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Volumn 44, Issue 1, 2009, Pages 62-69

Immobilization of Candida antarctica Lipase B on fumed silica

Author keywords

Adsorption; CALB; Enzyme immobilization; Enzyme stability; Fumed silica; Hexane

Indexed keywords

ADSORPTION; CATALYST ACTIVITY; CATALYSTS; ELECTROCHEMICAL SENSORS; ENZYME ACTIVITY; ENZYMES; ESTERS; FLUORESCENCE MICROSCOPY; HEXANE; ISOMERS; ORGANIC COMPOUNDS; ORGANIC SOLVENTS; OXIDES; PROTEINS; SILICA; SOLVENTS;

EID: 58049221149     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2008.09.011     Document Type: Article
Times cited : (32)

References (55)
  • 1
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov A.M. Improving enzymes by using them in organic solvents. Nature 409 (2001) 241-246
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 2
    • 27844563238 scopus 로고    scopus 로고
    • Biocatalysis in semi-aqueous and nearly anhydrous conditions
    • Hudson E.P., Eppler R.K., and Clark D.S. Biocatalysis in semi-aqueous and nearly anhydrous conditions. Curr Opin Biotechnol 16 (2005) 637-643
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 637-643
    • Hudson, E.P.1    Eppler, R.K.2    Clark, D.S.3
  • 3
    • 0035385138 scopus 로고    scopus 로고
    • Polymer synthesis by in vitro enzyme catalysis
    • Gross R.A., Kumar A., and Kalra B. Polymer synthesis by in vitro enzyme catalysis. Chem Rev 101 (2001) 2097-2124
    • (2001) Chem Rev , vol.101 , pp. 2097-2124
    • Gross, R.A.1    Kumar, A.2    Kalra, B.3
  • 4
    • 0037008507 scopus 로고    scopus 로고
    • Biodegradable polymers for the environment
    • Gross R.A., and Kalra B. Biodegradable polymers for the environment. Science 297 (2002) 803-807
    • (2002) Science , vol.297 , pp. 803-807
    • Gross, R.A.1    Kalra, B.2
  • 5
    • 0036327255 scopus 로고    scopus 로고
    • Biocatalysis applied to the preparation of pharmaceuticals
    • Gotor V. Biocatalysis applied to the preparation of pharmaceuticals. Org Process Res Dev 6 (2002) 420-426
    • (2002) Org Process Res Dev , vol.6 , pp. 420-426
    • Gotor, V.1
  • 6
    • 33645638804 scopus 로고    scopus 로고
    • Effect of water activity on the lipase catalyzed esterification of geraniol in ionic liquid [bmim]PF6
    • Barahona D., Pfromm P.H., and Rezac M.E. Effect of water activity on the lipase catalyzed esterification of geraniol in ionic liquid [bmim]PF6. Biotechnol Bioeng 93 (2006) 318-324
    • (2006) Biotechnol Bioeng , vol.93 , pp. 318-324
    • Barahona, D.1    Pfromm, P.H.2    Rezac, M.E.3
  • 7
    • 0035924140 scopus 로고    scopus 로고
    • Lipase-catalyzed synthesis of geranyl acetate in n-hexane with membrane-mediated water removal
    • Bartling K., Thompson J.U.S., Pfromm P.H., Czermak P., and Rezac M.E. Lipase-catalyzed synthesis of geranyl acetate in n-hexane with membrane-mediated water removal. Biotechnol Bioeng 75 (2001) 676-681
    • (2001) Biotechnol Bioeng , vol.75 , pp. 676-681
    • Bartling, K.1    Thompson, J.U.S.2    Pfromm, P.H.3    Czermak, P.4    Rezac, M.E.5
  • 9
    • 0041152088 scopus 로고    scopus 로고
    • Properties and synthetic applications of enzymes in organic solvents
    • Carrea G., and Riva S. Properties and synthetic applications of enzymes in organic solvents. Angewandte Chemie-Int Ed 39 (2000) 2226-2254
    • (2000) Angewandte Chemie-Int Ed , vol.39 , pp. 2226-2254
    • Carrea, G.1    Riva, S.2
  • 10
    • 0042757703 scopus 로고    scopus 로고
    • The utility of cyclodextrins in lipase-catalyzed transesterification in organic solvents: enhanced reaction rate and enantioselectivity
    • Ghanem A. The utility of cyclodextrins in lipase-catalyzed transesterification in organic solvents: enhanced reaction rate and enantioselectivity. Org Biomol Chem 1 (2003) 1282-1291
    • (2003) Org Biomol Chem , vol.1 , pp. 1282-1291
    • Ghanem, A.1
  • 11
    • 0031104802 scopus 로고    scopus 로고
    • Why are enzymes less active in organic solvents than in water?
    • Klibanov A.M. Why are enzymes less active in organic solvents than in water?. Trends Biotechnol 15 (1997) 97-101
    • (1997) Trends Biotechnol , vol.15 , pp. 97-101
    • Klibanov, A.M.1
  • 12
    • 0036905653 scopus 로고    scopus 로고
    • Factors governing the activity of lyophilised and immobilised lipase preparations in organic solvents
    • Persson M., Wehtje E., and Adlercreutz P. Factors governing the activity of lyophilised and immobilised lipase preparations in organic solvents. Chembiochem 3 (2002) 566-571
    • (2002) Chembiochem , vol.3 , pp. 566-571
    • Persson, M.1    Wehtje, E.2    Adlercreutz, P.3
  • 13
    • 34249930390 scopus 로고    scopus 로고
    • Combinatorial discovery of reusable noncovalent supports for enzyme immobilization and nonaqueous catalysis
    • Long J., Hutcheon G.A., and Cooper A.I. Combinatorial discovery of reusable noncovalent supports for enzyme immobilization and nonaqueous catalysis. J Comb Chem 9 (2007) 399-406
    • (2007) J Comb Chem , vol.9 , pp. 399-406
    • Long, J.1    Hutcheon, G.A.2    Cooper, A.I.3
  • 14
    • 28244452921 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates (CLEAs): a novel and versatile method for enzyme immobilization (a review)
    • Sheldon R.A., Schoevaart R., and Van Langen L.M. Cross-linked enzyme aggregates (CLEAs): a novel and versatile method for enzyme immobilization (a review). Biocatal Biotransform 23 (2005) 141-147
    • (2005) Biocatal Biotransform , vol.23 , pp. 141-147
    • Sheldon, R.A.1    Schoevaart, R.2    Van Langen, L.M.3
  • 15
    • 0037495218 scopus 로고    scopus 로고
    • Enhanced enzyme activity and enantioselectivity of lipases in organic solvents by crown ethers and cyclodextrins
    • Mine Y., Fukunaga K., Itoh K., Yoshimoto M., Nakao K., and Sugimura Y. Enhanced enzyme activity and enantioselectivity of lipases in organic solvents by crown ethers and cyclodextrins. J Biosci Bioeng 95 (2003) 441-447
    • (2003) J Biosci Bioeng , vol.95 , pp. 441-447
    • Mine, Y.1    Fukunaga, K.2    Itoh, K.3    Yoshimoto, M.4    Nakao, K.5    Sugimura, Y.6
  • 16
    • 34247487327 scopus 로고    scopus 로고
    • Can an inactivating agent increase enzyme activity in organic solvent? Effects of 18-crown-6 on lipase activity, enantioselectivity, and conformation
    • Secundo F., Barletta G.L., Dumitriu E., and Carrea G. Can an inactivating agent increase enzyme activity in organic solvent? Effects of 18-crown-6 on lipase activity, enantioselectivity, and conformation. Biotechnol Bioeng 97 (2007) 12-18
    • (2007) Biotechnol Bioeng , vol.97 , pp. 12-18
    • Secundo, F.1    Barletta, G.L.2    Dumitriu, E.3    Carrea, G.4
  • 17
    • 0035921170 scopus 로고    scopus 로고
    • Effect of crown ethers on structure, stability, activity, and enantioselectivity of subtilisin Carlsberg in organic solvents
    • Santos A.M., Vidal M., Pacheco Y., Frontera J., Baez C., Ornellas O., et al. Effect of crown ethers on structure, stability, activity, and enantioselectivity of subtilisin Carlsberg in organic solvents. Biotechnol Bioeng 74 (2001) 295-308
    • (2001) Biotechnol Bioeng , vol.74 , pp. 295-308
    • Santos, A.M.1    Vidal, M.2    Pacheco, Y.3    Frontera, J.4    Baez, C.5    Ornellas, O.6
  • 18
    • 0037008370 scopus 로고    scopus 로고
    • Penicillin amidase is activated for use in nonaqueous media by lyophilizing in the presence of potassium chloride
    • Lindsay J.P., Clark D.S., and Dordick J.S. Penicillin amidase is activated for use in nonaqueous media by lyophilizing in the presence of potassium chloride. Enzyme Microb Technol 31 (2002) 193-197
    • (2002) Enzyme Microb Technol , vol.31 , pp. 193-197
    • Lindsay, J.P.1    Clark, D.S.2    Dordick, J.S.3
  • 19
    • 1442277709 scopus 로고    scopus 로고
    • Combinatorial formulation of biocatalyst preparations for increased activity in organic solvents: salt activation of penicillin amidase
    • Lindsay J.P., Clark D.S., and Dordick J.S. Combinatorial formulation of biocatalyst preparations for increased activity in organic solvents: salt activation of penicillin amidase. Biotechnol Bioeng 85 (2004) 553-560
    • (2004) Biotechnol Bioeng , vol.85 , pp. 553-560
    • Lindsay, J.P.1    Clark, D.S.2    Dordick, J.S.3
  • 20
    • 0034058387 scopus 로고    scopus 로고
    • On the salt-induced activation of lyophilized enzymes in organic solvents: effect of salt kosmotropicity on enzyme activity
    • Ru M.T., Hirokane S.Y., Lo A.S., Dordick J.S., Reimer J.A., and Clark D.S. On the salt-induced activation of lyophilized enzymes in organic solvents: effect of salt kosmotropicity on enzyme activity. J Am Chem Soc 122 (2000) 1565-1571
    • (2000) J Am Chem Soc , vol.122 , pp. 1565-1571
    • Ru, M.T.1    Hirokane, S.Y.2    Lo, A.S.3    Dordick, J.S.4    Reimer, J.A.5    Clark, D.S.6
  • 21
    • 0035922876 scopus 로고    scopus 로고
    • Towards more active biocatalysts in organic media: Increasing the activity of salt-activated enzymes
    • Ru M.T., Wu K.C., Lindsay J.P., Dordick J.S., Reimer J.A., and Clark D.S. Towards more active biocatalysts in organic media: Increasing the activity of salt-activated enzymes. Biotechnol Bioeng 75 (2001) 187-196
    • (2001) Biotechnol Bioeng , vol.75 , pp. 187-196
    • Ru, M.T.1    Wu, K.C.2    Lindsay, J.P.3    Dordick, J.S.4    Reimer, J.A.5    Clark, D.S.6
  • 22
    • 20144380447 scopus 로고    scopus 로고
    • Activation of subtilisin Carlsberg in hexane by lyophilization in the presence of fumed silica
    • Wurges K., Pfromm P.H., Rezac M.E., and Czermak P. Activation of subtilisin Carlsberg in hexane by lyophilization in the presence of fumed silica. J Mol Catal B-Enzym 34 (2005) 18-24
    • (2005) J Mol Catal B-Enzym , vol.34 , pp. 18-24
    • Wurges, K.1    Pfromm, P.H.2    Rezac, M.E.3    Czermak, P.4
  • 23
    • 33846302825 scopus 로고    scopus 로고
    • Fumed silica activated subtilisin Carlsberg in hexane in a packed-bed reactor
    • Pfromm P.H., Rezac M.E., Wurges K., and Czermak P. Fumed silica activated subtilisin Carlsberg in hexane in a packed-bed reactor. Aiche J 53 (2007) 237-242
    • (2007) Aiche J , vol.53 , pp. 237-242
    • Pfromm, P.H.1    Rezac, M.E.2    Wurges, K.3    Czermak, P.4
  • 28
    • 0037022510 scopus 로고    scopus 로고
    • Impact of some organics on structural and adsorptive characteristics of fumed silica in different media
    • Gun'ko V.M., Zarko V.I., Voronin E.F., Turov V.V., Mironyuk I.F., Gerashchenko I.I., et al. Impact of some organics on structural and adsorptive characteristics of fumed silica in different media. Langmuir 18 (2002) 581-596
    • (2002) Langmuir , vol.18 , pp. 581-596
    • Gun'ko, V.M.1    Zarko, V.I.2    Voronin, E.F.3    Turov, V.V.4    Mironyuk, I.F.5    Gerashchenko, I.I.6
  • 32
    • 0037383063 scopus 로고    scopus 로고
    • Study of interaction of proteins with fumed silica in aqueous suspensions by adsorption and photon correlation spectroscopy methods
    • Gun'ko V.M., Mikhailova I.V., Zarko V.I., Gerashchenko I.I., Guzenko N.V., Janusz W., et al. Study of interaction of proteins with fumed silica in aqueous suspensions by adsorption and photon correlation spectroscopy methods. J Colloid Interface Sci 260 (2003) 56-69
    • (2003) J Colloid Interface Sci , vol.260 , pp. 56-69
    • Gun'ko, V.M.1    Mikhailova, I.V.2    Zarko, V.I.3    Gerashchenko, I.I.4    Guzenko, N.V.5    Janusz, W.6
  • 33
    • 34547747311 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes-stability, activity and implementation strategies for high temperature applications
    • Unsworth L.D., van der Oost J., and Koutsopoulos S. Hyperthermophilic enzymes-stability, activity and implementation strategies for high temperature applications. FEBS J 274 (2007) 4044-4056
    • (2007) FEBS J , vol.274 , pp. 4044-4056
    • Unsworth, L.D.1    van der Oost, J.2    Koutsopoulos, S.3
  • 35
    • 10044251257 scopus 로고    scopus 로고
    • Adsorption of a therapeutic enzyme to self-assembled monolayers: effect of surface chemistry and solution pH on the amount and activity of adsorbed enzyme
    • Barrias C.C., Martins C.L., Miranda C.S., and Barbosa M.A. Adsorption of a therapeutic enzyme to self-assembled monolayers: effect of surface chemistry and solution pH on the amount and activity of adsorbed enzyme. Biomaterials 26 (2005) 2695-2704
    • (2005) Biomaterials , vol.26 , pp. 2695-2704
    • Barrias, C.C.1    Martins, C.L.2    Miranda, C.S.3    Barbosa, M.A.4
  • 36
    • 33846209146 scopus 로고    scopus 로고
    • Trends in lipase-catalyzed asymmetric access to enantiomerically pure/enriched compounds
    • Ghanem A. Trends in lipase-catalyzed asymmetric access to enantiomerically pure/enriched compounds. Tetrahedron 63 (2007) 1721-1754
    • (2007) Tetrahedron , vol.63 , pp. 1721-1754
    • Ghanem, A.1
  • 37
    • 0031795317 scopus 로고    scopus 로고
    • One biocatalyst-many applications: the use of Candida antarctica B-lipase in organic synthesis
    • Anderson E.M., Karin M., and Kirk O. One biocatalyst-many applications: the use of Candida antarctica B-lipase in organic synthesis. Biocatal Biotransform 16 (1998) 181-204
    • (1998) Biocatal Biotransform , vol.16 , pp. 181-204
    • Anderson, E.M.1    Karin, M.2    Kirk, O.3
  • 38
    • 0032479388 scopus 로고    scopus 로고
    • Lipases: interfacial enzymes with attractive applications
    • Schmid R.D., and Verger R. Lipases: interfacial enzymes with attractive applications. Angewandte Chemie-Int Ed 37 (1998) 1609-1633
    • (1998) Angewandte Chemie-Int Ed , vol.37 , pp. 1609-1633
    • Schmid, R.D.1    Verger, R.2
  • 39
    • 34249884531 scopus 로고    scopus 로고
    • Effects of porous polystyrene resin parameters on Candida antarctica Lipase B adsorption, distribution, and polyester synthesis activity
    • Chen B., Miller M.E., and Gross R.A. Effects of porous polystyrene resin parameters on Candida antarctica Lipase B adsorption, distribution, and polyester synthesis activity. Langmuir 23 (2007) 6467-6474
    • (2007) Langmuir , vol.23 , pp. 6467-6474
    • Chen, B.1    Miller, M.E.2    Gross, R.A.3
  • 40
    • 33847205076 scopus 로고    scopus 로고
    • Effects of macroporous resin size on Candida antarctica Lipase B adsorption, fraction of active molecules, and catalytic activity for polyester synthesis
    • Chen B., Miller E.M., Miller L., Maikner J.J., and Gross R.A. Effects of macroporous resin size on Candida antarctica Lipase B adsorption, fraction of active molecules, and catalytic activity for polyester synthesis. Langmuir 23 (2007) 1381-1387
    • (2007) Langmuir , vol.23 , pp. 1381-1387
    • Chen, B.1    Miller, E.M.2    Miller, L.3    Maikner, J.J.4    Gross, R.A.5
  • 41
    • 39749162076 scopus 로고    scopus 로고
    • Candida antarctica lipase B chemically immobilized on epoxy-activated micro- and nanobeads: catalysts for polyester synthesis
    • Chen B., Hu J., Miller E.M., Xie W.C., Cai M.M., and Gross R.A. Candida antarctica lipase B chemically immobilized on epoxy-activated micro- and nanobeads: catalysts for polyester synthesis. Biomacromolecules 9 (2008) 463-471
    • (2008) Biomacromolecules , vol.9 , pp. 463-471
    • Chen, B.1    Hu, J.2    Miller, E.M.3    Xie, W.C.4    Cai, M.M.5    Gross, R.A.6
  • 42
    • 24044461723 scopus 로고    scopus 로고
    • Real time measurement and control of thermodynamic water activities for enzymatic catalysis in hexane
    • Kang I.J., Pfromm P.H., and Rezac M.E. Real time measurement and control of thermodynamic water activities for enzymatic catalysis in hexane. J Biotechnol 119 (2005) 147-154
    • (2005) J Biotechnol , vol.119 , pp. 147-154
    • Kang, I.J.1    Pfromm, P.H.2    Rezac, M.E.3
  • 43
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford M.M. Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 44
    • 4344584774 scopus 로고    scopus 로고
    • Lipases and their industrial applications-an overview
    • Houde A., Kademi A., and Leblanc D. Lipases and their industrial applications-an overview. Appl Biochem Biotechnol 118 (2004) 155-170
    • (2004) Appl Biochem Biotechnol , vol.118 , pp. 155-170
    • Houde, A.1    Kademi, A.2    Leblanc, D.3
  • 45
    • 0036327837 scopus 로고    scopus 로고
    • Lipases from Candida antarctica: unique biocatalysts from a unique origin
    • Kirk O., and Christensen M.W. Lipases from Candida antarctica: unique biocatalysts from a unique origin. Org Process Res Dev 6 (2002) 446-451
    • (2002) Org Process Res Dev , vol.6 , pp. 446-451
    • Kirk, O.1    Christensen, M.W.2
  • 46
    • 21644432752 scopus 로고    scopus 로고
    • Reaction equilibrium for lipase-catalyzed condensation in organic solvent systems
    • Kobayashi T., and Adachi S. Reaction equilibrium for lipase-catalyzed condensation in organic solvent systems. Biotechnol Lett 26 (2004) 1461-1468
    • (2004) Biotechnol Lett , vol.26 , pp. 1461-1468
    • Kobayashi, T.1    Adachi, S.2
  • 47
    • 4644286940 scopus 로고    scopus 로고
    • Engineering lipase B from Candida antarctica
    • Lutz S. Engineering lipase B from Candida antarctica. Tetrahedron: Asymmetry 15 (2004) 2743-2748
    • (2004) Tetrahedron: Asymmetry , vol.15 , pp. 2743-2748
    • Lutz, S.1
  • 48
    • 0037071917 scopus 로고    scopus 로고
    • Enzymatic acylation of di- and trisaccharides with fatty acids: choosing the appropriate enzyme, support and solvent
    • Plou F.J., Cruces M.A., Ferrer M., Fuentes G., Pastor E., Bernabe M., et al. Enzymatic acylation of di- and trisaccharides with fatty acids: choosing the appropriate enzyme, support and solvent. J Biotechnol 96 (2002) 55-66
    • (2002) J Biotechnol , vol.96 , pp. 55-66
    • Plou, F.J.1    Cruces, M.A.2    Ferrer, M.3    Fuentes, G.4    Pastor, E.5    Bernabe, M.6
  • 51
    • 34547490006 scopus 로고    scopus 로고
    • Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering
    • Sate D., Janssen M.H.A., Stephens G., Sheldon R.A., Seddon K.R., and Lu J.R. Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering. Green Chem 9 (2007) 859-867
    • (2007) Green Chem , vol.9 , pp. 859-867
    • Sate, D.1    Janssen, M.H.A.2    Stephens, G.3    Sheldon, R.A.4    Seddon, K.R.5    Lu, J.R.6
  • 52
    • 11244308955 scopus 로고    scopus 로고
    • Structural features of a hyperthermostable endo-beta-1,3-glucanase in solution and adsorbed on "invisible" particles
    • Koutsopoulos S., van der Oost J., and Norde W. Structural features of a hyperthermostable endo-beta-1,3-glucanase in solution and adsorbed on "invisible" particles. Biophys J 88 (2005) 467-474
    • (2005) Biophys J , vol.88 , pp. 467-474
    • Koutsopoulos, S.1    van der Oost, J.2    Norde, W.3
  • 55
    • 27644492050 scopus 로고    scopus 로고
    • On the activity loss of hydrolases in organic solvents - I. Rapid loss of activity of a variety of enzymes and formulations in a range of organic solvents
    • Castillo B., Pacheco Y., Al-Azzam W., Griebenow K., Devi M., Ferrer A., et al. On the activity loss of hydrolases in organic solvents - I. Rapid loss of activity of a variety of enzymes and formulations in a range of organic solvents. J Mol Catal B-Enzym 35 (2005) 147-153
    • (2005) J Mol Catal B-Enzym , vol.35 , pp. 147-153
    • Castillo, B.1    Pacheco, Y.2    Al-Azzam, W.3    Griebenow, K.4    Devi, M.5    Ferrer, A.6


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