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Volumn 20, Issue 1, 2004, Pages 156-161

Invertase-Lipid Biocomposite Films: Preparation, Characterization, and Enzymatic Activity

Author keywords

[No Author keywords available]

Indexed keywords

BIOFILMS; DIFFUSION; ENZYMES; FATTY ACIDS; LIPIDS; PH EFFECTS;

EID: 1142305971     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp034236t     Document Type: Article
Times cited : (24)

References (47)
  • 1
    • 0032508960 scopus 로고    scopus 로고
    • Displasmenylcholine folite liposomes: An efficient vehicle for intracellular drug delivery
    • Rui, Y.; Wang, S.; Low, P. S.; Thompson, D. H. Displasmenylcholine folite liposomes: An efficient vehicle for intracellular drug delivery. J. Am. Chem. Soc. 1998, 120, 11213-11218.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11213-11218
    • Rui, Y.1    Wang, S.2    Low, P.S.3    Thompson, D.H.4
  • 2
    • 0032013354 scopus 로고    scopus 로고
    • Liposomes mediated enhancement of the sensitivity in immunoassays of proteins and peptides in surface plasmon resonance spectrometry
    • Wink, T.; van Zuilen, S. J.; Bult, A.; van Bennekom, W. P. Liposomes mediated enhancement of the sensitivity in immunoassays of proteins and peptides in surface plasmon resonance spectrometry. Anal. Chem. 1998, 70, 827-832.
    • (1998) Anal. Chem. , vol.70 , pp. 827-832
    • Wink, T.1    Van Zuilen, S.J.2    Bult, A.3    Van Bennekom, W.P.4
  • 3
    • 0035162637 scopus 로고    scopus 로고
    • An approach for analysis of proteins toxins on thin films of lipid mixture in an optical biosensor
    • Puu, G. An approach for analysis of proteins toxins on thin films of lipid mixture in an optical biosensor. Anal. Chem. 2001, 73, 72-79.
    • (2001) Anal. Chem. , vol.73 , pp. 72-79
    • Puu, G.1
  • 4
    • 0033030004 scopus 로고    scopus 로고
    • Molecular theory of lipid-protein interactions and the La-HII transition
    • (a) May, S.; Ben-Shaul, A. A Molecular theory of lipid-protein interactions and the La-HII transition. Biophys. J. 1999, 76, 751-761.
    • (1999) Biophys. J. , vol.76 , pp. 751-761
    • May, S.1    Ben-Shaul, A.A.2
  • 5
    • 0021474573 scopus 로고
    • Mattress model of lipid-protein interactions in membrane
    • (b) Mouritsen, O. G.; Bloom, M. Mattress model of lipid-protein interactions in membrane. Biophys. J. 1984, 46, 141-153.
    • (1984) Biophys. J. , vol.46 , pp. 141-153
    • Mouritsen, O.G.1    Bloom, M.2
  • 6
    • 0002156239 scopus 로고    scopus 로고
    • Immobilized enzymes: Methods and applications
    • and references therein
    • Tischer, W.; Wedekind, F. Immobilized enzymes: methods and applications. Top. Curr. Chem. 1999, 200, 95-126 and references therein.
    • (1999) Top. Curr. Chem. , vol.200 , pp. 95-126
    • Tischer, W.1    Wedekind, F.2
  • 10
    • 0028042488 scopus 로고
    • Enhanced N-demethylase activity of cytochrome c bound to a phosphate-bearing synthetic bilayer membrane
    • (a) Hamachi, I.; Fujita, A.; Kunitake, T. Enhanced N-demethylase activity of cytochrome c bound to a phosphate-bearing synthetic bilayer membrane. J. Am. Chem. Soc. 1994, 116, 8811-8812.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8811-8812
    • Hamachi, I.1    Fujita, A.2    Kunitake, T.3
  • 11
    • 0032646986 scopus 로고    scopus 로고
    • Ordered electrochemically active films of hemoglobin, didodecyldimethylammonium ions and clay
    • (b) Chen, X.; Hu, N.; Zeng, Y.; Rusling, J. F.; Yang, J. Ordered electrochemically active films of hemoglobin, didodecyldimethylammonium ions and clay. Langmuir 1999, 15, 7022-7030.
    • (1999) Langmuir , vol.15 , pp. 7022-7030
    • Chen, X.1    Hu, N.2    Zeng, Y.3    Rusling, J.F.4    Yang, J.5
  • 12
    • 0001612509 scopus 로고    scopus 로고
    • Phase-separated two-component self-assembled organosilane monolayers and their use in selective adsorption of a protein
    • (a) Fang, J.; Knobler, C. M. Phase-separated two-component self-assembled organosilane monolayers and their use in selective adsorption of a protein. Langmuir 1996, 12, 1368-1374.
    • (1996) Langmuir , vol.12 , pp. 1368-1374
    • Fang, J.1    Knobler, C.M.2
  • 13
    • 0001604172 scopus 로고
    • Plasmon resonance permits in-situ measurement of protein adsorption on self-assembled monolayer of alkanethiolates on gold
    • (b) Mrksich, M.; Sigal, G. B.; Whitesides, G. M. Plasmon resonance permits in-situ measurement of protein adsorption on self-assembled monolayer of alkanethiolates on gold. Langmuir 1995, 11, 4383-4385.
    • (1995) Langmuir , vol.11 , pp. 4383-4385
    • Mrksich, M.1    Sigal, G.B.2    Whitesides, G.M.3
  • 14
    • 0032183316 scopus 로고    scopus 로고
    • Electron-transfer properties of cytochrome c Langmuir-Blodgett films and interactions of cytochrome c with lipids
    • (a) Boussaad, A.; Dziri, L.; Arechabalata, R.; Tao, N. J.; Leblanc R. M. Electron-transfer properties of cytochrome c Langmuir-Blodgett films and interactions of cytochrome c with lipids. Langmuir 1998, 14, 6215-6219.
    • (1998) Langmuir , vol.14 , pp. 6215-6219
    • Boussaad, A.1    Dziri, L.2    Arechabalata, R.3    Tao, N.J.4    Leblanc, R.M.5
  • 15
    • 0027372021 scopus 로고
    • Thermal stability of protein secondary structure in Langmuir-Blodgett films
    • (b) Nicolini, C.; Erokhin, V.; Antolini, F.; Catasti, P.; Facci, P. Thermal stability of protein secondary structure in Langmuir-Blodgett films. Biochim. Biophys. Acta 1993, 1158, 273-278.
    • (1993) Biochim. Biophys. Acta , vol.1158 , pp. 273-278
    • Nicolini, C.1    Erokhin, V.2    Antolini, F.3    Catasti, P.4    Facci, P.5
  • 17
    • 0032800787 scopus 로고    scopus 로고
    • Electrostatic immobilization of glucose oxidase in a weak acid, polyelectrolyte hyperbranched ultrathin film on gold: Fabrication characterization, and enzymatic activity
    • (b) Franchina, J. G.; Lackowski, W. M.; Dermody, D. L.; Crooks, R. M.; Bergbreiter, D. E.; Sirkar, K.; Russell, R. J.; Pishko, M. V. Electrostatic immobilization of glucose oxidase in a weak acid, polyelectrolyte hyperbranched ultrathin film on gold: fabrication characterization, and enzymatic activity. Anal. Chem. 1999, 71, 3133-3139.
    • (1999) Anal. Chem. , vol.71 , pp. 3133-3139
    • Franchina, J.G.1    Lackowski, W.M.2    Dermody, D.L.3    Crooks, R.M.4    Bergbreiter, D.E.5    Sirkar, K.6    Russell, R.J.7    Pishko, M.V.8
  • 18
    • 0000913547 scopus 로고    scopus 로고
    • Nanoencapsulation of cytochrome c and horseradish peroxidase at the galleries of α-zirconium phosphate
    • Kumar, C. V.; McLendon, G. L. Nanoencapsulation of cytochrome c and horseradish peroxidase at the galleries of α-zirconium phosphate. Chem. Mater. 1997, 9, 863-870.
    • (1997) Chem. Mater. , vol.9 , pp. 863-870
    • Kumar, C.V.1    McLendon, G.L.2
  • 19
    • 0037174353 scopus 로고    scopus 로고
    • Entrapping enzyme in a functionalized nanoporous support
    • (a) Lei, C.; Shin, Y.; Liu, J.; Ackerman, E. J. Entrapping enzyme in a functionalized nanoporous support. J. Am. Chem. Soc. 2002, 124, 11242-11243.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11242-11243
    • Lei, C.1    Shin, Y.2    Liu, J.3    Ackerman, E.J.4
  • 20
    • 0035965078 scopus 로고    scopus 로고
    • Enzyme immobilization using SBA-15 mesoporous molecular sieves with functionalised surface
    • (b) Yiu, H. H. P.; Wright, P. A.; Botting, N. P. Enzyme immobilization using SBA-15 mesoporous molecular sieves with functionalised surface. J. Mol. Catal. B: Enzym. 2001, 15, 81-92.
    • (2001) J. Mol. Catal. B: Enzym. , vol.15 , pp. 81-92
    • Yiu, H.H.P.1    Wright, P.A.2    Botting, N.P.3
  • 21
    • 0036799739 scopus 로고    scopus 로고
    • Electrostatic assembly of nanoparticles and biomolecules
    • and references therein
    • (a) Sastry, M.; Rao, M.; Ganesh, K N. Electrostatic assembly of nanoparticles and biomolecules. Acc. Chem. Res. 2002, 35, 847-855 and references therein,
    • (2002) Acc. Chem. Res. , vol.35 , pp. 847-855
    • Sastry, M.1    Rao, M.2    Ganesh, K.N.3
  • 22
    • 0036568555 scopus 로고    scopus 로고
    • Entrapment of proteins and DNA in thermally evaporated lipid films
    • and references therein
    • (b) Sastry, M. Entrapment of proteins and DNA in thermally evaporated lipid films. Trends Biotechnol. 2002, 20, 185-189 and references therein.
    • (2002) Trends Biotechnol. , vol.20 , pp. 185-189
    • Sastry, M.1
  • 23
    • 0035807172 scopus 로고    scopus 로고
    • Protein-friendly intercalation of cytochrome c and hemoglobin into thermally evaporated anionic and cationic lipid films: A new approach based on diffusion from solution
    • Gole, A.; Chaudhari, P.; Kaur, J.; Sastry, M. Protein-friendly intercalation of cytochrome c and hemoglobin into thermally evaporated anionic and cationic lipid films: A new approach based on diffusion from solution. Langmuir 2001, 17, 5646-5656.
    • (2001) Langmuir , vol.17 , pp. 5646-5656
    • Gole, A.1    Chaudhari, P.2    Kaur, J.3    Sastry, M.4
  • 24
    • 0034696213 scopus 로고    scopus 로고
    • Encapsulation and biocatalytic activity of the enzyme pepsin in fatty lipid films by selective electrostatic interactions
    • Gole, A.; Dash, C.; Rao, M.; Sastry, M. Encapsulation and biocatalytic activity of the enzyme pepsin in fatty lipid films by selective electrostatic interactions. J. Chem. Soc., Chem. Commun. 2000, 297-298.
    • (2000) J. Chem. Soc., Chem. Commun. , pp. 297-298
    • Gole, A.1    Dash, C.2    Rao, M.3    Sastry, M.4
  • 25
    • 0034665683 scopus 로고    scopus 로고
    • Fabrication, characterization, and enzymatic activity of encapsulated fungal protease-fatty lipid biocomposite films
    • Gole, A.; Dash, C.; Mandale, A. B.; Rao, M.; Sastry, M. Fabrication, characterization, and enzymatic activity of encapsulated fungal protease-fatty lipid biocomposite films. Anal. Chem. 2000, 72, 4301-4309.
    • (2000) Anal. Chem. , vol.72 , pp. 4301-4309
    • Gole, A.1    Dash, C.2    Mandale, A.B.3    Rao, M.4    Sastry, M.5
  • 26
    • 0035909196 scopus 로고    scopus 로고
    • Enhanced temperature and pH stability of fatty amine-endoglucanase composites: Fabrication, substrate protection, and biological activity
    • Gole, A.; Vyas, S.; Sainkar, S. R.; Lachke, A. L.; Sastry, M. Enhanced temperature and pH stability of fatty amine-endoglucanase composites: Fabrication, substrate protection, and biological activity. Langmuir 2001, 17, 5964-5970.
    • (2001) Langmuir , vol.17 , pp. 5964-5970
    • Gole, A.1    Vyas, S.2    Sainkar, S.R.3    Lachke, A.L.4    Sastry, M.5
  • 27
    • 0035988032 scopus 로고    scopus 로고
    • Penicillin G Acylase-fatty lipid biocomposite films show excellent catalytic activity and long-term stability/reusability
    • Phadtare, S.; Parekh, P.; Gole, A.; Patil. M.; Pundle, A.; Prabhune, A.; Sastry, M. Penicillin G Acylase-fatty lipid biocomposite films show excellent catalytic activity and long-term stability/reusability. Botechnol. Prog. 2002, 18, 483-488.
    • (2002) Botechnol. Prog. , vol.18 , pp. 483-488
    • Phadtare, S.1    Parekh, P.2    Gole, A.3    Patil, M.4    Pundle, A.5    Prabhune, A.6    Sastry, M.7
  • 28
    • 0035919907 scopus 로고    scopus 로고
    • A new method for the generation of patterned protein films by encapsulation in arrays of thermally evaporated lipids
    • Gole, A.; Sastry, M. A new method for the generation of patterned protein films by encapsulation in arrays of thermally evaporated lipids. Biotechnol. Bioeng. 2001, 74, 172-178.
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 172-178
    • Gole, A.1    Sastry, M.2
  • 29
    • 0028980452 scopus 로고
    • Purification of α-L-arabinofuranosidase using a single-column mini-scale isoelectric focusing unit
    • (a) Sathivel, C.; Lachke, A.; Radhakrishnan, S. Purification of α-L-arabinofuranosidase using a single-column mini-scale isoelectric focusing unit. J. Chromatogr. A 1995, 705, 400-402.
    • (1995) J. Chromatogr. A , vol.705 , pp. 400-402
    • Sathivel, C.1    Lachke, A.2    Radhakrishnan, S.3
  • 30
    • 0033020936 scopus 로고    scopus 로고
    • Size separation of colloidal nanoparticles using a miniscale isoelectric focusing technique
    • (b) Gole, A.; Sathivel, C.; Lachke, A.; Sastry, M. Size separation of colloidal nanoparticles using a miniscale isoelectric focusing technique. J. Chromatogr. A 1999, 848, 485-490.
    • (1999) J. Chromatogr. A , vol.848 , pp. 485-490
    • Gole, A.1    Sathivel, C.2    Lachke, A.3    Sastry, M.4
  • 31
    • 84951279351 scopus 로고
    • Verwendung von Schwingquarzen zur Wägung dünner Schichten und zur Mikrowägung
    • (a) Sauerbrey, G. Verwendung von Schwingquarzen zur Wägung dünner Schichten und zur Mikrowägung. Z. Phys. (Munich) 1959, 155, 206-222.
    • (1959) Z. Phys. (Munich) , vol.155 , pp. 206-222
    • Sauerbrey, G.1
  • 32
    • 11744318388 scopus 로고
    • Measurement of interfacial processes at electrode surfaces with the electrochemical quartz crystal microbalance
    • (b) Buttry, D. A.; Ward, M. D. Measurement of interfacial processes at electrode surfaces with the electrochemical quartz crystal microbalance. Chem. Rev. 1992, 92, 1355-1379,
    • (1992) Chem. Rev. , vol.92 , pp. 1355-1379
    • Buttry, D.A.1    Ward, M.D.2
  • 33
    • 0000481024 scopus 로고
    • Self-assembled thiol monolayers with carboxylic acid functionality: Measuring pH-dependent phase transitions with the quartz crystal microbalance
    • (c) Wang, J.; Frostman, L. M.; Ward, M. D. Self-assembled thiol monolayers with carboxylic acid functionality: measuring pH-dependent phase transitions with the quartz crystal microbalance. J. Phys. Chem. 1992, 96, 5224-5228.
    • (1992) J. Phys. Chem. , vol.96 , pp. 5224-5228
    • Wang, J.1    Frostman, L.M.2    Ward, M.D.3
  • 34
    • 0014408856 scopus 로고
    • Purification of the internal invertase of yeast
    • Gascon, S.; Lampen, O. Purification of the internal invertase of yeast. J. Biol. Chem. 1968, 243, 1567-1572.
    • (1968) J. Biol. Chem. , vol.243 , pp. 1567-1572
    • Gascon, S.1    Lampen, O.2
  • 35
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • Somogyi, N. Notes on sugar determination. J. Biol. Chem. 1952, 195, 19-23.
    • (1952) J. Biol. Chem. , vol.195 , pp. 19-23
    • Somogyi, N.1
  • 37
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink, M. R.; Ghiron, C. A. Fluorescence quenching studies with proteins. Anal. Biochem. 1981, 114, 199-227.
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 38
    • 0032029753 scopus 로고    scopus 로고
    • Tertiary structural changes of the α-Hemolysin from Staphylococcus aureus on association with liposome membranes
    • Bortoleto, R. K.; de Oliveira A. H. C.; Ruller, R.; Arhi, R. K.; Ward, R. J. Tertiary structural changes of the α-Hemolysin from Staphylococcus aureus on association with liposome membranes. Arch. Biochem. Biophys. 1998, 351, 47-52.
    • (1998) Arch. Biochem. Biophys. , vol.351 , pp. 47-52
    • Bortoleto, R.K.1    De Oliveira, A.H.C.2    Ruller, R.3    Arhi, R.K.4    Ward, R.J.5
  • 39
    • 0033179684 scopus 로고    scopus 로고
    • Immobilized enzymes: Crystals or carriers?
    • (a) Tischer, W.; Kasche, V. Immobilized enzymes: crystals or carriers? Trends Biotechnol. 1999, 17, 326-335.
    • (1999) Trends Biotechnol. , vol.17 , pp. 326-335
    • Tischer, W.1    Kasche, V.2
  • 40
    • 0032550645 scopus 로고    scopus 로고
    • Loss of activity or gain in stability of oxidase upon their immobilization in hydrated silica: Significance of the electrostatic interactions of surface arginine residues at the entrance of the reaction channels
    • (b) Heller, J.; Heller, A. Loss of activity or gain in stability of oxidase upon their immobilization in hydrated silica: Significance of the electrostatic interactions of surface arginine residues at the entrance of the reaction channels. J. Am. Chem. Soc. 1998, 120, 4586-4590.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4586-4590
    • Heller, J.1    Heller, A.2
  • 41
    • 0342980384 scopus 로고    scopus 로고
    • Immobilization of invertase attached to a granular dimer acid-co-alkyl polyamine
    • (a) Tumturk, H.; Arslan, F.; Disli, A.; Tufan, Y. Immobilization of invertase attached to a granular dimer acid-co-alkyl polyamine. Food Chem. 2000, 69, 5-9.
    • (2000) Food Chem. , vol.69 , pp. 5-9
    • Tumturk, H.1    Arslan, F.2    Disli, A.3    Tufan, Y.4
  • 42
    • 1142263218 scopus 로고    scopus 로고
    • Preparation and properties of Sclerotium rolfsii invertase immobilized on indion 48-R
    • (b) Kotwal, S. M.; Shankar, V. Preparation and properties of Sclerotium rolfsii invertase immobilized on indion 48-R. Appl. Biochem. Biotechnol. 1997, 62, 151-158.
    • (1997) Appl. Biochem. Biotechnol. , vol.62 , pp. 151-158
    • Kotwal, S.M.1    Shankar, V.2
  • 43
    • 0016410551 scopus 로고
    • D-Xylose isomerase from Lactobacillus brevis
    • Yamanaka, K. D-Xylose isomerase from Lactobacillus brevis. Methods Enzymol. 1975, 41, 466-471.
    • (1975) Methods Enzymol. , vol.41 , pp. 466-471
    • Yamanaka, K.1
  • 44
    • 0038137900 scopus 로고    scopus 로고
    • Alumina-pepsin hybrid nanoparticles with orientation specific enzyme coupling
    • (a) Li, J.; Wang, J.; Gavalas, V. G.; Atwood, D. A.; Bachas, L. G. Alumina-pepsin hybrid nanoparticles with orientation specific enzyme coupling. Nano Lett. 2003, 3, 55-58.
    • (2003) Nano Lett. , vol.3 , pp. 55-58
    • Li, J.1    Wang, J.2    Gavalas, V.G.3    Atwood, D.A.4    Bachas, L.G.5
  • 45
    • 0029329146 scopus 로고
    • Covalent immobilization of α-amylase onto pHEMA microspheres: Preparation and application to fixed bed reactors
    • (b) Arica, M. Y.; Hasirci, V.; Alaeddinoglu, N. G. Covalent immobilization of α-amylase onto pHEMA microspheres: preparation and application to fixed bed reactors. Biomaterials 1995, 16, 761-768.
    • (1995) Biomaterials , vol.16 , pp. 761-768
    • Arica, M.Y.1    Hasirci, V.2    Alaeddinoglu, N.G.3
  • 46
    • 0037207018 scopus 로고    scopus 로고
    • Reversible immobilization of urease onto Procion Brown MX-5BR-Ni(II) attached polyamide hollow fiber membrane
    • (c) Akgol, S.; Yalcinkaya, Y.; Bayramoglu, G.; Denizli, A.; Arica, M. Y. Reversible immobilization of urease onto Procion Brown MX-5BR-Ni(II) attached polyamide hollow fiber membrane. Process Biochem. 2002, 38, 675-683.
    • (2002) Process Biochem. , vol.38 , pp. 675-683
    • Akgol, S.1    Yalcinkaya, Y.2    Bayramoglu, G.3    Denizli, A.4    Arica, M.Y.5
  • 47
    • 0034500248 scopus 로고    scopus 로고
    • Catalytic activity in organic solvents and stability of immobilized enzymes depends on the pore size and surface characteristic of mesoporous silica
    • (d) Takahashi, H.; Li, B.; Sasaki, T.; Miyazaki, C.; Kajino, T.; Inagaki, S. Catalytic activity in organic solvents and stability of immobilized enzymes depends on the pore size and surface characteristic of mesoporous silica. Chem. Mater. 2000, 12, 3301-3305.
    • (2000) Chem. Mater. , vol.12 , pp. 3301-3305
    • Takahashi, H.1    Li, B.2    Sasaki, T.3    Miyazaki, C.4    Kajino, T.5    Inagaki, S.6


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