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Volumn 135, Issue 2, 2008, Pages 181-189

Probing the microenvironment of sol-gel entrapped cutinase: The role of added zeolite NaY

Author keywords

Cutinase; EDS; Fluorescence; Immobilization; Optical microscopy; SEM; Sol gel; Tryptophan; Zeolite

Indexed keywords

AMINO ACIDS; CHAIN LENGTH; FLUORESCENCE; OPTICAL MICROSCOPY; SCANNING ELECTRON MICROSCOPY; SILANES; SOL-GEL PROCESS; ZEOLITES;

EID: 44149084162     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2008.03.018     Document Type: Article
Times cited : (11)

References (46)
  • 1
    • 33751158445 scopus 로고
    • Enzymes and other proteins entrapped in sol-gel materials
    • Avnir D., Braun S., Lev O., and Ottolenghi M. Enzymes and other proteins entrapped in sol-gel materials. Chem. Mater. 6 (1994) 1605-1614
    • (1994) Chem. Mater. , vol.6 , pp. 1605-1614
    • Avnir, D.1    Braun, S.2    Lev, O.3    Ottolenghi, M.4
  • 2
    • 33644860341 scopus 로고    scopus 로고
    • Recent bio-applications of sol-gel materials
    • Avnir D., Coradin T., Lev O., and Livage J. Recent bio-applications of sol-gel materials. J. Mater. Chem. 16 (2006) 1013-1030
    • (2006) J. Mater. Chem. , vol.16 , pp. 1013-1030
    • Avnir, D.1    Coradin, T.2    Lev, O.3    Livage, J.4
  • 5
    • 33644909860 scopus 로고    scopus 로고
    • Turning biopolymer particles into hybrid capsules: the example of silica/alginate nanocomposites
    • Boissière M., Meadows P.J., Brayner R., Hélary C., Livage J., and Coradin T. Turning biopolymer particles into hybrid capsules: the example of silica/alginate nanocomposites. J. Mater. Chem. 16 (2006) 1178-1182
    • (2006) J. Mater. Chem. , vol.16 , pp. 1178-1182
    • Boissière, M.1    Meadows, P.J.2    Brayner, R.3    Hélary, C.4    Livage, J.5    Coradin, T.6
  • 7
    • 4043114820 scopus 로고    scopus 로고
    • Biocers: ceramics with incorporated microorganisms for biocatalytic, biosorptive and functional materials development
    • Böttcher H., Soltmann U., Mertig M., and Pompe W. Biocers: ceramics with incorporated microorganisms for biocatalytic, biosorptive and functional materials development. J. Mater. Chem. 14 (2004) 2176-2188
    • (2004) J. Mater. Chem. , vol.14 , pp. 2176-2188
    • Böttcher, H.1    Soltmann, U.2    Mertig, M.3    Pompe, W.4
  • 8
    • 0037432086 scopus 로고    scopus 로고
    • Using sugar and amino acid additives to stabilize enzymes within sol-gel derived silica
    • Brennan J.D., Benjamin D., DiBattista E., and Gulcev M.D. Using sugar and amino acid additives to stabilize enzymes within sol-gel derived silica. Chem. Mater. 15 (2003) 737-745
    • (2003) Chem. Mater. , vol.15 , pp. 737-745
    • Brennan, J.D.1    Benjamin, D.2    DiBattista, E.3    Gulcev, M.D.4
  • 9
    • 0035543887 scopus 로고    scopus 로고
    • Direct product sequestration of a recombinant cutinase from batch fermentations of Saccharomyces cerevisiae
    • Calado C.R.C., Hamilton G.E., Cabral J.M.S., Fonseca L.P., and Lyddiatt A. Direct product sequestration of a recombinant cutinase from batch fermentations of Saccharomyces cerevisiae. Bioseparation 10 (2001) 87-97
    • (2001) Bioseparation , vol.10 , pp. 87-97
    • Calado, C.R.C.1    Hamilton, G.E.2    Cabral, J.M.S.3    Fonseca, L.P.4    Lyddiatt, A.5
  • 10
    • 4043069168 scopus 로고    scopus 로고
    • Encapsulation of functional cells by sol-gel silica: actual progress and perspectives for cell therapy
    • Carturan G., Dal Toso R., Boninsegna S., and Dal Monte R. Encapsulation of functional cells by sol-gel silica: actual progress and perspectives for cell therapy. J. Mater. Sci. 14 (2004) 2087-2098
    • (2004) J. Mater. Sci. , vol.14 , pp. 2087-2098
    • Carturan, G.1    Dal Toso, R.2    Boninsegna, S.3    Dal Monte, R.4
  • 12
    • 0037115376 scopus 로고    scopus 로고
    • Multianalyte pin-printed biosensor arrays based on protein-doped xerogels
    • Cho E.J., Tao Z., Tehan E.C., and Bright F.V. Multianalyte pin-printed biosensor arrays based on protein-doped xerogels. Anal. Chem. 74 (2002) 6177-6184
    • (2002) Anal. Chem. , vol.74 , pp. 6177-6184
    • Cho, E.J.1    Tao, Z.2    Tehan, E.C.3    Bright, F.V.4
  • 13
    • 17844375933 scopus 로고    scopus 로고
    • Synthesis, characterization and diffusion properties of biomimetic silica-coated gelatine beads
    • Coradin T., and Livage J. Synthesis, characterization and diffusion properties of biomimetic silica-coated gelatine beads. Mater. Sci. Eng. C 25 (2005) 201-205
    • (2005) Mater. Sci. Eng. C , vol.25 , pp. 201-205
    • Coradin, T.1    Livage, J.2
  • 14
    • 0035092041 scopus 로고    scopus 로고
    • Molecular confinement influences protein structure and enhances thermal protein stability
    • Eggers D.K., and Valentine J.S. Molecular confinement influences protein structure and enhances thermal protein stability. Protein Sci. 10 (2001) 250-261
    • (2001) Protein Sci. , vol.10 , pp. 250-261
    • Eggers, D.K.1    Valentine, J.S.2
  • 15
    • 0035824871 scopus 로고    scopus 로고
    • Crowding and hydration effects on protein conformation: a study with sol-gel encapsulated proteins
    • Eggers D.K., and Valentine J.S. Crowding and hydration effects on protein conformation: a study with sol-gel encapsulated proteins. J. Mol. Biol. 314 (2001) 911-922
    • (2001) J. Mol. Biol. , vol.314 , pp. 911-922
    • Eggers, D.K.1    Valentine, J.S.2
  • 16
    • 33644554471 scopus 로고    scopus 로고
    • In vitro apatite forming ability of type I collagen hydrogels containing bioactive glass and silica sol-gel particles
    • Eglin D., Maalheem S., Livage J., and Coradin T. In vitro apatite forming ability of type I collagen hydrogels containing bioactive glass and silica sol-gel particles. J. Mater. Sci.: Mater. Med. 17 (2006) 161-167
    • (2006) J. Mater. Sci.: Mater. Med. , vol.17 , pp. 161-167
    • Eglin, D.1    Maalheem, S.2    Livage, J.3    Coradin, T.4
  • 17
    • 3543131812 scopus 로고    scopus 로고
    • New packing materials for bioreactors based on coated and fiber-reinforced biocers
    • Fiedler D., Thron A., Soltmann U., and Böttcher H. New packing materials for bioreactors based on coated and fiber-reinforced biocers. Chem. Mater. 16 (2004) 3040-3044
    • (2004) Chem. Mater. , vol.16 , pp. 3040-3044
    • Fiedler, D.1    Thron, A.2    Soltmann, U.3    Böttcher, H.4
  • 18
    • 20444381371 scopus 로고    scopus 로고
    • Sol-gel materials as efficient enzyme protectors: preserving the activity of phosphatases under extreme pH conditions
    • Frenkel-Mullerad H., and Avnir D. Sol-gel materials as efficient enzyme protectors: preserving the activity of phosphatases under extreme pH conditions. J. Am. Chem. Soc. 127 (2005) 8077-8081
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8077-8081
    • Frenkel-Mullerad, H.1    Avnir, D.2
  • 20
    • 0034773128 scopus 로고    scopus 로고
    • Bio-doped nanocomposite polymers: sol-gel bioencapsulates
    • Gill I. Bio-doped nanocomposite polymers: sol-gel bioencapsulates. Chem. Mater. 13 (2001) 3404-3421
    • (2001) Chem. Mater. , vol.13 , pp. 3404-3421
    • Gill, I.1
  • 23
    • 17644440298 scopus 로고    scopus 로고
    • Interaction of an anionic surfactant with a recombinant cutinase from Fusarium solani pisi: a spectroscopic study
    • Gonçalves A.M.D., Aires-Barros M.R., and Cabral J.M.S. Interaction of an anionic surfactant with a recombinant cutinase from Fusarium solani pisi: a spectroscopic study. Enzyme Microb. Technol. 32 (2003) 868-879
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 868-879
    • Gonçalves, A.M.D.1    Aires-Barros, M.R.2    Cabral, J.M.S.3
  • 24
    • 0017437920 scopus 로고
    • Humidity fixed points of binary saturated aqueous solutions
    • Greenspan L. Humidity fixed points of binary saturated aqueous solutions. Res. Nat. Bur. Stand. A: Phys. Chem. 81A (1977) 89-96
    • (1977) Res. Nat. Bur. Stand. A: Phys. Chem. , vol.81 A , pp. 89-96
    • Greenspan, L.1
  • 25
    • 15444373422 scopus 로고    scopus 로고
    • Monolithic bioreactor immobilizing trypsin for high-throughput analysis
    • Kato M., Inuzuka K., Sakai-Kato K., and Toyo'oka T. Monolithic bioreactor immobilizing trypsin for high-throughput analysis. Anal. Chem. 77 (2005) 1813-1818
    • (2005) Anal. Chem. , vol.77 , pp. 1813-1818
    • Kato, M.1    Inuzuka, K.2    Sakai-Kato, K.3    Toyo'oka, T.4
  • 27
    • 0030038712 scopus 로고    scopus 로고
    • Denaturation of a re-combinant cutinase from Fusarium solani pisi in AOT-iso-octane reverse micelles
    • Melo E.P., Costa S.M.B., and Cabral J.M.S. Denaturation of a re-combinant cutinase from Fusarium solani pisi in AOT-iso-octane reverse micelles. Photochem. Photobiol. 63 (1996) 169-175
    • (1996) Photochem. Photobiol. , vol.63 , pp. 169-175
    • Melo, E.P.1    Costa, S.M.B.2    Cabral, J.M.S.3
  • 30
    • 0028939393 scopus 로고
    • Interfacial activation-based molecular bioimprinting of lipolytic enzymes
    • Mingarro I., Abad C., and Braco L. Interfacial activation-based molecular bioimprinting of lipolytic enzymes. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 3308-3312
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 3308-3312
    • Mingarro, I.1    Abad, C.2    Braco, L.3
  • 33
    • 0032817737 scopus 로고    scopus 로고
    • Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase
    • Prompers J.J., Hilbers C.W., and Pepermans H.A.M. Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase. FEBS Lett. 456 (1996) 409-416
    • (1996) FEBS Lett. , vol.456 , pp. 409-416
    • Prompers, J.J.1    Hilbers, C.W.2    Pepermans, H.A.M.3
  • 34
    • 0029134278 scopus 로고
    • Efficient heterogeneous biocatalysts by entrapment of lipases in hydrophobic sol-gel materials
    • Reetz M.T., Zonta A., and Simpelkamp J. Efficient heterogeneous biocatalysts by entrapment of lipases in hydrophobic sol-gel materials. Angew. Chem. Int. Ed. 34 (1995) 301-303
    • (1995) Angew. Chem. Int. Ed. , vol.34 , pp. 301-303
    • Reetz, M.T.1    Zonta, A.2    Simpelkamp, J.3
  • 35
    • 0030569931 scopus 로고    scopus 로고
    • Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials
    • Reetz M.T., Zonta A., and Simplekamp J. Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials. Biotechnol. Bioeng. 49 (1996) 527-534
    • (1996) Biotechnol. Bioeng. , vol.49 , pp. 527-534
    • Reetz, M.T.1    Zonta, A.2    Simplekamp, J.3
  • 36
    • 0041687879 scopus 로고    scopus 로고
    • Second generation sol-gel encapsulated lipases: robust heterogeneous biocatalysts
    • Reetz M.T., Tielmann P., Wisenhöfer W., Könen W., and Zonta A. Second generation sol-gel encapsulated lipases: robust heterogeneous biocatalysts. Adv. Synth. Catal. 345 (2003) 717-728
    • (2003) Adv. Synth. Catal. , vol.345 , pp. 717-728
    • Reetz, M.T.1    Tielmann, P.2    Wisenhöfer, W.3    Könen, W.4    Zonta, A.5
  • 38
    • 0036888747 scopus 로고    scopus 로고
    • Novel approach to fabricate porous gelatin-siloxane hybrids for bone tissue engineering
    • Ren L., Tsuru K., Hayakawa S., and Osake A. Novel approach to fabricate porous gelatin-siloxane hybrids for bone tissue engineering. Biomaterials 23 (2002) 4765-4773
    • (2002) Biomaterials , vol.23 , pp. 4765-4773
    • Ren, L.1    Tsuru, K.2    Hayakawa, S.3    Osake, A.4
  • 39
    • 14844297001 scopus 로고    scopus 로고
    • Development of mammalian cell-enclosing subsieve-size agarose capsules (<100 μm) for cell therapy
    • Sakai S., Kawabata K., Ono T., Ijima H., and Kawakami K. Development of mammalian cell-enclosing subsieve-size agarose capsules (<100 μm) for cell therapy. Biomaterials 26 (2005) 4786-4792
    • (2005) Biomaterials , vol.26 , pp. 4786-4792
    • Sakai, S.1    Kawabata, K.2    Ono, T.3    Ijima, H.4    Kawakami, K.5
  • 42
    • 34247489528 scopus 로고
    • Absorption and fluorescence properties of fluorescein
    • Sjöback R., Nygren J., and Kubista M. Absorption and fluorescence properties of fluorescein. Spectrochim. Acta A 51 (1995) L7-L21
    • (1995) Spectrochim. Acta A , vol.51
    • Sjöback, R.1    Nygren, J.2    Kubista, M.3
  • 43
    • 14744295719 scopus 로고    scopus 로고
    • Unfolding and inactivation of cutinases by AOT and guanidine hydrochloride
    • Ternström T., Svendsen A., Akke M., and Adlercreutz P. Unfolding and inactivation of cutinases by AOT and guanidine hydrochloride. Biochim. Biophys. Acta 1748 (2005) 74-83
    • (2005) Biochim. Biophys. Acta , vol.1748 , pp. 74-83
    • Ternström, T.1    Svendsen, A.2    Akke, M.3    Adlercreutz, P.4
  • 45
    • 0030026581 scopus 로고    scopus 로고
    • Photophysics of the single tryptophan residue in Fusarium solani Cutinase: evidence for the occurrence of conformational substates with unusual fluorescence behaviour
    • Weisenborn P.C.M., Meder H., Egmond M.R., Visser T.J.W.G., and van Hoek A. Photophysics of the single tryptophan residue in Fusarium solani Cutinase: evidence for the occurrence of conformational substates with unusual fluorescence behaviour. Biophys. Chem. 58 (1996) 281-288
    • (1996) Biophys. Chem. , vol.58 , pp. 281-288
    • Weisenborn, P.C.M.1    Meder, H.2    Egmond, M.R.3    Visser, T.J.W.G.4    van Hoek, A.5
  • 46
    • 2542445323 scopus 로고    scopus 로고
    • An optical glucose biosensor based on entrapped-glucose oxidase in silicate xerogel hybridised with hydroxyethyl carboxymethyl cellulose
    • Wu X.J., and Choi M.M.F. An optical glucose biosensor based on entrapped-glucose oxidase in silicate xerogel hybridised with hydroxyethyl carboxymethyl cellulose. Anal. Chim. Acta 514 (2004) 219-226
    • (2004) Anal. Chim. Acta , vol.514 , pp. 219-226
    • Wu, X.J.1    Choi, M.M.F.2


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