B from Candida antarctica on porous styrene-divinylbenzene beads. Enzyme Microb Technol 2011, 49:72-78.
    • (2011) Enzyme Microb Technol , vol.49 , pp. 72-78
    • Hernandez, K.1    Garcia-Galan, C.2    Fernandez-Lafuente, R.3
  • 72
    • 84872415717 scopus 로고    scopus 로고
    • Enzyme stabilization by nano/microsized hybrid materials
    • Hwang E.T., Gu M.B. Enzyme stabilization by nano/microsized hybrid materials. Eng Life Sci 2013, 13:49-61.
    • (2013) Eng Life Sci , vol.13 , pp. 49-61
    • Hwang, E.T.1    Gu, M.B.2
  • 73
    • 39449136523 scopus 로고    scopus 로고
    • Covalent immobilization of antibody fragments on well-defined polymer brushes via site-directed method
    • Iwata R., Satoh R., Iwasaki Y., Akiyoshi K. Covalent immobilization of antibody fragments on well-defined polymer brushes via site-directed method. Colloids Surf B Biointerfaces 2008, 62:288-298.
    • (2008) Colloids Surf B Biointerfaces , vol.62 , pp. 288-298
    • Iwata, R.1    Satoh, R.2    Iwasaki, Y.3    Akiyoshi, K.4
  • 74
    • 0034864621 scopus 로고    scopus 로고
    • Preparation of stable, highly active and immobilized glucose oxidase using the anti-enzyme antibodies and F(ab)' 2
    • Jan U., Husain Q., Saleemuddin M. Preparation of stable, highly active and immobilized glucose oxidase using the anti-enzyme antibodies and F(ab)' 2. Biotechnol Appl Biochem 2001, 34:13-17.
    • (2001) Biotechnol Appl Biochem , vol.34 , pp. 13-17
    • Jan, U.1    Husain, Q.2    Saleemuddin, M.3
  • 75
    • 33749512192 scopus 로고    scopus 로고
    • A study on the comparative stability of insoluble complexes of glucose oxidase obtained with concanavalin A and specific polyclonal antibodies
    • Jan U., Khan A.A., Husain Q. A study on the comparative stability of insoluble complexes of glucose oxidase obtained with concanavalin A and specific polyclonal antibodies. World J Microbiol Biotechnol 2006, 22:1033-1039.
    • (2006) World J Microbiol Biotechnol , vol.22 , pp. 1033-1039
    • Jan, U.1    Khan, A.A.2    Husain, Q.3
  • 76
    • 14644393725 scopus 로고    scopus 로고
    • Simultaneous purification and immobilization of mushroom tyrosinase on an immunoaffinity support
    • Khan A.A., Akhtar S., Husain Q. Simultaneous purification and immobilization of mushroom tyrosinase on an immunoaffinity support. Process Biochem 2005, 40:2379-2386.
    • (2005) Process Biochem , vol.40 , pp. 2379-2386
    • Khan, A.A.1    Akhtar, S.2    Husain, Q.3
  • 77
    • 0029636512 scopus 로고
    • Preparation of immobilized enzyme with high activity using affinity tag based on proteins A and G
    • Kondo A., Teshima T. Preparation of immobilized enzyme with high activity using affinity tag based on proteins A and G. Biotechnol Bioeng 1995, 46:421-428.
    • (1995) Biotechnol Bioeng , vol.46 , pp. 421-428
    • Kondo, A.1    Teshima, T.2
  • 78
    • 84893941074 scopus 로고    scopus 로고
    • Protein engineering of chit42 towards improvement of chitinase and antifungal activities
    • Kowsari M., Motallebi M., Zamani M. Protein engineering of chit42 towards improvement of chitinase and antifungal activities. Curr Microbiol 2014, 68:495-502.
    • (2014) Curr Microbiol , vol.68 , pp. 495-502
    • Kowsari, M.1    Motallebi, M.2    Zamani, M.3
  • 79
    • 70349615664 scopus 로고    scopus 로고
    • Direct immobilization of functional single-chain variable fragment antibodies (scFvs) onto a polystyrene plate by genetic fusion of a polystyrene-binding peptide (PS-tag)
    • Kumada Y., Hamasaki K., Shiritani Y., Nakagawa A., Kuroki D., Ohse T., et al. Direct immobilization of functional single-chain variable fragment antibodies (scFvs) onto a polystyrene plate by genetic fusion of a polystyrene-binding peptide (PS-tag). Anal Bioanal Chem 2009, 395:759-765.
    • (2009) Anal Bioanal Chem , vol.395 , pp. 759-765
    • Kumada, Y.1    Hamasaki, K.2    Shiritani, Y.3    Nakagawa, A.4    Kuroki, D.5    Ohse, T.6
  • 81
    • 13244250035 scopus 로고    scopus 로고
    • Immobilization of Bacillus macerans cyclodextrin glycosyltransferase fused with poly-lysine using cation exchanger
    • Kweon D.H., Kim S.G., Han N.S., Lee J.H., Chung K.M., Seo J.H. Immobilization of Bacillus macerans cyclodextrin glycosyltransferase fused with poly-lysine using cation exchanger. Enzyme Microb Technol 2005, 36:571-578.
    • (2005) Enzyme Microb Technol , vol.36 , pp. 571-578
    • Kweon, D.H.1    Kim, S.G.2    Han, N.S.3    Lee, J.H.4    Chung, K.M.5    Seo, J.H.6
  • 82
    • 24644468575 scopus 로고    scopus 로고
    • Selective immobilization of fusion proteins on poly(hydroxyalkanoate) microbeads
    • Lee S.J., Park J.P., Park T.J., Lee S.Y., Lee S., Park J.K. Selective immobilization of fusion proteins on poly(hydroxyalkanoate) microbeads. Anal Chem 2005, 77:5755-5759.
    • (2005) Anal Chem , vol.77 , pp. 5755-5759
    • Lee, S.J.1    Park, J.P.2    Park, T.J.3    Lee, S.Y.4    Lee, S.5    Park, J.K.6
  • 83
    • 77949404994 scopus 로고    scopus 로고
    • Nitrilotriacetic acid (NTA) resin as a reversible immobilization matrix for polyhistidine tagged enzyme in enzyme thermistor
    • Li Y.J., Wang H.Y., Xie W.H. Nitrilotriacetic acid (NTA) resin as a reversible immobilization matrix for polyhistidine tagged enzyme in enzyme thermistor. Sens Lett 2009, 7:1072-1076.
    • (2009) Sens Lett , vol.7 , pp. 1072-1076
    • Li, Y.J.1    Wang, H.Y.2    Xie, W.H.3
  • 84
    • 84867397422 scopus 로고    scopus 로고
    • Comparison of magnetic carboxymethyl chitosan nanoparticles and cation exchange resin for the efficient purification of lysine-tagged small ubiquitin-like modifier protease
    • Li J., Zhang Y., Shen F., Yang Y. Comparison of magnetic carboxymethyl chitosan nanoparticles and cation exchange resin for the efficient purification of lysine-tagged small ubiquitin-like modifier protease. J Chromatogr B Analyt Technol Biomed Life Sci 2012, 907:159-162.
    • (2012) J Chromatogr B Analyt Technol Biomed Life Sci , vol.907 , pp. 159-162
    • Li, J.1    Zhang, Y.2    Shen, F.3    Yang, Y.4
  • 85
    • 80555156061 scopus 로고    scopus 로고
    • Specifically and reversibly immobilizing proteins/enzymes to nitriolotriacetic-acid-modified mesoporous silicas through histidine tags for purification or catalysis
    • Lin Y.C., Liang M.R., Lin Y.C., Chen C.T. Specifically and reversibly immobilizing proteins/enzymes to nitriolotriacetic-acid-modified mesoporous silicas through histidine tags for purification or catalysis. Chem Eur J 2011, 17:13059-13067.
    • (2011) Chem Eur J , vol.17 , pp. 13059-13067
    • Lin, Y.C.1    Liang, M.R.2    Lin, Y.C.3    Chen, C.T.4
  • 86
    • 0343247806 scopus 로고    scopus 로고
    • The roles and function of cellulose-binding domains
    • Linder M., Teeri T.T. The roles and function of cellulose-binding domains. J Biotechnol 1997, 57:15-28.
    • (1997) J Biotechnol , vol.57 , pp. 15-28
    • Linder, M.1    Teeri, T.T.2
  • 87
    • 0032488360 scopus 로고    scopus 로고
    • Improved immobilization of fusion proteins via cellulose-binding domains
    • Linder M., Nevanen T., Soderholm L., Bengs O., Teeri T.T. Improved immobilization of fusion proteins via cellulose-binding domains. Biotechnol Bioeng 1998, 60:642-647.
    • (1998) Biotechnol Bioeng , vol.60 , pp. 642-647
    • Linder, M.1    Nevanen, T.2    Soderholm, L.3    Bengs, O.4    Teeri, T.T.5
  • 88
    • 84858732424 scopus 로고    scopus 로고
    • Directed, strong, and reversible immobilization of proteins tagged with a β-trefoil lectin domain: a simple method to immobilize biomolecules on plain agarose matrixes
    • López-Gallego F., Acebrón I., Mancheño J.M., Raja S., Lillo M.P., Guisán Seijas J.M. Directed, strong, and reversible immobilization of proteins tagged with a β-trefoil lectin domain: a simple method to immobilize biomolecules on plain agarose matrixes. Bioconjug Chem 2012, 23:565-573.
    • (2012) Bioconjug Chem , vol.23 , pp. 565-573
    • López-Gallego, F.1    Acebrón, I.2    Mancheño, J.M.3    Raja, S.4    Lillo, M.P.5    Guisán Seijas, J.M.6
  • 89
    • 84861681740 scopus 로고    scopus 로고
    • Synthesis of galactooligosaccharides by CBD fusion β-galactosidase immobilized on cellulose
    • Lu L., Xu S., Zhao R., Zhang D., Li Z., Li Y., et al. Synthesis of galactooligosaccharides by CBD fusion β-galactosidase immobilized on cellulose. Bioresour Technol 2012, 116:327-333.
    • (2012) Bioresour Technol , vol.116 , pp. 327-333
    • Lu, L.1    Xu, S.2    Zhao, R.3    Zhang, D.4    Li, Z.5    Li, Y.6
  • 90
    • 84923359729 scopus 로고    scopus 로고
    • Immobilization of lipases on hydrophobic supports involves the open form of the enzyme
    • [(2015) Enzyme and Microbial Technology
    • Manoel E.A., dos Santos J.C.S, Freire D.M.G., Rueda N., Fernandez-Lafuente R. Immobilization of lipases on hydrophobic supports involves the open form of the enzyme. Enzyme Microb Technol 2015, [(2015) Enzyme and Microbial Technology, 71, pp. 53-57]. 10.1016/j.enzmictec.2015.02.001.
    • (2015) Enzyme Microb Technol , vol.71 , pp. 53-57
    • Manoel, E.A.1    dos Santos, J.C.S.2    Freire, D.M.G.3    Rueda, N.4    Fernandez-Lafuente, R.5
  • 91
    • 0033913710 scopus 로고    scopus 로고
    • Cloning and purification of the hydrophilic fragment of hepatitis C virus E2 protein fused to the choline-binding domain of the major autolysin of Streptococcus pneumoniae: evaluation of the humoral immune response in rabbits
    • Martinez G., Vina A., Garcia J.L., Morales-Grillo J. Cloning and purification of the hydrophilic fragment of hepatitis C virus E2 protein fused to the choline-binding domain of the major autolysin of Streptococcus pneumoniae: evaluation of the humoral immune response in rabbits. Biotecnol Apl 2000, 17:85-88.
    • (2000) Biotecnol Apl , vol.17 , pp. 85-88
    • Martinez, G.1    Vina, A.2    Garcia, J.L.3    Morales-Grillo, J.4
  • 92
    • 0034575018 scopus 로고    scopus 로고
    • Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage
    • Mateo C., Fernández-Lorente G., Abian O., Fernández-Lafuente R., Guisán J.M. Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage. Biomacromolecules 2000, 1:739-745.
    • (2000) Biomacromolecules , vol.1 , pp. 739-745
    • Mateo, C.1    Fernández-Lorente, G.2    Abian, O.3    Fernández-Lafuente, R.4    Guisán, J.M.5
  • 93
    • 0035148782 scopus 로고    scopus 로고
    • One-step purification, covalent immobilization, and additional stabilization of poly-his-tagged proteins using novel heterofunctional chelate-epoxy supports
    • Mateo C., Fernández-Lorente G., Cortés E., Garcia J.L., Fernández-Lafuente R., Guisan J.M. One-step purification, covalent immobilization, and additional stabilization of poly-his-tagged proteins using novel heterofunctional chelate-epoxy supports. Biotechnol Bioeng 2001, 76:269-276.
    • (2001) Biotechnol Bioeng , vol.76 , pp. 269-276
    • Mateo, C.1    Fernández-Lorente, G.2    Cortés, E.3    Garcia, J.L.4    Fernández-Lafuente, R.5    Guisan, J.M.6
  • 94
    • 0035957867 scopus 로고    scopus 로고
    • Affinity chromatography of polyhistidine tagged enzymes - new dextran-coated immobilized metal ion affinity chromatography matrices for prevention of undesired multipoint adsorptions
    • Mateo C., Fernandez-Lorente G., Pessela B.C.C., Vian A., Carrascosa A.V., Garcia J.L., et al. Affinity chromatography of polyhistidine tagged enzymes - new dextran-coated immobilized metal ion affinity chromatography matrices for prevention of undesired multipoint adsorptions. J Chromatogr A 2001, 915:97-106.
    • (2001) J Chromatogr A , vol.915 , pp. 97-106
    • Mateo, C.1    Fernandez-Lorente, G.2    Pessela, B.C.C.3    Vian, A.4    Carrascosa, A.V.5    Garcia, J.L.6
  • 97
    • 33646500582 scopus 로고    scopus 로고
    • Glyoxyl agarose: a fully inert and hydrophilic support for immobilization and high stabilization of proteins
    • Mateo C., Palomo J.M., Fuentes M., Betancor L., Grazu V., López-Gallego F., et al. Glyoxyl agarose: a fully inert and hydrophilic support for immobilization and high stabilization of proteins. Enzyme Microb Technol 2006, 39:274-280.
    • (2006) Enzyme Microb Technol , vol.39 , pp. 274-280
    • Mateo, C.1    Palomo, J.M.2    Fuentes, M.3    Betancor, L.4    Grazu, V.5    López-Gallego, F.6
  • 99
    • 37749025783 scopus 로고    scopus 로고
    • Advances in the design of new epoxy supports for enzyme immobilization-stabilization
    • Mateo C., Grazú V., Pessela B.C.C., Montes T., Palomo J.M., Torres R., et al. Advances in the design of new epoxy supports for enzyme immobilization-stabilization. Biochem Soc Trans 2007, 35:1593-1601.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1593-1601
    • Mateo, C.1    Grazú, V.2    Pessela, B.C.C.3    Montes, T.4    Palomo, J.M.5    Torres, R.6
  • 101
    • 0021647752 scopus 로고
    • Salt-mediated retention of proteins in hydrophobic-interaction chromatography. Application of solvophobic theory
    • Melander W.R., Corradini D., Horvath C. Salt-mediated retention of proteins in hydrophobic-interaction chromatography. Application of solvophobic theory. J Chromatogr 1984, 317:67-85.
    • (1984) J Chromatogr , vol.317 , pp. 67-85
    • Melander, W.R.1    Corradini, D.2    Horvath, C.3
  • 102
    • 4143138635 scopus 로고    scopus 로고
    • Contruction of a chimeric thermostable pyrophosphatase to facilitate its purification and immobilization by using the choline-binding tag
    • Moldes C., García J.L., García P. Contruction of a chimeric thermostable pyrophosphatase to facilitate its purification and immobilization by using the choline-binding tag. Appl Environ Microbiol 2004, 70:4642-4647.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 4642-4647
    • Moldes, C.1    García, J.L.2    García, P.3
  • 103
    • 2942558481 scopus 로고    scopus 로고
    • In vivo immobilization of fusion proteins on bioplastics by the novel tag BioF
    • Moldes C., García P., García J.L., Prieto M.A. In vivo immobilization of fusion proteins on bioplastics by the novel tag BioF. Appl Environ Microbiol 2004, 70:3205-3212.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3205-3212
    • Moldes, C.1    García, P.2    García, J.L.3    Prieto, M.A.4
  • 104
    • 0032876699 scopus 로고    scopus 로고
    • Affinity chromatography of plasma proteins (guanidinobenzoatase): use of mimetic matrices and mimetic soluble ligands to prevent the binding of albumin on target affinity matrices
    • Murza A., Aguilar A.R., Fernandez-Lafuente R., Guisan J.M. Affinity chromatography of plasma proteins (guanidinobenzoatase): use of mimetic matrices and mimetic soluble ligands to prevent the binding of albumin on target affinity matrices. J Chromatogr B Biomed Sci Appl 1999, 732:165-172.
    • (1999) J Chromatogr B Biomed Sci Appl , vol.732 , pp. 165-172
    • Murza, A.1    Aguilar, A.R.2    Fernandez-Lafuente, R.3    Guisan, J.M.4
  • 105
    • 0031559948 scopus 로고    scopus 로고
    • Reversible, site-specific immobilization of polyarginine-tagged fusion proteins on mica surfaces
    • Nock S., Spudich J.A., Wagner P. Reversible, site-specific immobilization of polyarginine-tagged fusion proteins on mica surfaces. FEBS Lett 1997, 414:233-238.
    • (1997) FEBS Lett , vol.414 , pp. 233-238
    • Nock, S.1    Spudich, J.A.2    Wagner, P.3
  • 106
    • 61449164761 scopus 로고    scopus 로고
    • Molecular engineering of the cellulosome complex for affinity and bioenergy applications
    • Nordon R.E., Craig S.J., Foong F.C. Molecular engineering of the cellulosome complex for affinity and bioenergy applications. Biotechnol Lett 2009, 31:465-476.
    • (2009) Biotechnol Lett , vol.31 , pp. 465-476
    • Nordon, R.E.1    Craig, S.J.2    Foong, F.C.3
  • 108
    • 0037010728 scopus 로고    scopus 로고
    • Interfacial adsorption of lipases on very hydrophobic support (octadecyl-sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases
    • Palomo J.M., Muoz G., Fernández-Lorente G., Mateo C., Fernández-Lafuente R., Guisán J.M. Interfacial adsorption of lipases on very hydrophobic support (octadecyl-sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases. J Mol Catal B: Enzym 2002, 19-20:279-286.
    • (2002) J Mol Catal B: Enzym , pp. 279-286
    • Palomo, J.M.1    Muoz, G.2    Fernández-Lorente, G.3    Mateo, C.4    Fernández-Lafuente, R.5    Guisán, J.M.6
  • 112
    • 33847619328 scopus 로고    scopus 로고
    • Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxyl-agarose supports: correlation between enzyme-support linkages and thermal stability
    • Pedroche J., del Mar Yust M., Mateo C., Fernández-Lafuente R., Girón-Calle J., Alaiz M., et al. Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxyl-agarose supports: correlation between enzyme-support linkages and thermal stability. Enzyme Microb Technol 2007, 40:1160-1166.
    • (2007) Enzyme Microb Technol , vol.40 , pp. 1160-1166
    • Pedroche, J.1    del Mar Yust, M.2    Mateo, C.3    Fernández-Lafuente, R.4    Girón-Calle, J.5    Alaiz, M.6
  • 113
    • 0038701946 scopus 로고    scopus 로고
    • One-step purification, covalent immobilization, and additional stabilization of a thermophilic poly-his-tagged β-galactosidase from Thermus sp. strain T2 by using novel heterofunctional chelate - epoxy sepabeads
    • Pessela B.C.C., Mateo C., Carrascosa A.V., Vian A., García J.L., Rivas G., et al. One-step purification, covalent immobilization, and additional stabilization of a thermophilic poly-his-tagged β-galactosidase from Thermus sp. strain T2 by using novel heterofunctional chelate - epoxy sepabeads. Biomacromolecules 2003, 4:107-113.
    • (2003) Biomacromolecules , vol.4 , pp. 107-113
    • Pessela, B.C.C.1    Mateo, C.2    Carrascosa, A.V.3    Vian, A.4    García, J.L.5    Rivas, G.6
  • 114
    • 1642302124 scopus 로고    scopus 로고
    • Ion exchange using poorly activated supports, an easy way for purification of large proteins
    • Pessela B.C.C., Munilla R., Betancor L., Fuentes M., Carrascosa A.V., Vian A., et al. Ion exchange using poorly activated supports, an easy way for purification of large proteins. J Chromatogr A 2004, 1034:155-159.
    • (2004) J Chromatogr A , vol.1034 , pp. 155-159
    • Pessela, B.C.C.1    Munilla, R.2    Betancor, L.3    Fuentes, M.4    Carrascosa, A.V.5    Vian, A.6
  • 115
    • 7044234722 scopus 로고    scopus 로고
    • Selective and mild adsorption of large proteins on lowly activated immobilized metal ion affinity chromatography matrices: purification of multimeric thermophilic enzymes overexpressed in Escherichia coli
    • Pessela B.C.C., Torres R., Fuentes M., Mateo C., Munilla R., Vian A., et al. Selective and mild adsorption of large proteins on lowly activated immobilized metal ion affinity chromatography matrices: purification of multimeric thermophilic enzymes overexpressed in Escherichia coli. J Chromatogr A 2004, 1055:93-98.
    • (2004) J Chromatogr A , vol.1055 , pp. 93-98
    • Pessela, B.C.C.1    Torres, R.2    Fuentes, M.3    Mateo, C.4    Munilla, R.5    Vian, A.6
  • 116
    • 33745184478 scopus 로고    scopus 로고
    • Purification and very strong reversible immobilization of large proteins on anionic exchangers by controlling the support and the immobilization conditions
    • Pessela B.C.C., Fuentes M., Mateo C., Munilla R., Carrascosa A.V., Fernandez-Lafuente R., et al. Purification and very strong reversible immobilization of large proteins on anionic exchangers by controlling the support and the immobilization conditions. Enzyme Microb Technol 2006, 39:909-915.
    • (2006) Enzyme Microb Technol , vol.39 , pp. 909-915
    • Pessela, B.C.C.1    Fuentes, M.2    Mateo, C.3    Munilla, R.4    Carrascosa, A.V.5    Fernandez-Lafuente, R.6
  • 118
    • 33751164160 scopus 로고    scopus 로고
    • Selective adsorption of large proteins on highly activated IMAC supports in the presence of high imidazole concentrations: purification, reversible immobilization and stabilization of thermophilic α- and β-galactosidases
    • Pessela B.C.C., Mateo C., Filho M., Carrascosa A., Fernández-Lafuente R., Guisan J.M. Selective adsorption of large proteins on highly activated IMAC supports in the presence of high imidazole concentrations: purification, reversible immobilization and stabilization of thermophilic α- and β-galactosidases. Enzyme Microb Technol 2007, 40:242-248.
    • (2007) Enzyme Microb Technol , vol.40 , pp. 242-248
    • Pessela, B.C.C.1    Mateo, C.2    Filho, M.3    Carrascosa, A.4    Fernández-Lafuente, R.5    Guisan, J.M.6
  • 119
    • 0029933809 scopus 로고    scopus 로고
    • Theoretical investigation of the dynamics of the active site lid in Rhizomucor miehei lipase
    • Peters G.H., Olsen O.H., Svendsen A., Wade R.C. Theoretical investigation of the dynamics of the active site lid in Rhizomucor miehei lipase. Biophys J 1996, 71:119-129.
    • (1996) Biophys J , vol.71 , pp. 119-129
    • Peters, G.H.1    Olsen, O.H.2    Svendsen, A.3    Wade, R.C.4
  • 120
    • 84859778992 scopus 로고    scopus 로고
    • Influence of different immobilization techniques for Candida cylindracea lipase on its stability and fish oil hydrolysis
    • Pizarro C., Brañes M.C., Markovits A., Fernández-Lorente G., Guisán J.M., Chamy R., et al. Influence of different immobilization techniques for Candida cylindracea lipase on its stability and fish oil hydrolysis. J Mol Catal B: Enzym 2012, 78:111-118.
    • (2012) J Mol Catal B: Enzym , vol.78 , pp. 111-118
    • Pizarro, C.1    Brañes, M.C.2    Markovits, A.3    Fernández-Lorente, G.4    Guisán, J.M.5    Chamy, R.6
  • 121
    • 0031444343 scopus 로고    scopus 로고
    • Factors controlling ion-exchange selectivity in suppressed ion chromatography
    • Pohl C.A., Stillian J.R., Jackson P.E. Factors controlling ion-exchange selectivity in suppressed ion chromatography. J Chromatogr A 1997, 789:29-41.
    • (1997) J Chromatogr A , vol.789 , pp. 29-41
    • Pohl, C.A.1    Stillian, J.R.2    Jackson, P.E.3
  • 122
    • 0026910385 scopus 로고
    • Immobilized metal ion affinity chromatography
    • Porath J. Immobilized metal ion affinity chromatography. Protein Expr Purif 1992, 3:263-281.
    • (1992) Protein Expr Purif , vol.3 , pp. 263-281
    • Porath, J.1
  • 123
    • 0021114727 scopus 로고
    • Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions
    • Porath J., Olin B. Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions. Biochemistry 1983, 22:1621-1630.
    • (1983) Biochemistry , vol.22 , pp. 1621-1630
    • Porath, J.1    Olin, B.2
  • 124
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • Porath J., Carlsson J., Olsson I., Belfrage G. Metal chelate affinity chromatography, a new approach to protein fractionation. Nature 1975, 258:598-599.
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 125
    • 84883272014 scopus 로고    scopus 로고
    • Biocatalysis in organic chemistry and biotechnology: past, present, and future
    • Reetz M.T. Biocatalysis in organic chemistry and biotechnology: past, present, and future. J Am Chem Soc 2013, 135:12480-12496.
    • (2013) J Am Chem Soc , vol.135 , pp. 12480-12496
    • Reetz, M.T.1
  • 126
    • 0034692619 scopus 로고    scopus 로고
    • Expression, immobilization, and enzymatic characterization of cellulose-binding domain-organophosphorus hydrolase fusion enzymes
    • Richins R.D., Mulchandani A., Chen W. Expression, immobilization, and enzymatic characterization of cellulose-binding domain-organophosphorus hydrolase fusion enzymes. Biotechnol Bioeng 2000, 69:591-596.
    • (2000) Biotechnol Bioeng , vol.69 , pp. 591-596
    • Richins, R.D.1    Mulchandani, A.2    Chen, W.3
  • 128
    • 84906872022 scopus 로고    scopus 로고
    • Amination of enzymes to improve biocatalyst performance: coupling genetic modification and physicochemical tools
    • Rodrigues R.C., Barbosa O., Ortiz C., Berenguer-Murcia Á., Torres R., Fernandez-Lafuente R. Amination of enzymes to improve biocatalyst performance: coupling genetic modification and physicochemical tools. RSC Adv 2014, 4:38350-38374.
    • (2014) RSC Adv , vol.4 , pp. 38350-38374
    • Rodrigues, R.C.1    Barbosa, O.2    Ortiz, C.3    Berenguer-Murcia, Á.4    Torres, R.5    Fernandez-Lafuente, R.6
  • 130
    • 0032506270 scopus 로고    scopus 로고
    • 'Interfacial affinity chromatography' of lipases: separation of different fractions by selective adsorption on supports activated with hydrophobic groups
    • Sabuquillo P., Reina J., Fernandez-Lorente G., Guisan J.M., Fernandez-Lafuente R. 'Interfacial affinity chromatography' of lipases: separation of different fractions by selective adsorption on supports activated with hydrophobic groups. Biochim Biophys Acta Protein Struct Mol Enzymol 1998, 1388:337-348.
    • (1998) Biochim Biophys Acta Protein Struct Mol Enzymol , vol.1388 , pp. 337-348
    • Sabuquillo, P.1    Reina, J.2    Fernandez-Lorente, G.3    Guisan, J.M.4    Fernandez-Lafuente, R.5
  • 131
    • 0032611445 scopus 로고    scopus 로고
    • Bioaffinity based immobilization of enzymes
    • Saleemuddin M. Bioaffinity based immobilization of enzymes. Adv Biochem Eng Biotechnol 1999, 64:203-226.
    • (1999) Adv Biochem Eng Biotechnol , vol.64 , pp. 203-226
    • Saleemuddin, M.1
  • 132
    • 0021320171 scopus 로고
    • A polypeptide fusion designed for the purification of recombinant proteins
    • Sassenfeld H.M., Brewer S.J. A polypeptide fusion designed for the purification of recombinant proteins. Biotechnology (N Y) 1984, 2:76-81.
    • (1984) Biotechnology (N Y) , vol.2 , pp. 76-81
    • Sassenfeld, H.M.1    Brewer, S.J.2
  • 133
    • 29144501578 scopus 로고    scopus 로고
    • Improvement of catalytic properties of Escherichia coli penicillin G acylase immobilized on glyoxyl agarose by addition of a six-amino-acid tag
    • Scaramozzino F., Estruch I., Rossolillo P., Terreni M., Albertini A.M. Improvement of catalytic properties of Escherichia coli penicillin G acylase immobilized on glyoxyl agarose by addition of a six-amino-acid tag. Appl Environ Microbiol 2005, 71:8937-8940.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8937-8940
    • Scaramozzino, F.1    Estruch, I.2    Rossolillo, P.3    Terreni, M.4    Albertini, A.M.5
  • 134
    • 29244474901 scopus 로고    scopus 로고
    • Site-directed antibody immobilization on gold substrate for surface plasmon resonance sensors
    • Schmid A.H., Stanca S.E., Thakur M.S., Thampi K.R., Suri C.R. Site-directed antibody immobilization on gold substrate for surface plasmon resonance sensors. Sens Actuators B 2006, 113:297-303.
    • (2006) Sens Actuators B , vol.113 , pp. 297-303
    • Schmid, A.H.1    Stanca, S.E.2    Thakur, M.S.3    Thampi, K.R.4    Suri, C.R.5
  • 135
    • 0037436563 scopus 로고    scopus 로고
    • Dispelling the myths - biocatalysis in industrial synthesis
    • Schoemaker H.E., Mink D., WubboLts M.G. Dispelling the myths - biocatalysis in industrial synthesis. Science 2003, 299:1694-1697.
    • (2003) Science , vol.299 , pp. 1694-1697
    • Schoemaker, H.E.1    Mink, D.2    WubboLts, M.G.3
  • 136
    • 84884267795 scopus 로고    scopus 로고
    • The role of biocatalysis in the asymmetric synthesis of alkaloids
    • Schrittwieser J.H., Resch V. The role of biocatalysis in the asymmetric synthesis of alkaloids. RSC Adv 2013, 3:17602-17632.
    • (2013) RSC Adv , vol.3 , pp. 17602-17632
    • Schrittwieser, J.H.1    Resch, V.2
  • 137
    • 2942720843 scopus 로고    scopus 로고
    • Different properties of the lipases contained in porcine pancreatic lipase extracts as enantioselective biocatalysts
    • Segura R.L., Palomo J.M., Mateo C., Cortes A., Terreni M., Fernández-Lafuente R., et al. Different properties of the lipases contained in porcine pancreatic lipase extracts as enantioselective biocatalysts. Biotechnol Prog 2004, 20:825-829.
    • (2004) Biotechnol Prog , vol.20 , pp. 825-829
    • Segura, R.L.1    Palomo, J.M.2    Mateo, C.3    Cortes, A.4    Terreni, M.5    Fernández-Lafuente, R.6
  • 138
    • 33745194615 scopus 로고    scopus 로고
    • Purification and identification of different lipases contained in PPL commercial extracts: a minor contaminant is the main responsible of most esterasic activity
    • Segura R.L., Betancor L., Palomo J.M., Hidalgo A., Fernández-Lorente G., Terreni M., et al. Purification and identification of different lipases contained in PPL commercial extracts: a minor contaminant is the main responsible of most esterasic activity. Enzyme Microb Technol 2006, 39:817-823.
    • (2006) Enzyme Microb Technol , vol.39 , pp. 817-823
    • Segura, R.L.1    Betancor, L.2    Palomo, J.M.3    Hidalgo, A.4    Fernández-Lorente, G.5    Terreni, M.6
  • 140
    • 63449102770 scopus 로고    scopus 로고
    • Coupling of site-directed mutagenesis and immobilization for the rational design of more efficient biocatalysts: the case of immobilized 3G3K PGA from E. coli.
    • Serra I., Ceechini D.A., UbiaIi D., Manazza E.M., Albertini A.M., Terreni M. Coupling of site-directed mutagenesis and immobilization for the rational design of more efficient biocatalysts: the case of immobilized 3G3K PGA from E. coli. J Org Chem 2009, 1384-1389.
    • (2009) J Org Chem , pp. 1384-1389
    • Serra, I.1    Ceechini, D.A.2    UbiaIi, D.3    Manazza, E.M.4    Albertini, A.M.5    Terreni, M.6
  • 141
    • 84873732314 scopus 로고    scopus 로고
    • Assessment of immobilized PGA orientation via the LC-MS analysis of tryptic digests of the wild type and its 3K-PGA mutant assists in the rational design of a high-performance biocatalyst
    • Serra I., Ubiali D., Cecchini D.A., Calleri E., Albertini A.M., Terreni M., et al. Assessment of immobilized PGA orientation via the LC-MS analysis of tryptic digests of the wild type and its 3K-PGA mutant assists in the rational design of a high-performance biocatalyst. Anal Bioanal Chem 2013, 405:745-753.
    • (2013) Anal Bioanal Chem , vol.405 , pp. 745-753
    • Serra, I.1    Ubiali, D.2    Cecchini, D.A.3    Calleri, E.4    Albertini, A.M.5    Terreni, M.6
  • 142
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilization: the quest for optimum performance
    • Sheldon R.A. Enzyme immobilization: the quest for optimum performance. Adv Synth Catal 2007, 349:1289-1307.
    • (2007) Adv Synth Catal , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 144
    • 0036148091 scopus 로고    scopus 로고
    • Immobilisation of enzymes on poly(aniline)-poly(anion) composite films. Preparation of bioanodes for biofuel cell applications
    • Simon E., Halliwell C.M., Toh C.S., Cass A.E.G., Bartlett P.N. Immobilisation of enzymes on poly(aniline)-poly(anion) composite films. Preparation of bioanodes for biofuel cell applications. Bioelectrochemistry 2002, 55:13-15.
    • (2002) Bioelectrochemistry , vol.55 , pp. 13-15
    • Simon, E.1    Halliwell, C.M.2    Toh, C.S.3    Cass, A.E.G.4    Bartlett, P.N.5
  • 145
    • 0023958874 scopus 로고
    • Influence of salts on the covalent immobilization of proteins to modified copolymers of 2-hydroxyethyl methacrylate with ethylene dimethacrylate
    • Smalla K., Turkova J., Coupek J., Hermann P. Influence of salts on the covalent immobilization of proteins to modified copolymers of 2-hydroxyethyl methacrylate with ethylene dimethacrylate. Biotechnol Appl Biochem 1988, 10:21-31.
    • (1988) Biotechnol Appl Biochem , vol.10 , pp. 21-31
    • Smalla, K.1    Turkova, J.2    Coupek, J.3    Hermann, P.4
  • 146
    • 0026019938 scopus 로고
    • Highly active enzyme preparations immobilized via matrix-conjugated anti-Fc antibodies
    • Solomon B., Hadas E., Koppel R., Schwartz F., Fleminger G. Highly active enzyme preparations immobilized via matrix-conjugated anti-Fc antibodies. J Chromatogr 1991, 539:335-341.
    • (1991) J Chromatogr , vol.539 , pp. 335-341
    • Solomon, B.1    Hadas, E.2    Koppel, R.3    Schwartz, F.4    Fleminger, G.5
  • 148
    • 84897688146 scopus 로고    scopus 로고
    • Biocatalysis combined with physical technologies for development of a green biodiesel process
    • Teixeira C.B., Madeira Junior J.V., Macedo G.A. Biocatalysis combined with physical technologies for development of a green biodiesel process. Renew Sust Energ Rev 2014, 33:333-343.
    • (2014) Renew Sust Energ Rev , vol.33 , pp. 333-343
    • Teixeira, C.B.1    Madeira Junior, J.V.2    Macedo, G.A.3
  • 149
    • 77954585606 scopus 로고    scopus 로고
    • Characterization and study of the orientation of immobilized enzymes by tryptic digestion and HPLC-MS: design of an efficient catalyst for the synthesis of cephalosporins
    • Temporini C., Bonomi P., Serra I., Tagliani A., Bavaro T., Ubiali D., et al. Characterization and study of the orientation of immobilized enzymes by tryptic digestion and HPLC-MS: design of an efficient catalyst for the synthesis of cephalosporins. Biomacromolecules 2010, 11:1623-1632.
    • (2010) Biomacromolecules , vol.11 , pp. 1623-1632
    • Temporini, C.1    Bonomi, P.2    Serra, I.3    Tagliani, A.4    Bavaro, T.5    Ubiali, D.6
  • 150
    • 22944457568 scopus 로고    scopus 로고
    • Design of a specific peptide tag that affords covalent and site-specific enzyme immobilization catalyzed by microbial transglutaminase
    • Tominaga J., Kamiya N., Doi S., Ichinose H., Maruyama T., Goto M. Design of a specific peptide tag that affords covalent and site-specific enzyme immobilization catalyzed by microbial transglutaminase. Biomacromolecules 2005, 6:2299-2304.
    • (2005) Biomacromolecules , vol.6 , pp. 2299-2304
    • Tominaga, J.1    Kamiya, N.2    Doi, S.3    Ichinose, H.4    Maruyama, T.5    Goto, M.6
  • 152
    • 0028039930 scopus 로고
    • Crystallization and preliminary X-ray studies of lipase B from Candida antarctica
    • Uppenberg J., Patkar S., Bergfors T., Jones T.A. Crystallization and preliminary X-ray studies of lipase B from Candida antarctica. J Mol Biol 1994, 235:790-792.
    • (1994) J Mol Biol , vol.235 , pp. 790-792
    • Uppenberg, J.1    Patkar, S.2    Bergfors, T.3    Jones, T.A.4
  • 153
    • 0027200087 scopus 로고
    • Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography
    • Van Tilbeurgh H., Egloff M.P., Martinez C., Rugani N., Verger R., Cambillau C. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature 1993, 362:814-820.
    • (1993) Nature , vol.362 , pp. 814-820
    • Van Tilbeurgh, H.1    Egloff, M.P.2    Martinez, C.3    Rugani, N.4    Verger, R.5    Cambillau, C.6
  • 154
    • 0034814777 scopus 로고    scopus 로고
    • Immobilization of SpA::Eco RI on IgG support improves the thermal stability of restriction activity
    • Varshney H., Saleemuddin M., Rhee J.I., Schugerl K. Immobilization of SpA::Eco RI on IgG support improves the thermal stability of restriction activity. Process Biochem 2001, 37:275-278.
    • (2001) Process Biochem , vol.37 , pp. 275-278
    • Varshney, H.1    Saleemuddin, M.2    Rhee, J.I.3    Schugerl, K.4
  • 155
    • 0031023666 scopus 로고    scopus 로고
    • 'Interfacial activation' of lipases: facts and artifacts
    • Verger R. 'Interfacial activation' of lipases: facts and artifacts. Trends Biotechnol 1997, 15:32-38.
    • (1997) Trends Biotechnol , vol.15 , pp. 32-38
    • Verger, R.1
  • 156
    • 0028874414 scopus 로고
    • Site-directed and random enzyme immobilization on functionalized membranes: kinetic studies and models
    • Vishwanath S., Bhattacharyya D., Huang W., Bachas L.G. Site-directed and random enzyme immobilization on functionalized membranes: kinetic studies and models. J Membr Sci 1995, 108:1-13.
    • (1995) J Membr Sci , vol.108 , pp. 1-13
    • Vishwanath, S.1    Bhattacharyya, D.2    Huang, W.3    Bachas, L.G.4
  • 157
    • 0031105299 scopus 로고    scopus 로고
    • Kinetic studies of site-specifically and randomly immobilized alkaline phosphatase on functionalized membranes
    • Vishwanath S.K., Watson C.R., Huang W., Bachas L.G., Bhattacharyya D. Kinetic studies of site-specifically and randomly immobilized alkaline phosphatase on functionalized membranes. J Chem Technol Biotechnol 1997, 68:294-302.
    • (1997) J Chem Technol Biotechnol , vol.68 , pp. 294-302
    • Vishwanath, S.K.1    Watson, C.R.2    Huang, W.3    Bachas, L.G.4    Bhattacharyya, D.5
  • 158
    • 72949106533 scopus 로고    scopus 로고
    • Single-step purification of different lipases from Staphylococcus warneri
    • Volpato G., Filice M., Ayub M.A.Z., Guisan J.M., Palomo J.M. Single-step purification of different lipases from Staphylococcus warneri. J Chromatogr A 2010, 1217:473-478.
    • (2010) J Chromatogr A , vol.1217 , pp. 473-478
    • Volpato, G.1    Filice, M.2    Ayub, M.A.Z.3    Guisan, J.M.4    Palomo, J.M.5
  • 159
    • 79958259731 scopus 로고    scopus 로고
    • Purification, immobilization, and characterization of a specific lipase from Staphylococcus warneri EX17 by enzyme fractionating via adsorption on different hydrophobic supports
    • Volpato G., Filice M., de las Rivas B., Rodrigues R.C., Heck J.X., Fernandez-Lafuente R., et al. Purification, immobilization, and characterization of a specific lipase from Staphylococcus warneri EX17 by enzyme fractionating via adsorption on different hydrophobic supports. Biotechnol Prog 2011, 27:717-723.
    • (2011) Biotechnol Prog , vol.27 , pp. 717-723
    • Volpato, G.1    Filice, M.2    de las Rivas, B.3    Rodrigues, R.C.4    Heck, J.X.5    Fernandez-Lafuente, R.6
  • 160
    • 0031106782 scopus 로고    scopus 로고
    • Specific immobilization of firefly luciferase through a biotin carboxyl carrier protein domain
    • Wang C.Y., Hitz S., Andrade J.D., Stewart R.J. Specific immobilization of firefly luciferase through a biotin carboxyl carrier protein domain. Anal Biochem 1997, 246:133-139.
    • (1997) Anal Biochem , vol.246 , pp. 133-139
    • Wang, C.Y.1    Hitz, S.2    Andrade, J.D.3    Stewart, R.J.4
  • 161
    • 0034935569 scopus 로고    scopus 로고
    • Improving the activity of immobilized subtilisin by site-directed attachment through a genetically engineered affinity tag
    • Wang J., Bhattacharyya D., Bachas L.G. Improving the activity of immobilized subtilisin by site-directed attachment through a genetically engineered affinity tag. Fresenius J Anal Chem 2001, 369:280-285.
    • (2001) Fresenius J Anal Chem , vol.369 , pp. 280-285
    • Wang, J.1    Bhattacharyya, D.2    Bachas, L.G.3
  • 162
    • 0034819923 scopus 로고    scopus 로고
    • Orientation specific immobilization of organophosphorus hydrolase on magnetic particles through gene fusion
    • Wang J., Bhattacharyya D., Bachas L.G. Orientation specific immobilization of organophosphorus hydrolase on magnetic particles through gene fusion. Biomacromolecules 2001, 2:700-705.
    • (2001) Biomacromolecules , vol.2 , pp. 700-705
    • Wang, J.1    Bhattacharyya, D.2    Bachas, L.G.3
  • 163
    • 77957328836 scopus 로고    scopus 로고
    • Specific and reversible immobilization of NADH oxidase on functionalized carbon nanotubes
    • Wang L., Wei L., Chen Y., Jiang R. Specific and reversible immobilization of NADH oxidase on functionalized carbon nanotubes. J Biotechnol 2010, 150:57-63.
    • (2010) J Biotechnol , vol.150 , pp. 57-63
    • Wang, L.1    Wei, L.2    Chen, Y.3    Jiang, R.4
  • 164
    • 84874791965 scopus 로고    scopus 로고
    • Convenient one-step purification and immobilization of lipase using a genetically encoded aldehyde tag
    • Wang A., Du F., Wang F., Shen Y., Gao W., Zhang P. Convenient one-step purification and immobilization of lipase using a genetically encoded aldehyde tag. Biochem Eng J 2013, 73:86-92.
    • (2013) Biochem Eng J , vol.73 , pp. 86-92
    • Wang, A.1    Du, F.2    Wang, F.3    Shen, Y.4    Gao, W.5    Zhang, P.6
  • 165
    • 84875715205 scopus 로고    scopus 로고
    • Characterization of a novel thermostable chitin-binding domain and its application in immobilization of a multifunctional hemicellulase
    • Wang Q., Xue Y., Wu X. Characterization of a novel thermostable chitin-binding domain and its application in immobilization of a multifunctional hemicellulase. J Agric Food Chem 2013, 61:3074-3081.
    • (2013) J Agric Food Chem , vol.61 , pp. 3074-3081
    • Wang, Q.1    Xue, Y.2    Wu, X.3
  • 166
    • 84898640018 scopus 로고    scopus 로고
    • Biocatalysis as a strategic green technology for the chemical industry
    • Wells A., Meyer H.P. Biocatalysis as a strategic green technology for the chemical industry. ChemCatChem 2014, 6:918-920.
    • (2014) ChemCatChem , vol.6 , pp. 918-920
    • Wells, A.1    Meyer, H.P.2
  • 167
    • 0027326779 scopus 로고
    • Salt-induced immobilization of proteins on a high-performance liquid chromatographic epoxide affinity support
    • Wheatley J.B., Schmidt D.E. Salt-induced immobilization of proteins on a high-performance liquid chromatographic epoxide affinity support. J Chromatogr 1993, 644:11-16.
    • (1993) J Chromatogr , vol.644 , pp. 11-16
    • Wheatley, J.B.1    Schmidt, D.E.2
  • 168
    • 0033042026 scopus 로고    scopus 로고
    • Salt-induced immobilization of affinity ligands onto epoxide-activated supports
    • Wheatley J.B., Schmidt D.E. Salt-induced immobilization of affinity ligands onto epoxide-activated supports. J Chromatogr A 1999, 849:1-12.
    • (1999) J Chromatogr A , vol.849 , pp. 1-12
    • Wheatley, J.B.1    Schmidt, D.E.2
  • 169
    • 80051810009 scopus 로고    scopus 로고
    • Oriented immobilization of enzymes made fit for applied biocatalysis: non-covalent attachment to anionic supports using Zbasic2 module
    • Wiesbauer J., Bolivar J.M., Mueller M., Schiller M., Nidetzky B. Oriented immobilization of enzymes made fit for applied biocatalysis: non-covalent attachment to anionic supports using Zbasic2 module. ChemCatChem 2011, 3:1299-1303.
    • (2011) ChemCatChem , vol.3 , pp. 1299-1303
    • Wiesbauer, J.1    Bolivar, J.M.2    Mueller, M.3    Schiller, M.4    Nidetzky, B.5
  • 171
    • 0027598435 scopus 로고
    • Enzyme-linked immunosorbent assay for an octapeptide based on a genetically engineered fusion protein
    • Witkowski A., Daunert S., Kindy M.S., Bachas L.G. Enzyme-linked immunosorbent assay for an octapeptide based on a genetically engineered fusion protein. Anal Chem 1993, 65:1147-1151.
    • (1993) Anal Chem , vol.65 , pp. 1147-1151
    • Witkowski, A.1    Daunert, S.2    Kindy, M.S.3    Bachas, L.G.4
  • 172
    • 84878825678 scopus 로고    scopus 로고
    • Characterization of the diatomite binding domain in the ribosomal protein L2 from E. coli and functions as an affinity tag
    • Yang Y., Li J., Zhang Y. Characterization of the diatomite binding domain in the ribosomal protein L2 from E. coli and functions as an affinity tag. Appl Microbiol Biotechnol 2013, 97:2541-2549.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 2541-2549
    • Yang, Y.1    Li, J.2    Zhang, Y.3
  • 173
    • 0035832858 scopus 로고    scopus 로고
    • Stabilization of pancreatic ribonuclease A by immobilization on Sepharose-linked antibodies that recognize the labile region of the enzyme
    • Younus H., Owais M., Rao D.N., Saleemuddin M. Stabilization of pancreatic ribonuclease A by immobilization on Sepharose-linked antibodies that recognize the labile region of the enzyme. Biochim Biophys Acta Protein Struct Mol Enzymol 2001, 1548:114-120.
    • (2001) Biochim Biophys Acta Protein Struct Mol Enzymol , vol.1548 , pp. 114-120
    • Younus, H.1    Owais, M.2    Rao, D.N.3    Saleemuddin, M.4
  • 174
    • 0036847226 scopus 로고    scopus 로고
    • Selective stabilization of a labile mutant form of bovine pancreatic ribonuclease A by antibodies
    • Younus H., Köditz J., Saleemuddin M., Ulbrich-Hofmann R. Selective stabilization of a labile mutant form of bovine pancreatic ribonuclease A by antibodies. Biotechnol Lett 2002, 24:1821-1826.
    • (2002) Biotechnol Lett , vol.24 , pp. 1821-1826
    • Younus, H.1    Köditz, J.2    Saleemuddin, M.3    Ulbrich-Hofmann, R.4
  • 175
    • 4043175540 scopus 로고    scopus 로고
    • Behaviour of a recombinant cabbage (Brassica oleracea) phospholipase D immobilized on CNBr-activated and antibody supports
    • Younus H., Rajcani J., Ulbrich-Hofmann R., Saleemuddin M. Behaviour of a recombinant cabbage (Brassica oleracea) phospholipase D immobilized on CNBr-activated and antibody supports. Biotechnol Appl Biochem 2004, 40:95-99.
    • (2004) Biotechnol Appl Biochem , vol.40 , pp. 95-99
    • Younus, H.1    Rajcani, J.2    Ulbrich-Hofmann, R.3    Saleemuddin, M.4
  • 176
    • 0033230992 scopus 로고    scopus 로고
    • Membrane chromatography: preparation and applications to protein separation
    • Zeng X., Ruckenstein E. Membrane chromatography: preparation and applications to protein separation. Biotechnol Prog 1999, 15:1003-1019.
    • (1999) Biotechnol Prog , vol.15 , pp. 1003-1019
    • Zeng, X.1    Ruckenstein, E.2
  • 177
    • 84887348704 scopus 로고    scopus 로고
    • Enzymatic properties of Thermoanaerobacterium thermosaccharolyticum β-glucosidase fused to Clostridium cellulovorans cellulose binding domain and its application in hydrolysis of microcrystalline cellulose
    • Zhao L., Pang Q., Xie J., Pei J., Wang F., Fan S. Enzymatic properties of Thermoanaerobacterium thermosaccharolyticum β-glucosidase fused to Clostridium cellulovorans cellulose binding domain and its application in hydrolysis of microcrystalline cellulose. BMC Biotechnol 2013, 13.
    • (2013) BMC Biotechnol , vol.13
    • Zhao, L.1    Pang, Q.2    Xie, J.3    Pei, J.4    Wang, F.5    Fan, S.6
  • 178
    • 84907095838 scopus 로고    scopus 로고
    • Inorganic materials as supports for covalent enzyme immobilization: methods and mechanisms
    • Zucca P., Sanjust E. Inorganic materials as supports for covalent enzyme immobilization: methods and mechanisms. Molecules 2014, 19:14139-14194.
    • (2014) Molecules , vol.19 , pp. 14139-14194
    • Zucca, P.1    Sanjust, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.