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Volumn 19, Issue 9, 2014, Pages 14139-14194

Inorganic materials as supports for covalent enzyme immobilization: Methods and mechanisms

Author keywords

Activation; Covalent binding; Enzymes; Functionalization; Grafting; Immobilization; Inorganic; Mesoporous; Silica; Stabilization

Indexed keywords

CROSS LINKING REAGENT; HALOGENATED HYDROCARBON; IMMOBILIZED ENZYME; PROTEIN BINDING; SILICON DIOXIDE;

EID: 84907095838     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules190914139     Document Type: Review
Times cited : (392)

References (229)
  • 1
    • 84860804330 scopus 로고    scopus 로고
    • Enzyme stabilization and immobilization
    • Series: Methods in Molecular Biology; A product of Humana Press: New York, NY, USA
    • Minteer, S.D. Enzyme stabilization and immobilization. In Methods and Protocols; Series: Methods in Molecular Biology; A product of Humana Press: New York, NY, USA, 2011.
    • (2011) Methods and Protocols
    • Minteer, S.D.1
  • 2
    • 84857501859 scopus 로고    scopus 로고
    • Immobilization strategies to develop enzymatic biosensors
    • Sassolas, A.; Blum, L.J.; Leca-Bouvier, B.D. Immobilization strategies to develop enzymatic biosensors. Biotechnol. Adv. 2012, 30, 489-511.
    • (2012) Biotechnol. Adv. , vol.30 , pp. 489-511
    • Sassolas, A.1    Blum, L.J.2    Leca-Bouvier, B.D.3
  • 3
    • 84878698340 scopus 로고    scopus 로고
    • Immobilisation of enzymes on mesoporous silicate materials
    • Magner, E. Immobilisation of enzymes on mesoporous silicate materials. Chem. Soc. Rev. 2013, 42, 6213-6222.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 6213-6222
    • Magner, E.1
  • 4
    • 25444449268 scopus 로고    scopus 로고
    • Ordered mesoporous materials for bioadsorption and biocatalysis
    • Hartmann, M. Ordered mesoporous materials for bioadsorption and biocatalysis. Chem. Mater. 2005, 17, 4577-4593.
    • (2005) Chem. Mater. , vol.17 , pp. 4577-4593
    • Hartmann, M.1
  • 5
    • 32944473446 scopus 로고    scopus 로고
    • Immobilizing catalysts on porous materials
    • Zhao, X.S.; Bao, X.Y.; Guo, W.; Lee, F.Y. Immobilizing catalysts on porous materials. Mater. Today 2006, 9, 32-39.
    • (2006) Mater. Today , vol.9 , pp. 32-39
    • Zhao, X.S.1    Bao, X.Y.2    Guo, W.3    Lee, F.Y.4
  • 6
    • 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
  • 9
    • 79961235658 scopus 로고    scopus 로고
    • Perspective of recent progress in immobilization of enzymes
    • Tran, D.N.; Balkus, K.J. Perspective of recent progress in immobilization of enzymes. ACS Catal. 2011, 1, 956-968.
    • (2011) ACS Catal. , vol.1 , pp. 956-968
    • Tran, D.N.1    Balkus, K.J.2
  • 10
    • 44449174565 scopus 로고    scopus 로고
    • Oxidation of indole using chloroperoxidase and glucose oxidase immobilized on sba-15 as tandem biocatalyst
    • Jung, D.; Streb, C.; Hartmann, M. Oxidation of indole using chloroperoxidase and glucose oxidase immobilized on sba-15 as tandem biocatalyst. Microporous Mesoporous Mater. 2008, 113, 523-529.
    • (2008) Microporous Mesoporous Mater. , vol.113 , pp. 523-529
    • Jung, D.1    Streb, C.2    Hartmann, M.3
  • 12
    • 46049096923 scopus 로고    scopus 로고
    • Role of carbon nanotubes in electroanalytical chemistry. A review
    • Agüí, L.; Yáñez-Sedeño, P.; Pingarrón, J.M. Role of carbon nanotubes in electroanalytical chemistry. A review. Anal. Chim. Acta 2008, 622, 11-47.
    • (2008) Anal. Chim. Acta , vol.622 , pp. 11-47
    • Agüí, L.1    Yáñez-Sedeño, P.2    Pingarrón, J.M.3
  • 14
    • 0035344512 scopus 로고    scopus 로고
    • New pulp biobleaching system involving manganese peroxidase immobilized in a silica support with controlled pore sizes
    • Sasaki, T.; Kajino, T.; Li, B.; Sugiyama, H.; Takahashi, H. New pulp biobleaching system involving manganese peroxidase immobilized in a silica support with controlled pore sizes. Appl. Environ. Microbiol. 2001, 67, 2208-2212.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2208-2212
    • Sasaki, T.1    Kajino, T.2    Li, B.3    Sugiyama, H.4    Takahashi, H.5
  • 15
    • 74549115462 scopus 로고    scopus 로고
    • Biocatalysis with enzymes immobilized on mesoporous hosts: The status quo and future trends
    • Hartmann, M.; Jung, D. Biocatalysis with enzymes immobilized on mesoporous hosts: The status quo and future trends. J. Mater. Chem. 2010, 20, 844-857.
    • (2010) J. Mater. Chem. , vol.20 , pp. 844-857
    • Hartmann, M.1    Jung, D.2
  • 16
    • 84887076167 scopus 로고    scopus 로고
    • Improvement of P. Aeruginosa 42A2 lipase preparations for FAMEs production, both in immobilized and soluble form
    • Cesarini, S.; Pastor, F.I.J.; Diaz, P. Improvement of P. Aeruginosa 42A2 lipase preparations for FAMEs production, both in immobilized and soluble form. J. Mol. Catal. B Enzym. 2014, 99, 1-7.
    • (2014) J. Mol. Catal. B Enzym. , vol.99 , pp. 1-7
    • Cesarini, S.1    Pastor, F.I.J.2    Diaz, P.3
  • 18
    • 84896325803 scopus 로고    scopus 로고
    • Production of biodiesel using a nanoscaled immobilized lipase as the catalyst
    • Liu, Y.; Hua, X. Production of biodiesel using a nanoscaled immobilized lipase as the catalyst. Catal. Lett. 2014, 144, 248-251.
    • (2014) Catal. Lett. , vol.144 , pp. 248-251
    • Liu, Y.1    Hua, X.2
  • 19
    • 77953390460 scopus 로고    scopus 로고
    • Physical and chemical lipase adsorption on sba-15: Effect of different interactions on enzyme loading and catalytic performance
    • Salis, A.; Casula, M.F.; Bhattacharyya, M.S.; Pinna, M.; Solinas, V.; Monduzzi, M. Physical and chemical lipase adsorption on sba-15: Effect of different interactions on enzyme loading and catalytic performance. Chem Cat Chem 2010, 2, 322-329.
    • (2010) Chem Cat Chem , vol.2 , pp. 322-329
    • Salis, A.1    Casula, M.F.2    Bhattacharyya, M.S.3    Pinna, M.4    Solinas, V.5    Monduzzi, M.6
  • 20
    • 44649132757 scopus 로고    scopus 로고
    • Comparison among immobilised lipases on macroporous polypropylene toward biodiesel synthesis
    • Salis, A.; Pinna, M.; Monduzzi, M.; Solinas, V. Comparison among immobilised lipases on macroporous polypropylene toward biodiesel synthesis. J. Mol. Catal. B Enzym. 2008, 54, 19-26.
    • (2008) J. Mol. Catal. B Enzym. , vol.54 , pp. 19-26
    • Salis, A.1    Pinna, M.2    Monduzzi, M.3    Solinas, V.4
  • 21
    • 84886852119 scopus 로고    scopus 로고
    • Celb and β-glucosidase immobilization for carboxymethyl cellulose hydrolysis
    • Tran, C.T.H.; Nosworthy, N.J.; Kondyurin, A.; McKenzie, D.R.; Bilek, M.M.M. Celb and β-glucosidase immobilization for carboxymethyl cellulose hydrolysis. RSC Adv. 2013, 3, 23604-23611.
    • (2013) RSC Adv. , vol.3 , pp. 23604-23611
    • Tran, C.T.H.1    Nosworthy, N.J.2    Kondyurin, A.3    McKenzie, D.R.4    Bilek, M.M.M.5
  • 22
    • 77956310474 scopus 로고    scopus 로고
    • Hemoglobin immobilized on mesoporous silica as effective material for the removal of polycyclic aromatic hydrocarbons pollutants from water
    • Laveille, P.; Falcimaigne, A.; Chamouleau, F.; Renard, G.; Drone, J.; Fajula, F.; Pulvin, S.; Thomas, D.; Bailly, C.; Galarneau, A. Hemoglobin immobilized on mesoporous silica as effective material for the removal of polycyclic aromatic hydrocarbons pollutants from water. New J. Chem. 2010, 34, 2153-2165.
    • (2010) New J. Chem. , vol.34 , pp. 2153-2165
    • Laveille, P.1    Falcimaigne, A.2    Chamouleau, F.3    Renard, G.4    Drone, J.5    Fajula, F.6    Pulvin, S.7    Thomas, D.8    Bailly, C.9    Galarneau, A.10
  • 23
    • 33646154205 scopus 로고    scopus 로고
    • Laccases: Blue enzymes for green chemistry
    • Riva, S. Laccases: Blue enzymes for green chemistry. Trends Biotechnol. 2006, 24, 219-226.
    • (2006) Trends Biotechnol. , vol.24 , pp. 219-226
    • Riva, S.1
  • 24
    • 84871851300 scopus 로고    scopus 로고
    • Recent progress in biocatalysis with enzymes immobilized on mesoporous hosts
    • Zhou, Z.; Hartmann, M. Recent progress in biocatalysis with enzymes immobilized on mesoporous hosts. Top. Catal. 2012, 55, 1081-1100.
    • (2012) Top. Catal. , vol.55 , pp. 1081-1100
    • Zhou, Z.1    Hartmann, M.2
  • 26
    • 84858052739 scopus 로고    scopus 로고
    • Order-of-magnitude enhancement of an enzymatic hydrogen-air fuel cell based on pyrenyl carbon nanostructures
    • Krishnan, S.; Armstrong, F.A. Order-of-magnitude enhancement of an enzymatic hydrogen-air fuel cell based on pyrenyl carbon nanostructures. Chem. Sci. 2012, 3, 1015-1023.
    • (2012) Chem. Sci. , vol.3 , pp. 1015-1023
    • Krishnan, S.1    Armstrong, F.A.2
  • 28
    • 57849086401 scopus 로고    scopus 로고
    • Enzyme-functionalized mesoporous silica for bioanalytical applications
    • Ispas, C.; Sokolov, I.; Andreescu, S. Enzyme-functionalized mesoporous silica for bioanalytical applications. Anal. Bioanal. Chem. 2009, 393, 543-554.
    • (2009) Anal. Bioanal. Chem. , vol.393 , pp. 543-554
    • Ispas, C.1    Sokolov, I.2    Andreescu, S.3
  • 29
    • 0017267831 scopus 로고
    • Covalent coupling methods for inorganic support materials
    • Klaus, M., Ed.; Academic Press: Waltham, MA, USA
    • Weetall, H.H. Covalent coupling methods for inorganic support materials. In Methods in Enzymology; Klaus, M., Ed.; Academic Press: Waltham, MA, USA, 1976; Volume 44, pp. 134-148.
    • (1976) Methods in Enzymology , vol.44 , pp. 134-148
    • Weetall, H.H.1
  • 30
    • 84880082972 scopus 로고    scopus 로고
    • Immobilization of enzymes on porous silicas-benefits and challenges
    • Hartmann, M.; Kostrov, X. Immobilization of enzymes on porous silicas-benefits and challenges. Chem. Soc. Rev. 2013, 42, 6277-6289.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 6277-6289
    • Hartmann, M.1    Kostrov, X.2
  • 32
    • 74449091448 scopus 로고    scopus 로고
    • Improved enzymatic activity of thermomyces lanuginosus lipase immobilized in a hydrophobic particulate mesoporous carrier
    • Sörensen, M.H.; Ng, J.B.S.; Bergström, L.; Alberius, P.C.A. Improved enzymatic activity of thermomyces lanuginosus lipase immobilized in a hydrophobic particulate mesoporous carrier. J. Colloid Interface Sci. 2010, 343, 359-365.
    • (2010) J. Colloid Interface Sci. , vol.343 , pp. 359-365
    • Sörensen, M.H.1    Ng, J.B.S.2    Bergström, L.3    Alberius, P.C.A.4
  • 33
    • 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, A.; Rodrigues, R.C.; Fernandez-Lafuente, R. Heterofunctional supports in enzyme immobilization: From traditional immobilization protocols to opportunities in tuning enzyme properties. Biomacromolecules 2013, 14, 2433-2462.
    • (2013) Biomacromolecules , vol.14 , pp. 2433-2462
    • Barbosa, O.1    Torres, R.2    Ortiz, C.3    Berenguer-Murcia, A.4    Rodrigues, R.C.5    Fernandez-Lafuente, R.6
  • 34
    • 0023063750 scopus 로고
    • Characterization of immobilized biocatalysts
    • Klaus, M., Ed.; Academic Press: Waltham, MA, USA
    • Buchholz, K.; Klein, J. Characterization of immobilized biocatalysts. In Methods in Enzymology; Klaus, M., Ed.; Academic Press: Waltham, MA, USA, 1987; Volume 135, pp. 3-30.
    • (1987) Methods in Enzymology , vol.135 , pp. 3-30
    • Buchholz, K.1    Klein, J.2
  • 35
    • 0027619202 scopus 로고
    • Preparation of immobilized proteins covalently coupled through silane coupling agents to inorganic supports
    • Weetall, H.H. Preparation of immobilized proteins covalently coupled through silane coupling agents to inorganic supports. Appl. Biochem. Biotechnol. 1993, 41, 157-188.
    • (1993) Appl. Biochem. Biotechnol. , vol.41 , pp. 157-188
    • Weetall, H.H.1
  • 36
    • 0017279164 scopus 로고
    • Enzymes immobilized to cellulose
    • Klaus, M., Ed.; Academic Press: Waltham, MA, USA
    • Lilly, M.D. Enzymes immobilized to cellulose. In Methods in Enzymology; Klaus, M., Ed.; Academic Press: Waltham, MA, USA, 1976; Volume 44, pp. 46-53.
    • (1976) Methods in Enzymology , vol.44 , pp. 46-53
    • Lilly, M.D.1
  • 37
    • 0017248044 scopus 로고
    • Immobilization of enzymes to agar, agarose, and sephadex support
    • Klaus, M., Ed.; Academic Press: Waltham, MA, USA
    • Porath, J.; Axén, R. Immobilization of enzymes to agar, agarose, and sephadex support. In Methods in Enzymology; Klaus, M., Ed.; Academic Press: Waltham, MA, USA, 1976; Volume 44, pp. 19-45.
    • (1976) Methods in Enzymology , vol.44 , pp. 19-45
    • Porath, J.1    Axén, R.2
  • 38
    • 0017224408 scopus 로고
    • Enzymes covalently bound to polyacrylic and polymethacrylic copolymers
    • Klaus, M., Ed.; Academic Press: Waltham, MA, USA
    • Epton, R.; Hibbert, B.L.; Thomas, T.H. Enzymes covalently bound to polyacrylic and polymethacrylic copolymers. In Methods in Enzymology; Klaus, M., Ed.; Academic Press: Waltham, MA, USA, 1976; Volume 44, pp. 84-107.
    • (1976) Methods in Enzymology , vol.44 , pp. 84-107
    • Epton, R.1    Hibbert, B.L.2    Thomas, T.H.3
  • 39
    • 0017222261 scopus 로고
    • Immobilization of enzymes to various acrylic copolymer
    • Klaus, M., Ed.; Academic Press Waltham, MA, USA
    • Mosbach, R.; Koch-Schmidt, A.-C.; Mosbach, K. Immobilization of enzymes to various acrylic copolymer. In Methods in Enzymology; Klaus, M., Ed.; Academic Press Waltham, MA, USA, 1976; Volume 44, pp. 53-65.
    • (1976) Methods in Enzymology , vol.44 , pp. 53-65
    • Mosbach, R.1    Koch-Schmidt, A.-C.2    Mosbach, K.3
  • 40
    • 61349113312 scopus 로고    scopus 로고
    • Activation of nylon net and its application to a biosensor for determination of glucose in human serum
    • Nan, C.; Zhang, Y.; Zhang, G.; Dong, C.; Shuang, S.; Choi, M.M.F. Activation of nylon net and its application to a biosensor for determination of glucose in human serum. Enzym. Microb. Technol. 2009, 44, 249-253.
    • (2009) Enzym. Microb. Technol. , vol.44 , pp. 249-253
    • Nan, C.1    Zhang, Y.2    Zhang, G.3    Dong, C.4    Shuang, S.5    Choi, M.M.F.6
  • 41
    • 0017249418 scopus 로고
    • Immobilization of enzymes on nylon
    • Klaus, M., Ed.; Academic Press: Waltham, MA, USA
    • Hornby, W.E.; Goldstein, L. Immobilization of enzymes on nylon. In Methods in Enzymology; Klaus, M., Ed.; Academic Press: Waltham, MA, USA, 1976; Volume 44, pp. 118-134.
    • (1976) Methods in Enzymology , vol.44 , pp. 118-134
    • Hornby, W.E.1    Goldstein, L.2
  • 43
    • 84862757759 scopus 로고    scopus 로고
    • Immobilization of lipase from mucor miehei and rhizopus oryzae into mesoporous silica-The effect of varied particle size and morphology
    • Gustafsson, H.; Johansson, E.M.; Barrabino, A.; Odén, M.; Holmberg, K. Immobilization of lipase from mucor miehei and rhizopus oryzae into mesoporous silica-the effect of varied particle size and morphology. Colloids Surf. B. Biointerfaces 2012, 100, 22-30.
    • (2012) Colloids Surf. B. Biointerfaces , vol.100 , pp. 22-30
    • Gustafsson, H.1    Johansson, E.M.2    Barrabino, A.3    Odén, M.4    Holmberg, K.5
  • 44
    • 0001939504 scopus 로고    scopus 로고
    • A general survey of quartz and quartz-like materials: Packing distortions, temperature, and pressure effects
    • Philippot, E.; Palmier, D.; Pintard, M.; Goiffon, A. A general survey of quartz and quartz-like materials: Packing distortions, temperature, and pressure effects. J. Solid State Chem. 1996, 123, 1-13.
    • (1996) J. Solid State Chem. , vol.123 , pp. 1-13
    • Philippot, E.1    Palmier, D.2    Pintard, M.3    Goiffon, A.4
  • 45
    • 0018302032 scopus 로고
    • John Wiley and Sons: New York, NY, USA
    • Iler, R.K. The Chemistry of Silica; John Wiley and Sons: New York, NY, USA, 1979.
    • (1979) The Chemistry of Silica
    • Iler, R.K.1
  • 46
    • 84877757895 scopus 로고    scopus 로고
    • Silica surface features and their role in the adsorption of biomolecules: Computational modeling and experiments
    • Rimola, A.; Costa, D.; Sodupe, M.; Lambert, J.-F.; Ugliengo, P. Silica surface features and their role in the adsorption of biomolecules: Computational modeling and experiments. Chem. Rev. 2013, 113, 4216-4313.
    • (2013) Chem. Rev. , vol.113 , pp. 4216-4313
    • Rimola, A.1    Costa, D.2    Sodupe, M.3    Lambert, J.-F.4    Ugliengo, P.5
  • 47
    • 84905649040 scopus 로고    scopus 로고
    • Enzyme immobilization by adsorption: A review
    • Jesionowski, T.; Zdarta, J.; Krajewska, B. Enzyme immobilization by adsorption: A review. Adsorption 2014, 20, 801-821.
    • (2014) Adsorption , vol.20 , pp. 801-821
    • Jesionowski, T.1    Zdarta, J.2    Krajewska, B.3
  • 48
    • 0000016810 scopus 로고
    • First natural occurrence of coesite
    • Chao, E.C.T.; Shoemaker, E.M.; Madsen, B.M. First natural occurrence of coesite. Science 1960, 132, 220-222.
    • (1960) Science , vol.132 , pp. 220-222
    • Chao, E.C.T.1    Shoemaker, E.M.2    Madsen, B.M.3
  • 50
    • 66149126829 scopus 로고
    • Über siliciumchalkogenide. Vi. Zur kenntnis der faserigen siliciumdioxyd-modifikation
    • Weiss, A.; Weiss, A. Über siliciumchalkogenide. Vi. Zur kenntnis der faserigen siliciumdioxyd-modifikation. Z. Anorg. Allg. Chem. 1954, 276, 95-112.
    • (1954) Z. Anorg. Allg. Chem. , vol.276 , pp. 95-112
    • Weiss, A.1    Weiss, A.2
  • 51
    • 0642335747 scopus 로고    scopus 로고
    • Energies of strained silica rings
    • Hamann, D.R. Energies of strained silica rings. Phys. Rev. B 1997, 55, 14784-14793.
    • (1997) Phys. Rev. B , vol.55 , pp. 14784-14793
    • Hamann, D.R.1
  • 52
    • 0034634766 scopus 로고    scopus 로고
    • The surface chemistry of amorphous silica. Zhuravlev model
    • Zhuravlev, L.T. The surface chemistry of amorphous silica. Zhuravlev model. Colloids Surf. Physicochem. Eng. Asp. 2000, 173, 1-38.
    • (2000) Colloids Surf. Physicochem. Eng. Asp. , vol.173 , pp. 1-38
    • Zhuravlev, L.T.1
  • 53
    • 33847799605 scopus 로고
    • Infrared studies of reactions on oxide surfaces. 7. Mechanism of the adsorption of water and ammonia on dehydroxylated silica
    • Morrow, B.A.; Cody, I.A.; Lee, L.S.M. Infrared studies of reactions on oxide surfaces. 7. Mechanism of the adsorption of water and ammonia on dehydroxylated silica. J. Phys. Chem. 1976, 80, 2761-2767.
    • (1976) J. Phys. Chem. , vol.80 , pp. 2761-2767
    • Morrow, B.A.1    Cody, I.A.2    Lee, L.S.M.3
  • 54
    • 68949083509 scopus 로고    scopus 로고
    • Thermochemistry for silicic acid formation reaction: Prediction of new reaction pathway
    • Mondal, B.; Ghosh, D.; Das, A.K. Thermochemistry for silicic acid formation reaction: Prediction of new reaction pathway. Chem. Phys. Lett. 2009, 478, 115-119.
    • (2009) Chem. Phys. Lett. , vol.478 , pp. 115-119
    • Mondal, B.1    Ghosh, D.2    Das, A.K.3
  • 56
    • 33947479147 scopus 로고
    • Hydrogen bonding studies. V. The relative basicities of ethers, alkoxysilanes and siloxanes and the nature of the silicon-oxygen bond1,2
    • West, R.; Whatley, L.S.; Lake, K.J. Hydrogen bonding studies. V. The relative basicities of ethers, alkoxysilanes and siloxanes and the nature of the silicon-oxygen bond1,2. J. Am. Chem. Soc. 1961, 83, 761-764.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 761-764
    • West, R.1    Whatley, L.S.2    Lake, K.J.3
  • 57
    • 2942526613 scopus 로고    scopus 로고
    • Papirer, E., Ed.; CRC Press, Taylor & Francis Group: Santa Barbara, CA, USA
    • Davydov, V.Y. Adsorption on Silica Surfaces; Papirer, E., Ed.; CRC Press, Taylor & Francis Group: Santa Barbara, CA, USA, 2000; Volume 90, p. 63.
    • (2000) Adsorption on Silica Surfaces , vol.90 , pp. 63
    • Davydov, V.Y.1
  • 58
    • 36049041259 scopus 로고    scopus 로고
    • The structure of silicate anions in aqueous alkaline solutions
    • Knight, C.T.G.; Balec, R.J.; Kinrade, S.D. The structure of silicate anions in aqueous alkaline solutions. Angew. Chem. Int. Ed. 2007, 46, 8148-8152.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 8148-8152
    • Knight, C.T.G.1    Balec, R.J.2    Kinrade, S.D.3
  • 59
    • 1042290113 scopus 로고
    • Silicon-29 nmr study of the surface of silica gel by cross polarization and magic-angle spinning
    • Maciel, G.E.; Sindorf, D.W. Silicon-29 nmr study of the surface of silica gel by cross polarization and magic-angle spinning. J. Am. Chem. Soc. 1980, 102, 7606-7607.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7606-7607
    • MacIel, G.E.1    Sindorf, D.W.2
  • 60
    • 0017279162 scopus 로고
    • Adsorption and inorganic bridge formations
    • Klaus, M., Ed.; Academic Press: Waltham, MA, USA
    • Messing, R.A. Adsorption and inorganic bridge formations. In Methods in Enzymology; Klaus, M., Ed.; Academic Press: Waltham, MA, USA, 1976; Volume 44, pp. 148-169.
    • (1976) Methods in Enzymology , vol.44 , pp. 148-169
    • Messing, R.A.1
  • 65
    • 0025168065 scopus 로고
    • The preparation of alkyltrimethylammoniumkanemite complexes and their conversion to microporous materials
    • Yanagisawa, T.; Shimizu, T.; Kuroda, K.; Kato, C. The preparation of alkyltrimethylammoniumkanemite complexes and their conversion to microporous materials. Bull. Chem. Soc. Jpn. 1990, 63, 988-992.
    • (1990) Bull. Chem. Soc. Jpn. , vol.63 , pp. 988-992
    • Yanagisawa, T.1    Shimizu, T.2    Kuroda, K.3    Kato, C.4
  • 66
    • 2442502864 scopus 로고
    • Synthesis of highly ordered mesoporous materials from a layered polysilicate
    • Inagaki, S.; Fukushima, Y.; Kuroda, K. Synthesis of highly ordered mesoporous materials from a layered polysilicate. J. Chem. Soc. Chem. Commun. 1993, doi: 10.1039/C39930000680.
    • (1993) J. Chem. Soc. Chem. Commun.
    • Inagaki, S.1    Fukushima, Y.2    Kuroda, K.3
  • 69
    • 0026931265 scopus 로고
    • Ordered mesoporous molecular sieves synthesized by a liquid-crystal template mechanism
    • Kresge, C.T.; Leonowicz, M.E.; Roth, W.J.; Vartuli, J.C.; Beck, J.S. Ordered mesoporous molecular sieves synthesized by a liquid-crystal template mechanism. Nature 1992, 359, 710-712.
    • (1992) Nature , vol.359 , pp. 710-712
    • Kresge, C.T.1    Leonowicz, M.E.2    Roth, W.J.3    Vartuli, J.C.4    Beck, J.S.5
  • 70
    • 35348983485 scopus 로고    scopus 로고
    • Synthesis and functionalization of a mesoporous silica nanoparticle based on the sol-gel process and applications in controlled release
    • Trewyn, B.G.; Slowing, I.I.; Giri, S.; Chen, H.T.; Lin, V.S.Y. Synthesis and functionalization of a mesoporous silica nanoparticle based on the sol-gel process and applications in controlled release. Acc. Chem. Res. 2007, 40, 846-853.
    • (2007) Acc. Chem. Res. , vol.40 , pp. 846-853
    • Trewyn, B.G.1    Slowing, I.I.2    Giri, S.3    Chen, H.T.4    Lin, V.S.Y.5
  • 71
    • 0032559316 scopus 로고    scopus 로고
    • Triblock copolymer syntheses of mesoporous silica with periodic 50 to 300 angstrom pores
    • Zhao, D.; Feng, J.; Huo, Q.; Melosh, N.; Fredrickson, G.H.; Chmelka, B.F.; Stucky, G.D. Triblock copolymer syntheses of mesoporous silica with periodic 50 to 300 angstrom pores. Science 1998, 279, 548-552.
    • (1998) Science , vol.279 , pp. 548-552
    • Zhao, D.1    Feng, J.2    Huo, Q.3    Melosh, N.4    Fredrickson, G.H.5    Chmelka, B.F.6    Stucky, G.D.7
  • 72
    • 0031801728 scopus 로고    scopus 로고
    • Nonionic triblock and star diblock copolymer and oligomeric sufactant syntheses of highly ordered, hydrothermally stable, mesoporous silica structures
    • Zhao, D.; Huo, Q.; Feng, J.; Chmelka, B.F.; Stucky, G.D. Nonionic triblock and star diblock copolymer and oligomeric sufactant syntheses of highly ordered, hydrothermally stable, mesoporous silica structures. J. Am. Chem. Soc. 1998, 120, 6024-6036.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6024-6036
    • Zhao, D.1    Huo, Q.2    Feng, J.3    Chmelka, B.F.4    Stucky, G.D.5
  • 74
    • 85125418220 scopus 로고    scopus 로고
    • Mesoporous silica nanoparticles: Synthesis and applications
    • World Scientific: Singapore, Singapore
    • Vivero-Escoto, J.L.; Trewyn, B.G.; Lin, S.Y.V. Mesoporous silica nanoparticles: Synthesis and applications. In Annual Review of Nano Research; World Scientific: Singapore, Singapore, 2009; Volume 3, pp. 191-231.
    • (2009) Annual Review of Nano Research , vol.3 , pp. 191-231
    • Vivero-Escoto, J.L.1    Trewyn, B.G.2    Lin, S.Y.V.3
  • 75
    • 0040500022 scopus 로고
    • Templating of mesoporous molecular sieves by nonionic polyethylene oxide surfactants
    • Bagshaw, S.A.; Prouzet, E.; Pinnavaia, T.J. Templating of mesoporous molecular sieves by nonionic polyethylene oxide surfactants. Science 1995, 269, 1242-1244.
    • (1995) Science , vol.269 , pp. 1242-1244
    • Bagshaw, S.A.1    Prouzet, E.2    Pinnavaia, T.J.3
  • 78
    • 0016227164 scopus 로고
    • Porous glass for affinity chromatography applications
    • Weetall, H.H.; Filbert, A.M. porous glass for affinity chromatography applications. Methods Enzymol. 1974, 34, 59-72.
    • (1974) Methods Enzymol. , vol.34 , pp. 59-72
    • Weetall, H.H.1    Filbert, A.M.2
  • 79
    • 63249123191 scopus 로고    scopus 로고
    • Characterization and properties of catalase immobilized onto controlled pore glass and its application in batch and plug-flow type reactors
    • Alptekin, O.; Tükel, S.S.; Yildirim, D.; Alagöz, D. Characterization and properties of catalase immobilized onto controlled pore glass and its application in batch and plug-flow type reactors. J. Mol. Catal. B Enzym. 2009, 58, 124-131.
    • (2009) J. Mol. Catal. B Enzym. , vol.58 , pp. 124-131
    • Alptekin, O.1    Tükel, S.S.2    Yildirim, D.3    Alagöz, D.4
  • 80
    • 34347382387 scopus 로고    scopus 로고
    • Immobilization of mushroom tyrosinase on controlled pore glass: Effect of chemical modification
    • Girelli, A.M.; Mattei, E.; Messina, A.; Papaleo, D. Immobilization of mushroom tyrosinase on controlled pore glass: Effect of chemical modification. Sens. Actuators B Chem. 2007, 125, 48-54.
    • (2007) Sens. Actuators B Chem. , vol.125 , pp. 48-54
    • Girelli, A.M.1    Mattei, E.2    Messina, A.3    Papaleo, D.4
  • 81
    • 77952958931 scopus 로고    scopus 로고
    • Conformational changes and catalytic competency of hydrolases adsorbing on fumed silica nanoparticles: I. Tertiary structure
    • Cruz, J.C.; Pfromm, P.H.; Tomich, J.M.; Rezac, M.E. Conformational changes and catalytic competency of hydrolases adsorbing on fumed silica nanoparticles: I. Tertiary structure. Colloids Surf. B Biointerfaces 2010, 79, 97-104.
    • (2010) Colloids Surf. B Biointerfaces , vol.79 , pp. 97-104
    • Cruz, J.C.1    Pfromm, P.H.2    Tomich, J.M.3    Rezac, M.E.4
  • 83
    • 0003310264 scopus 로고
    • The sol-gel process
    • Hench, L.L.; West, J.K. The sol-gel process. Chem. Rev. 1990, 90, 33-72.
    • (1990) Chem. Rev. , vol.90 , pp. 33-72
    • Hench, L.L.1    West, J.K.2
  • 84
    • 67349230855 scopus 로고    scopus 로고
    • Synthesis of silica nanoparticles by modified sol-gel process: The effect of mixing modes of the reactants and drying techniques
    • Jafarzadeh, M.; Rahman, I.A.; Sipaut, C.S. Synthesis of silica nanoparticles by modified sol-gel process: The effect of mixing modes of the reactants and drying techniques. J. Sol-Gel Sci. Technol. 2009, 50, 328-336.
    • (2009) J. Sol-Gel Sci. Technol. , vol.50 , pp. 328-336
    • Jafarzadeh, M.1    Rahman, I.A.2    Sipaut, C.S.3
  • 85
    • 20444406055 scopus 로고
    • Controlled growth of monodisperse silica spheres in the micron size range
    • Stöber, W.; Fink, A.; Bohn, E. Controlled growth of monodisperse silica spheres in the micron size range. J. Colloid Interface Sci. 1968, 26, 62-69.
    • (1968) J. Colloid Interface Sci. , vol.26 , pp. 62-69
    • Stöber, W.1    Fink, A.2    Bohn, E.3
  • 89
    • 84880142529 scopus 로고    scopus 로고
    • Silica nanoparticles immobilized benzoylthiourea ferrous complex as an efficient and reusable catalyst for one-pot synthesis of benzopyranopyrimidines
    • Amirnejat, S.; Movahedi, F.; Masrouri, H.; Mohadesi, M.; Kassaee, M.Z. Silica nanoparticles immobilized benzoylthiourea ferrous complex as an efficient and reusable catalyst for one-pot synthesis of benzopyranopyrimidines. J. Mol. Catal. A Chem. 2013, 378, 135-141.
    • (2013) J. Mol. Catal. A Chem. , vol.378 , pp. 135-141
    • Amirnejat, S.1    Movahedi, F.2    Masrouri, H.3    Mohadesi, M.4    Kassaee, M.Z.5
  • 90
    • 84895068605 scopus 로고    scopus 로고
    • Recent development of silica nanoparticles as delivery vectors for cancer imaging and therapy
    • Wu, X.; Wu, M.; Zhao, J.X. Recent development of silica nanoparticles as delivery vectors for cancer imaging and therapy. Nanomed. Nanotechnol. Biol. Med. 2014, 10, 297-312.
    • (2014) Nanomed. Nanotechnol. Biol. Med. , vol.10 , pp. 297-312
    • Wu, X.1    Wu, M.2    Zhao, J.X.3
  • 91
    • 79952532841 scopus 로고    scopus 로고
    • Immobilization of glucose oxidase and platinum on mesoporous silica nanoparticles for the fabrication of glucose biosensor
    • Li, H.; He, J.; Zhao, Y.; Wu, D.; Cai, Y.; Wei, Q.; Yang, M. Immobilization of glucose oxidase and platinum on mesoporous silica nanoparticles for the fabrication of glucose biosensor. Electrochim. Acta 2011, 56, 2960-2965.
    • (2011) Electrochim. Acta , vol.56 , pp. 2960-2965
    • Li, H.1    He, J.2    Zhao, Y.3    Wu, D.4    Cai, Y.5    Wei, Q.6    Yang, M.7
  • 92
    • 84857501798 scopus 로고    scopus 로고
    • Potential applications of enzymes immobilized on/in nano materials: A review
    • Ansari, S.A.; Husain, Q. Potential applications of enzymes immobilized on/in nano materials: A review. Biotechnol. Adv. 2012, 30, 512-523.
    • (2012) Biotechnol. Adv. , vol.30 , pp. 512-523
    • Ansari, S.A.1    Husain, Q.2
  • 93
    • 84894070146 scopus 로고    scopus 로고
    • Monodispersed silica nanoparticles as carrier for co-immobilization of bi-enzyme and its application for glucose biosensing
    • Yang, H.; Wei, W.; Liu, S. Monodispersed silica nanoparticles as carrier for co-immobilization of bi-enzyme and its application for glucose biosensing. Spectrochim. Acta Part A Mol. Biomol. Spectrosc. 2014, 125, 183-188.
    • (2014) Spectrochim. Acta Part A Mol. Biomol. Spectrosc. , vol.125 , pp. 183-188
    • Yang, H.1    Wei, W.2    Liu, S.3
  • 94
    • 80054883655 scopus 로고    scopus 로고
    • A-amylase immobilization on the silica nanoparticles for cleaning performance towards starch soils in laundry detergents
    • Soleimani, M.; Khani, A.; Najafzadeh, K. A-amylase immobilization on the silica nanoparticles for cleaning performance towards starch soils in laundry detergents. J. Mol. Catal. B Enzym. 2012, 74, 1-5.
    • (2012) J. Mol. Catal. B Enzym. , vol.74 , pp. 1-5
    • Soleimani, M.1    Khani, A.2    Najafzadeh, K.3
  • 95
    • 84872422197 scopus 로고    scopus 로고
    • Catalytic behavior of carbonic anhydrase enzyme immobilized onto nonporous silica nanoparticles for enhancing co2 absorption into a carbonate solution
    • Zhang, S.; Lu, Y.; Ye, X. Catalytic behavior of carbonic anhydrase enzyme immobilized onto nonporous silica nanoparticles for enhancing co2 absorption into a carbonate solution. Int. J. Greenh. Gas Control 2013, 13, 17-25.
    • (2013) Int. J. Greenh. Gas Control , vol.13 , pp. 17-25
    • Zhang, S.1    Lu, Y.2    Ye, X.3
  • 96
    • 85040955804 scopus 로고
    • Deer, W.A., Howie, R.A., Zussman, J., Eds.; Longman Scientific & Technical: Harlow, England; Wiley: New York, NY, USA
    • Deer, W.A. An Introduction to the Rock-forming Minerals; Deer, W.A., Howie, R.A., Zussman, J., Eds.; Longman Scientific & Technical: Harlow, England; Wiley: New York, NY, USA, 1992.
    • (1992) An Introduction to the Rock-forming Minerals
    • Deer, W.A.1
  • 99
    • 74549198707 scopus 로고    scopus 로고
    • Biodegradation of a simulated textile effluent by immobilised-coated laccase in laboratory-scale reactors
    • Osma, J.F.; Toca-Herrera, J.L.; Rodríguez-Couto, S. Biodegradation of a simulated textile effluent by immobilised-coated laccase in laboratory-scale reactors. Appl. Catal. A Gen. 2010, 373, 147-153.
    • (2010) Appl. Catal. A Gen. , vol.373 , pp. 147-153
    • Osma, J.F.1    Toca-Herrera, J.L.2    Rodríguez-Couto, S.3
  • 100
    • 84901202066 scopus 로고    scopus 로고
    • Nanostructured tin dioxide-A promising multipurpose support material for catalytic and biocatalytic applications
    • Dimitrov, M.; Guncheva, M.; Zhiryakova, D.; Lazarova, T.; Lalev, G.; Tsoncheva, T. Nanostructured tin dioxide-A promising multipurpose support material for catalytic and biocatalytic applications. Chem. Eng. J. 2014, 252, 55-63.
    • (2014) Chem. Eng. J. , vol.252 , pp. 55-63
    • Dimitrov, M.1    Guncheva, M.2    Zhiryakova, D.3    Lazarova, T.4    Lalev, G.5    Tsoncheva, T.6
  • 101
    • 84900490041 scopus 로고    scopus 로고
    • Macroporous ceramics: Novel route using partial sintering of alumina-powder agglomerates obtained by spray-drying
    • Jean, G.; Sciamanna, V.; Demuynck, M.; Cambier, F.; Gonon, M. Macroporous ceramics: Novel route using partial sintering of alumina-powder agglomerates obtained by spray-drying. Ceram. Int. 2014, 40, 10197-10203.
    • (2014) Ceram. Int. , vol.40 , pp. 10197-10203
    • Jean, G.1    Sciamanna, V.2    Demuynck, M.3    Cambier, F.4    Gonon, M.5
  • 102
    • 84897915830 scopus 로고    scopus 로고
    • The effects of the chemical composition of titanate nanotubes and solvent type on 3-aminopropyltriethoxysilane grafting efficiency
    • Pontón, P.I.; d'Almeida, J.R.; Marinkovic, B.A.; Savić, S.M.; Mancic, L.; Rey, N.A.; Morgado, E., Jr.; Rizzo, F.C. The effects of the chemical composition of titanate nanotubes and solvent type on 3-aminopropyltriethoxysilane grafting efficiency. Appl. Surf. Sci. 2014, 301, 315-322.
    • (2014) Appl. Surf. Sci. , vol.301 , pp. 315-322
    • Pontón, P.I.1    D'Almeida, J.R.2    Marinkovic, B.A.3    Savić, S.M.4    Mancic, L.5    Rey, N.A.6    Morgado, E.7    Rizzo, F.C.8
  • 103
    • 84890045049 scopus 로고    scopus 로고
    • Preparation and characterization of montmorillonite modified with 3-aminopropyltriethoxysilane
    • Bertuoli, P.T.; Piazza, D.; Scienza, L.C.; Zattera, A.J. Preparation and characterization of montmorillonite modified with 3-aminopropyltriethoxysilane. Appl. Clay Sci. 2014, 87, 46-51.
    • (2014) Appl. Clay Sci. , vol.87 , pp. 46-51
    • Bertuoli, P.T.1    Piazza, D.2    Scienza, L.C.3    Zattera, A.J.4
  • 104
    • 84907093922 scopus 로고    scopus 로고
    • Chapter 11.2.2-porous ceramic materials
    • 2nd ed.; Somiya, S., Ed.; Academic Press: Oxford, UK
    • Ohji, T. Chapter 11.2.2-Porous ceramic materials. In Handbook of Advanced Ceramics, 2nd ed.; Somiya, S., Ed.; Academic Press: Oxford, UK, 2013; pp. 1131-1148.
    • (2013) Handbook of Advanced Ceramics , pp. 1131-1148
    • Ohji, T.1
  • 105
    • 84878343578 scopus 로고    scopus 로고
    • Functionalized ceramics for biomedical, biotechnological and environmental applications
    • Treccani, L.; Yvonne Klein, T.; Meder, F.; Pardun, K.; Rezwan, K. Functionalized ceramics for biomedical, biotechnological and environmental applications. Acta Biomater. 2013, 9, 7115-7150.
    • (2013) Acta Biomater. , vol.9 , pp. 7115-7150
    • Treccani, L.1    Yvonne Klein, T.2    Meder, F.3    Pardun, K.4    Rezwan, K.5
  • 109
    • 84856600312 scopus 로고    scopus 로고
    • Horseradish peroxidase immobilized on the silane-modified ceramics for the catalytic oxidation of simulated oily water
    • Wang, W.; Li, Z.; Liu, W.; Wu, J. Horseradish peroxidase immobilized on the silane-modified ceramics for the catalytic oxidation of simulated oily water. Sep. Purif. Technol. 2012, 89, 206-211.
    • (2012) Sep. Purif. Technol. , vol.89 , pp. 206-211
    • Wang, W.1    Li, Z.2    Liu, W.3    Wu, J.4
  • 111
    • 0030531482 scopus 로고    scopus 로고
    • Surface chemistry of titania (anatase) and titania-supported catalysts
    • Hadjiivanov, K.I.; Klissurski, D.G. Surface chemistry of titania (anatase) and titania-supported catalysts. Chem. Soc. Rev. 1996, 25, 61-69.
    • (1996) Chem. Soc. Rev. , vol.25 , pp. 61-69
    • Hadjiivanov, K.I.1    Klissurski, D.G.2
  • 112
    • 12844258903 scopus 로고    scopus 로고
    • Applying the taguchi method to the optimization for the synthesis of tio2 nanoparticles by hydrolysis of teot in micelles
    • Kim, K.D.; Kim, S.H.; Kim, H.T. Applying the taguchi method to the optimization for the synthesis of tio2 nanoparticles by hydrolysis of teot in micelles. Colloids Surf. Physicochem. Eng. Asp. 2005, 254, 99-105.
    • (2005) Colloids Surf. Physicochem. Eng. Asp. , vol.254 , pp. 99-105
    • Kim, K.D.1    Kim, S.H.2    Kim, H.T.3
  • 113
    • 0037459931 scopus 로고    scopus 로고
    • Synthesis of photocatalytic tio2 nanoparticles: Optimization of the preparation conditions
    • Bessekhouad, Y.; Robert, D.; Weber, J.V. Synthesis of photocatalytic tio2 nanoparticles: Optimization of the preparation conditions. J. Photochem. Photobiol. A Chem. 2003, 157, 47-53.
    • (2003) J. Photochem. Photobiol. A Chem. , vol.157 , pp. 47-53
    • Bessekhouad, Y.1    Robert, D.2    Weber, J.V.3
  • 115
    • 0000054345 scopus 로고
    • Titania-silica mixed oxides. I. Influence of sol-gel and drying conditions on structural properties
    • Dutoit, D.C.M.; Schneider, M.; Baiker, A. Titania-silica mixed oxides. I. Influence of sol-gel and drying conditions on structural properties. J. Catal. 1995, 153, 165-176.
    • (1995) J. Catal. , vol.153 , pp. 165-176
    • Dutoit, D.C.M.1    Schneider, M.2    Baiker, A.3
  • 116
    • 34547486889 scopus 로고    scopus 로고
    • Titanium dioxide nanomaterials: Synthesis, properties, modifications and applications
    • Chen, X.; Mao, S.S. Titanium dioxide nanomaterials: Synthesis, properties, modifications and applications. Chem. Rev. 2007, 107, 2891-2959.
    • (2007) Chem. Rev. , vol.107 , pp. 2891-2959
    • Chen, X.1    Mao, S.S.2
  • 118
    • 0028317369 scopus 로고
    • New materials for biotechnology: Chromatographic stationary phases based on zirconia
    • Nawrocki, J.; Dunlap, C.J.; Carr, P.W.; Blackwell, J.A. New materials for biotechnology: Chromatographic stationary phases based on zirconia. Biotechnol. Prog. 1994, 10, 561-573.
    • (1994) Biotechnol. Prog. , vol.10 , pp. 561-573
    • Nawrocki, J.1    Dunlap, C.J.2    Carr, P.W.3    Blackwell, J.A.4
  • 119
    • 34249077182 scopus 로고    scopus 로고
    • Immobilization of α-amylase on zirconia: A heterogeneous biocatalyst for starch hydrolysis
    • Reshmi, R.; Sanjay, G.; Sugunan, S. Immobilization of α-amylase on zirconia: A heterogeneous biocatalyst for starch hydrolysis. Catal. Commun. 2007, 8, 393-399.
    • (2007) Catal. Commun. , vol.8 , pp. 393-399
    • Reshmi, R.1    Sanjay, G.2    Sugunan, S.3
  • 120
    • 0347395459 scopus 로고
    • Catalytic aluminas i. Surface chemistry of eta and gamma alumina
    • Maciver, D.S.; Tobin, H.H.; Barth, R.T. Catalytic aluminas i. Surface chemistry of eta and gamma alumina. J. Catal. 1963, 2, 485-497.
    • (1963) J. Catal. , vol.2 , pp. 485-497
    • MacIver, D.S.1    Tobin, H.H.2    Barth, R.T.3
  • 121
    • 0000516663 scopus 로고
    • Conditions for the formation of bayerite and gibbsite
    • McHardy, W.; Thomson, A. Conditions for the formation of bayerite and gibbsite. Mineral. Mag. 1971, 38, 358-368.
    • (1971) Mineral. Mag. , vol.38 , pp. 358-368
    • McHardy, W.1    Thomson, A.2
  • 122
    • 84885637380 scopus 로고    scopus 로고
    • Structural models of activated γ-alumina surfaces revisited: Thermodynamics, nmr and ir spectroscopies from ab initio calculations
    • Ferreira, A.R.; Küçükbenli, E.; de Gironcoli, S.; Souza, W.F.; Chiaro, S.S.X.; Konstantinova, E.; Leitão, A.A. Structural models of activated γ-alumina surfaces revisited: Thermodynamics, nmr and ir spectroscopies from ab initio calculations. Chem. Phys. 2013, 423, 62-72.
    • (2013) Chem. Phys. , vol.423 , pp. 62-72
    • Ferreira, A.R.1    Küçükbenli, E.2    De Gironcoli, S.3    Souza, W.F.4    Chiaro, S.S.X.5    Konstantinova, E.6    Leitão, A.A.7
  • 123
    • 41649118198 scopus 로고    scopus 로고
    • Study on the activity and stability of urease immobilized onto nanoporous alumina membranes
    • Yang, Z.; Si, S.; Zhang, C. Study on the activity and stability of urease immobilized onto nanoporous alumina membranes. Microporous Mesoporous Mater. 2008, 111, 359-366.
    • (2008) Microporous Mesoporous Mater. , vol.111 , pp. 359-366
    • Yang, Z.1    Si, S.2    Zhang, C.3
  • 124
    • 78650721011 scopus 로고    scopus 로고
    • Adsorption onto alumina and stabilization of cysteine proteinases from crude extract of solanum granuloso-leprosum fruits
    • Vallés, D.; Furtado, S.; Villadóniga, C.; Cantera, A.M.B. Adsorption onto alumina and stabilization of cysteine proteinases from crude extract of solanum granuloso-leprosum fruits. Process Biochem. 2011, 46, 592-598.
    • (2011) Process Biochem. , vol.46 , pp. 592-598
    • Vallés, D.1    Furtado, S.2    Villadóniga, C.3    Cantera, A.M.B.4
  • 126
    • 40749098986 scopus 로고    scopus 로고
    • Modification of magnetite nanoparticles via surface-initiated atom transfer radical polymerization (atrp)
    • Zhou, Y.; Wang, S.; Ding, B.; Yang, Z. Modification of magnetite nanoparticles via surface-initiated atom transfer radical polymerization (atrp). Chem. Eng. J. 2008, 138, 578-585.
    • (2008) Chem. Eng. J. , vol.138 , pp. 578-585
    • Zhou, Y.1    Wang, S.2    Ding, B.3    Yang, Z.4
  • 127
    • 0346789811 scopus 로고    scopus 로고
    • Synthesis of magnetite nanoparticles by precipitation with forced mixing
    • Zhu, Y.; Wu, Q. Synthesis of magnetite nanoparticles by precipitation with forced mixing. J. Nanopart. Res. 1999, 1, 393-396.
    • (1999) J. Nanopart. Res. , vol.1 , pp. 393-396
    • Zhu, Y.1    Wu, Q.2
  • 128
    • 84859090203 scopus 로고    scopus 로고
    • Preparation and magnetic properties of nano size nickel ferrite particles using hydrothermal method
    • Nejati, K.; Zabihi, R. Preparation and magnetic properties of nano size nickel ferrite particles using hydrothermal method. Chem. Cent. J. 2012, 6, doi:10.1186/1752-153X-6-23.
    • (2012) Chem. Cent. J. , vol.6
    • Nejati, K.1    Zabihi, R.2
  • 129
    • 84861906936 scopus 로고    scopus 로고
    • Development of an amperometric hydrogen peroxide biosensor based on the immobilization of horseradish peroxidase onto nickel ferrite nanoparticle-chitosan composite
    • Yalçiner, F.; Çevik, E.; Şenel, M.; Baykal, A. Development of an amperometric hydrogen peroxide biosensor based on the immobilization of horseradish peroxidase onto nickel ferrite nanoparticle-chitosan composite. Nano-Micro Lett. 2011, 3, 91-98.
    • (2011) Nano-Micro Lett. , vol.3 , pp. 91-98
    • Yalçiner, F.1    Çevik, E.2    Şenel, M.3    Baykal, A.4
  • 130
    • 33749598820 scopus 로고    scopus 로고
    • Synthesis and magnetic properties of cobalt ferrite (cofe2o4) nanoparticles prepared by wet chemical route
    • Maaz, K.; Mumtaz, A.; Hasanain, S.K.; Ceylan, A. Synthesis and magnetic properties of cobalt ferrite (cofe2o4) nanoparticles prepared by wet chemical route. J. Magn. Magn. Mater. 2007, 308, 289-295.
    • (2007) J. Magn. Magn. Mater. , vol.308 , pp. 289-295
    • Maaz, K.1    Mumtaz, A.2    Hasanain, S.K.3    Ceylan, A.4
  • 131
    • 0001877084 scopus 로고
    • Magnetic supports for immobilized enzymes and bioaffinity adsorbents
    • Halling, P.J.; Dunnill, P. Magnetic supports for immobilized enzymes and bioaffinity adsorbents. Enzym. Microb. Technol. 1980, 2, 2-10.
    • (1980) Enzym. Microb. Technol. , vol.2 , pp. 2-10
    • Halling, P.J.1    Dunnill, P.2
  • 133
    • 84894572804 scopus 로고    scopus 로고
    • Novel hybrid materials on the basis of nanostructured tin dioxide and a lipase from rhizopus delemar with improved enantioselectivity
    • Guncheva, M.; Dimitrov, M.; Napoly, F.; Draye, M.; Andrioletti, B. Novel hybrid materials on the basis of nanostructured tin dioxide and a lipase from rhizopus delemar with improved enantioselectivity. J. Mol. Catal. B Enzym. 2014, 102, 72-80.
    • (2014) J. Mol. Catal. B Enzym. , vol.102 , pp. 72-80
    • Guncheva, M.1    Dimitrov, M.2    Napoly, F.3    Draye, M.4    Andrioletti, B.5
  • 134
    • 77957851695 scopus 로고    scopus 로고
    • Protein immobilization at gold-thiol surfaces and potential for biosensing
    • Frasconi, M.; Mazzei, F.; Ferri, T. Protein immobilization at gold-thiol surfaces and potential for biosensing. Anal. Bioanal. Chem. 2010, 398, 1545-1564.
    • (2010) Anal. Bioanal. Chem. , vol.398 , pp. 1545-1564
    • Frasconi, M.1    Mazzei, F.2    Ferri, T.3
  • 135
    • 84858032717 scopus 로고    scopus 로고
    • Functional self-assembled monolayers (sams) of organic compounds on gold nanoparticles
    • Jadhav, S.A. Functional self-assembled monolayers (sams) of organic compounds on gold nanoparticles. J. Mater. Chem. 2012, 22, 5894-5899.
    • (2012) J. Mater. Chem. , vol.22 , pp. 5894-5899
    • Jadhav, S.A.1
  • 136
    • 0346753829 scopus 로고    scopus 로고
    • Direct attachment of fibronectin to tresyl chloride-activated titanium
    • Hayakawa, T.; Yoshinari, M.; Nemoto, K. Direct attachment of fibronectin to tresyl chloride-activated titanium. J. Biomed. Mater. Res. Part A 2003, 67, 684-688.
    • (2003) J. Biomed. Mater. Res. Part A , vol.67 , pp. 684-688
    • Hayakawa, T.1    Yoshinari, M.2    Nemoto, K.3
  • 138
    • 0642307922 scopus 로고
    • Puzzles and paradoxes in protein adsorption
    • Ramsden, J.J. Puzzles and paradoxes in protein adsorption. Chem. Soc. Rev. 1995, 24, 73-78.
    • (1995) Chem. Soc. Rev. , vol.24 , pp. 73-78
    • Ramsden, J.J.1
  • 139
    • 13444301110 scopus 로고    scopus 로고
    • Cholinesterase immobilisation on the surface of screen-printed electrodes based on concanavalin a affinity
    • Bucur, B.; Danet, A.F.; Marty, J.L. Cholinesterase immobilisation on the surface of screen-printed electrodes based on concanavalin a affinity. Anal. Chim. Acta 2005, 530, 1-6.
    • (2005) Anal. Chim. Acta , vol.530 , pp. 1-6
    • Bucur, B.1    Danet, A.F.2    Marty, J.L.3
  • 140
    • 0023677621 scopus 로고
    • Affinity immobilization
    • Mattiasson, B. Affinity immobilization. Methods Enzymol. 1988, 137, 647-656.
    • (1988) Methods Enzymol. , vol.137 , pp. 647-656
    • Mattiasson, B.1
  • 141
    • 84907103041 scopus 로고    scopus 로고
    • Irreversible affinity immobilization of lentil seedling amine oxidase with activity retention
    • Sollai, F.; Noli, B.; Floris, G.; Sanjust, E. Irreversible affinity immobilization of lentil seedling amine oxidase with activity retention. Environ. Eng. Manag. J. 2007, 6, 31-35.
    • (2007) Environ. Eng. Manag. J. , vol.6 , pp. 31-35
    • Sollai, F.1    Noli, B.2    Floris, G.3    Sanjust, E.4
  • 142
    • 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. Enzym. Microb. Technol. 2009, 45, 405-418.
    • (2009) Enzym. Microb. Technol. , vol.45 , pp. 405-418
    • Fernandez-Lafuente, R.1
  • 145
    • 0035470561 scopus 로고    scopus 로고
    • Polyhedral oligomeric silsesquioxane (poss) polymers and copolymers: A review
    • Li, G.; Wang, L.; Ni, H.; Pittman, C., Jr. Polyhedral oligomeric silsesquioxane (poss) polymers and copolymers: A review. J. Inorg. Organomet. Polym. 2001, 11, 123-154.
    • (2001) J. Inorg. Organomet. Polym. , vol.11 , pp. 123-154
    • Li, G.1    Wang, L.2    Ni, H.3    Pittman, C.4
  • 146
    • 0141869046 scopus 로고    scopus 로고
    • Novel route to periodic mesoporous aminosilicas, pmas: Ammonolysis of periodic mesoporous organosilicas
    • Asefa, T.; Kruk, M.; Coombs, N.; Grondey, H.; MacLachlan, M.J.; Jaroniec, M.; Ozin, G.A. Novel route to periodic mesoporous aminosilicas, pmas: Ammonolysis of periodic mesoporous organosilicas. J. Am. Chem. Soc. 2003, 125, 11662-11673.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11662-11673
    • Asefa, T.1    Kruk, M.2    Coombs, N.3    Grondey, H.4    MacLachlan, M.J.5    Jaroniec, M.6    Ozin, G.A.7
  • 147
    • 57349153240 scopus 로고    scopus 로고
    • Attachment of 3-(aminopropyl)triethoxysilane on silicon oxide surfaces: Dependence on solution temperature
    • Pasternack, R.M.; Rivillon Amy, S.; Chabal, Y.J. Attachment of 3-(aminopropyl)triethoxysilane on silicon oxide surfaces: Dependence on solution temperature. Langmuir 2008, 24, 12963-12971.
    • (2008) Langmuir , vol.24 , pp. 12963-12971
    • Pasternack, R.M.1    Rivillon Amy, S.2    Chabal, Y.J.3
  • 148
  • 149
    • 84887031075 scopus 로고    scopus 로고
    • Gradual hydrophobic surface functionalization of dry silica aerogels by reaction with silane precursors dissolved in supercritical carbon dioxide
    • Sanz-Moral, L.M.; Rueda, M.; Nieto, A.; Novak, Z.; Knez, Ž.; Martín, Á. Gradual hydrophobic surface functionalization of dry silica aerogels by reaction with silane precursors dissolved in supercritical carbon dioxide. J. Supercrit. Fluids 2013, 84, 74-79.
    • (2013) J. Supercrit. Fluids , vol.84 , pp. 74-79
    • Sanz-Moral, L.M.1    Rueda, M.2    Nieto, A.3    Novak, Z.4    Knez Ž.5    Martín Á.6
  • 150
    • 1642391614 scopus 로고    scopus 로고
    • Toward single-site, immobilized molecular catalysts: Site-isolated ti ethylene polymerization catalysts supported on porous silica
    • McKittrick, M.W.; Jones, C.W. Toward single-site, immobilized molecular catalysts: Site-isolated ti ethylene polymerization catalysts supported on porous silica. J. Am. Chem. Soc. 2004, 126, 3052-3053.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3052-3053
    • McKittrick, M.W.1    Jones, C.W.2
  • 152
    • 0016247471 scopus 로고
    • [3] covalent linkage of functional groups, ligands, and proteins to polyacrylamide beads
    • Inman, J.K. [3] covalent linkage of functional groups, ligands, and proteins to polyacrylamide beads. Methods Enzymol. 1974, 34, 30-58.
    • (1974) Methods Enzymol. , vol.34 , pp. 30-58
    • Inman, J.K.1
  • 153
    • 0014772602 scopus 로고
    • Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides
    • Kaiser, E.; Colescott, R.L.; Bossinger, C.D.; Cook, P.I. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal. Biochem. 1970, 34, 595-598.
    • (1970) Anal. Biochem. , vol.34 , pp. 595-598
    • Kaiser, E.1    Colescott, R.L.2    Bossinger, C.D.3    Cook, P.I.4
  • 154
    • 84861611274 scopus 로고    scopus 로고
    • Synthesis and characterization of chitosan-homocysteine thiolactone as a mucoadhesive polymer
    • Juntapram, K.; Praphairaksit, N.; Siraleartmukul, K.; Muangsin, N. Synthesis and characterization of chitosan-homocysteine thiolactone as a mucoadhesive polymer. Carbohydr. Polym. 2012, 87, 2399-2408.
    • (2012) Carbohydr. Polym. , vol.87 , pp. 2399-2408
    • Juntapram, K.1    Praphairaksit, N.2    Siraleartmukul, K.3    Muangsin, N.4
  • 155
    • 35748975643 scopus 로고    scopus 로고
    • 5, 10, 15, 20-tetrakis (4-sulfonato-phenyl) porphine-mn (iii) immobilized on imidazole-activated silica as a novel lignin-peroxidase-like biomimetic catalyst
    • Zucca, P.; Mocci, G.; Rescigno, A.; Sanjust, E. 5, 10, 15, 20-tetrakis (4-sulfonato-phenyl) porphine-mn (iii) immobilized on imidazole-activated silica as a novel lignin-peroxidase-like biomimetic catalyst. J. Mol. Catal. A Chem. 2007, 278, 220-227.
    • (2007) J. Mol. Catal. A Chem. , vol.278 , pp. 220-227
    • Zucca, P.1    Mocci, G.2    Rescigno, A.3    Sanjust, E.4
  • 156
    • 84871257700 scopus 로고    scopus 로고
    • Degradation of textile dyes using immobilized lignin peroxidase-like metalloporphines under mild experimental conditions
    • Zucca, P.; Rescigno, A.; Pintus, M.; Rinaldi, A.C.; Sanjust, E. Degradation of textile dyes using immobilized lignin peroxidase-like metalloporphines under mild experimental conditions. Chem. Cent. J. 2012, 6, 1-8.
    • (2012) Chem. Cent. J. , vol.6 , pp. 1-8
    • Zucca, P.1    Rescigno, A.2    Pintus, M.3    Rinaldi, A.C.4    Sanjust, E.5
  • 157
    • 77949277734 scopus 로고    scopus 로고
    • Is the bleaching of phenosafranine by hydrogen peroxide oxidation catalyzed by silica-supported 5, 10, 15, 20-tetrakis-(sulfonatophenyl) porphine-mn (iii) really biomimetic?
    • Zucca, P.; Vinci, C.; Rescigno, A.; Dumitriu, E.; Sanjust, E. Is the bleaching of phenosafranine by hydrogen peroxide oxidation catalyzed by silica-supported 5, 10, 15, 20-tetrakis-(sulfonatophenyl) porphine-mn (iii) really biomimetic? J. Mol. Catal. A Chem. 2010, 321, 27-33.
    • (2010) J. Mol. Catal. A Chem. , vol.321 , pp. 27-33
    • Zucca, P.1    Vinci, C.2    Rescigno, A.3    Dumitriu, E.4    Sanjust, E.5
  • 158
    • 44449151995 scopus 로고    scopus 로고
    • Degradation of alizarin red s under mild experimental conditions by immobilized 5, 10, 15, 20-tetrakis (4-sulfonatophenyl) porphine-mn (iii) as a biomimetic peroxidase-like catalyst
    • Zucca, P.; Vinci, C.; Sollai, F.; Rescigno, A.; Sanjust, E. Degradation of alizarin red s under mild experimental conditions by immobilized 5, 10, 15, 20-tetrakis (4-sulfonatophenyl) porphine-mn (iii) as a biomimetic peroxidase-like catalyst. J. Mol. Catal. A Chem. 2008, 288, 97-102.
    • (2008) J. Mol. Catal. A Chem. , vol.288 , pp. 97-102
    • Zucca, P.1    Vinci, C.2    Sollai, F.3    Rescigno, A.4    Sanjust, E.5
  • 159
    • 1042289443 scopus 로고    scopus 로고
    • Stability analysis of bacillus stearothermophilus l1 lipase immobilized on surface-modified silica gels
    • Hwang, S.; Lee, K.-T.; Park, J.-W.; Min, B.-R.; Haam, S.; Ahn, I.-S.; Jung, J.-K. Stability analysis of bacillus stearothermophilus l1 lipase immobilized on surface-modified silica gels. Biochem. Eng. J. 2004, 17, 85-90.
    • (2004) Biochem. Eng. J. , vol.17 , pp. 85-90
    • Hwang, S.1    Lee, K.-T.2    Park, J.-W.3    Min, B.-R.4    Haam, S.5    Ahn, I.-S.6    Jung, J.-K.7
  • 160
    • 84873411955 scopus 로고    scopus 로고
    • Enhanced stability of catalase covalently immobilized on functionalized titania submicrospheres
    • Wu, H.; Liang, Y.; Shi, J.; Wang, X.; Yang, D.; Jiang, Z. Enhanced stability of catalase covalently immobilized on functionalized titania submicrospheres. Mater. Sci. Eng. C 2013, 33, 1438-1445.
    • (2013) Mater. Sci. Eng. C , vol.33 , pp. 1438-1445
    • Wu, H.1    Liang, Y.2    Shi, J.3    Wang, X.4    Yang, D.5    Jiang, Z.6
  • 161
    • 84877586092 scopus 로고    scopus 로고
    • Catechol modification and covalent immobilization of catalase on titania submicrospheres
    • Wu, H.; Zhang, C.; Liang, Y.; Shi, J.; Wang, X.; Jiang, Z. Catechol modification and covalent immobilization of catalase on titania submicrospheres. J. Mol. Catal. B Enzym. 2013, 92, 44-50.
    • (2013) J. Mol. Catal. B Enzym. , vol.92 , pp. 44-50
    • Wu, H.1    Zhang, C.2    Liang, Y.3    Shi, J.4    Wang, X.5    Jiang, Z.6
  • 163
    • 0037173287 scopus 로고    scopus 로고
    • Self-assembly of carboxyalkylphosphonic acids on metal oxide powders
    • Pawsey, S.; Yach, K.; Reven, L. Self-assembly of carboxyalkylphosphonic acids on metal oxide powders. Langmuir 2002, 18, 5205-5212.
    • (2002) Langmuir , vol.18 , pp. 5205-5212
    • Pawsey, S.1    Yach, K.2    Reven, L.3
  • 164
    • 0024375411 scopus 로고
    • Alumina-phosphate complexes for immobilization of biomolecules
    • Coletti-Previero, M.A.; Previero, A. Alumina-phosphate complexes for immobilization of biomolecules. Anal. Biochem. 1989, 180, 1-10.
    • (1989) Anal. Biochem. , vol.180 , pp. 1-10
    • Coletti-Previero, M.A.1    Previero, A.2
  • 165
    • 0032923637 scopus 로고    scopus 로고
    • Purification of monoclonal antibodies from cell culture supernatants using a modified zirconia based cation-exchange support
    • Clausen, A.M.; Subramanian, A.; Carr, P.W. Purification of monoclonal antibodies from cell culture supernatants using a modified zirconia based cation-exchange support. J. Chromatogr. 1999, 831, 63-72.
    • (1999) J. Chromatogr. , vol.831 , pp. 63-72
    • Clausen, A.M.1    Subramanian, A.2    Carr, P.W.3
  • 166
    • 0017248834 scopus 로고
    • Functional groups on enzymes suitable for binding to matrices
    • Klaus, M., Ed.; Academic Press: Waltham, MA, USA
    • Srere, P.A.; Uyeda, K. Functional groups on enzymes suitable for binding to matrices. In Methods in Enzymology; Klaus, M., Ed.; Academic Press: Waltham, MA, USA, 1976; Volume 44, pp. 11-19.
    • (1976) Methods in Enzymology , vol.44 , pp. 11-19
    • Srere, P.A.1    Uyeda, K.2
  • 168
    • 67650214721 scopus 로고    scopus 로고
    • Immobilization-stabilization of the lipase from thermomyces lanuginosus: Critical role of chemical amination
    • Rodrigues, R.C.; Godoy, C.A.; Volpato, G.; Ayub, M.A.Z.; Fernandez-Lafuente, R.; Guisan, J.M. Immobilization-stabilization of the lipase from thermomyces lanuginosus: Critical role of chemical amination. Process Biochem. 2009, 44, 963-968.
    • (2009) Process Biochem. , vol.44 , pp. 963-968
    • Rodrigues, R.C.1    Godoy, C.A.2    Volpato, G.3    Ayub, M.A.Z.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 170
    • 0020174792 scopus 로고
    • A new approach (cyano-transfer) for cyanogen bromide activation of sepharose at neutral ph, which yields activated resins, free of interfering nitrogen derivatives
    • Kohn, J.; Wilchek, M. A new approach (cyano-transfer) for cyanogen bromide activation of sepharose at neutral ph, which yields activated resins, free of interfering nitrogen derivatives. Biochem. Biophys. Res. Commun. 1982, 107, 878-884.
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 878-884
    • Kohn, J.1    Wilchek, M.2
  • 171
    • 0019605122 scopus 로고
    • Procedures for the analysis of cyanogen bromide-activated sepharose or sephadex by quantitative determination of cyanate esters and imidocarbonates
    • Kohn, J.; Wilchek, M. Procedures for the analysis of cyanogen bromide-activated sepharose or sephadex by quantitative determination of cyanate esters and imidocarbonates. Anal. Biochem. 1981, 115, 375-382.
    • (1981) Anal. Biochem. , vol.115 , pp. 375-382
    • Kohn, J.1    Wilchek, M.2
  • 172
    • 0023087636 scopus 로고
    • A survey of enzyme coupling techniques
    • Academic Press: Waltham, MA, USA
    • Scouten, W.H. A survey of enzyme coupling techniques. In Methods in Enzymology; Academic Press: Waltham, MA, USA, 1987; Volume 135, pp. 30-65.
    • (1987) Methods in Enzymology , vol.135 , pp. 30-65
    • Scouten, W.H.1
  • 173
    • 0020125711 scopus 로고
    • Mechanism of activation of sepharose and sephadex by cyanogen bromide
    • Kohn, J.; Wilchek, M. Mechanism of activation of sepharose and sephadex by cyanogen bromide. Enzym. Microb. Technol. 1982, 4, 161-163.
    • (1982) Enzym. Microb. Technol. , vol.4 , pp. 161-163
    • Kohn, J.1    Wilchek, M.2
  • 174
    • 0000148546 scopus 로고
    • Structure of a soluble super active insulin is revealed by the nature of the complex between cyanogen bromide activated sepharose and amines (n substituted isoureas/n1 n2 disubstituted guanidines/insulin sepharose/insulin insensitivity/super active peptide hormones)
    • Wilchek, M.; Oka, T.; Topper, Y.J. Structure of a soluble super active insulin is revealed by the nature of the complex between cyanogen bromide activated sepharose and amines (n substituted isoureas/n1 n2 disubstituted guanidines/insulin sepharose/insulin insensitivity/super active peptide hormones). Proc. Natl. Acad. Sci. USA 1975, 72, 1055-1058.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1055-1058
    • Wilchek, M.1    Oka, T.2    Topper, Y.J.3
  • 175
    • 0020838007 scopus 로고
    • High-performance liquid affinity chromatography on silica-bound alcohol dehydrogenase
    • Nilsson, K.; Larsson, P.-O. High-performance liquid affinity chromatography on silica-bound alcohol dehydrogenase. Anal. Biochem. 1983, 134, 60-72.
    • (1983) Anal. Biochem. , vol.134 , pp. 60-72
    • Nilsson, K.1    Larsson, P.-O.2
  • 176
    • 0017070145 scopus 로고
    • Immobilization of enzymes by covalent binding to amine supports via cyanogen bromide activation
    • Schnapp, J.; Shalitin, Y. Immobilization of enzymes by covalent binding to amine supports via cyanogen bromide activation. Biochem. Biophys. Res. Commun. 1976, 70, 8-14.
    • (1976) Biochem. Biophys. Res. Commun. , vol.70 , pp. 8-14
    • Schnapp, J.1    Shalitin, Y.2
  • 177
    • 0000374977 scopus 로고
    • 1-cyano-4-dimethylamino pyridinium tetrafluoroborate as a cyanylating agent for the covalent attachment of ligand to polysaccharide resins
    • Kohn, J.; Wilchek, M. 1-cyano-4-dimethylamino pyridinium tetrafluoroborate as a cyanylating agent for the covalent attachment of ligand to polysaccharide resins. FEBS Lett. 1983, 154, 209-210.
    • (1983) FEBS Lett. , vol.154 , pp. 209-210
    • Kohn, J.1    Wilchek, M.2
  • 179
    • 77957050418 scopus 로고    scopus 로고
    • Covalent immobilization of crude and partially-purified upases onto inorganic supports: Stability and hyperactivation
    • Alcántara, A.R.; Borreguero, I.; López-Belmonte, M.T.; Sinisterra, J.V. Covalent immobilization of crude and partially-purified upases onto inorganic supports: Stability and hyperactivation. Prog. Biotechnol. 1998, 15, 571-576.
    • (1998) Prog. Biotechnol. , vol.15 , pp. 571-576
    • Alcántara, A.R.1    Borreguero, I.2    López-Belmonte, M.T.3    Sinisterra, J.V.4
  • 180
    • 0028525055 scopus 로고
    • Immobilization of lipase from candida cylindracea on inorganic supports
    • Moreno, J.M.; Sinisterra, J.V. Immobilization of lipase from candida cylindracea on inorganic supports. J. Mol. Catal. 1994, 93, 357-369.
    • (1994) J. Mol. Catal. , vol.93 , pp. 357-369
    • Moreno, J.M.1    Sinisterra, J.V.2
  • 181
    • 0023068986 scopus 로고
    • Tresyl chloride-activated supports for enzyme immobilization
    • Klaus, M., Ed.; Academic Press: Waltham, MA, USA
    • Nilsson, K.; Mosbach, K. Tresyl chloride-activated supports for enzyme immobilization. In Methods in Enzymology; Klaus, M., Ed.; Academic Press: Waltham, MA, USA, 1987; Volume 135, pp. 65-78.
    • (1987) Methods in Enzymology , vol.135 , pp. 65-78
    • Nilsson, K.1    Mosbach, K.2
  • 182
    • 0001030611 scopus 로고
    • Sulfonate leaving groups, structure and reactivity. 2,2,2-trifluoroethanesulfonate
    • Crossland, R.; Wells, W.; Shiner, V., Jr. Sulfonate leaving groups, structure and reactivity. 2,2,2-Trifluoroethanesulfonate. J. Am. Chem. Soc. 1971, 93, 4217-4219.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 4217-4219
    • Crossland, R.1    Wells, W.2    Shiner, V.3
  • 183
    • 0023062464 scopus 로고
    • Colored sulfonyl chloride as an activating agent for hydroxylic matrices
    • Klaus, M., Ed.; Academic Press: Waltham, MA, USA
    • Scouten, W.H.; van den Tweel, W.; Kranenburg, H.; Dekker, M. Colored sulfonyl chloride as an activating agent for hydroxylic matrices. In Methods in Enzymology; Klaus, M., Ed.; Academic Press: Waltham, MA, USA, 1987; Volume 135, pp. 79-84.
    • (1987) Methods in Enzymology , vol.135 , pp. 79-84
    • Scouten, W.H.1    Van Den-Tweel, W.2    Kranenburg, H.3    Dekker, M.4
  • 185
    • 54949118377 scopus 로고    scopus 로고
    • A comparative study on immobilization of urease on different matrices
    • Selvamurugan, C.; Lavanya, A.; Sivasankar, B. A comparative study on immobilization of urease on different matrices. J. Sci. Ind. Res. 2007, 66, 655-659.
    • (2007) J. Sci. Ind. Res. , vol.66 , pp. 655-659
    • Selvamurugan, C.1    Lavanya, A.2    Sivasankar, B.3
  • 186
    • 51249186176 scopus 로고
    • P-nitrophenylcyanate: An efficient, convenient, and nonhazardous substitute for cyanogen bromide as an activating agent for sepharose
    • Kohn, J.; Lenger, R.; Wilchek, M. P-nitrophenylcyanate: An efficient, convenient, and nonhazardous substitute for cyanogen bromide as an activating agent for sepharose. Appl. Biochem. Biotechnol. 1983, 8, 227-235.
    • (1983) Appl. Biochem. Biotechnol. , vol.8 , pp. 227-235
    • Kohn, J.1    Lenger, R.2    Wilchek, M.3
  • 187
    • 0023076433 scopus 로고
    • Immobilization of proteins and ligands using chlorocarbonates
    • Klaus, M., Ed.; Academic Press: Waltham, MA, USA
    • Miron, T.; Wilchek, M. Immobilization of proteins and ligands using chlorocarbonates. In Methods in Enzymology; Klaus, M., Ed.; Academic Press: Waltham, MA, USA, 1987; Volume 135, pp. 84-90.
    • (1987) Methods in Enzymology , vol.135 , pp. 84-90
    • Miron, T.1    Wilchek, M.2
  • 188
    • 0002905967 scopus 로고    scopus 로고
    • Immobilization of proteins on thionyl chloride-activated controlled-pore glass
    • Bickerstaff, G., Ed.; Humana Press: New York, NY, USA
    • Janolino, V.; Swaisgood, H. Immobilization of proteins on thionyl chloride-activated controlled-pore glass. In Immobilization of Enzymes and Cells; Bickerstaff, G., Ed.; Humana Press: New York, NY, USA, 1997; Volume 1, pp. 21-26.
    • (1997) Immobilization of Enzymes and Cells , vol.1 , pp. 21-26
    • Janolino, V.1    Swaisgood, H.2
  • 189
    • 34249696995 scopus 로고    scopus 로고
    • Covalent immobilization of trypsin on to siliceous mesostructured cellular foams to obtain effective biocatalysts
    • Jarze{ogonek}bski, A.B.; Szymańska, K.; Bryjak, J.; Mrowiec-Białoń, J. Covalent immobilization of trypsin on to siliceous mesostructured cellular foams to obtain effective biocatalysts. Catal. Today 2007, 124, 2-10.
    • (2007) Catal. Today , vol.124 , pp. 2-10
    • Jarzebski, A.B.1    Szymańska, K.2    Bryjak, J.3    Mrowiec-Białoń, J.4
  • 190
    • 84890047134 scopus 로고    scopus 로고
    • Glutaraldehyde in bio-catalysts design: A useful crosslinker and a versatile tool in enzyme immobilization
    • Barbosa, O.; Ortiz, C.; Berenguer-Murcia, A.; Torres, R.; Rodrigues, R.C.; Fernandez-Lafuente, R. Glutaraldehyde in bio-catalysts design: A useful crosslinker and a versatile tool in enzyme immobilization. RSC Adv. 2014, 4, 1583-1600.
    • (2014) RSC Adv. , vol.4 , pp. 1583-1600
    • Barbosa, O.1    Ortiz, C.2    Berenguer-Murcia, A.3    Torres, R.4    Rodrigues, R.C.5    Fernandez-Lafuente, R.6
  • 191
    • 8444230519 scopus 로고    scopus 로고
    • Glutaraldehyde: Behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking
    • Migneault, I.; Dartiguenave, C.; Bertrand, M.J.; Waldron, K.C. Glutaraldehyde: Behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking. Bio Techniques 2004, 37, 790-802.
    • (2004) Bio Techniques , vol.37 , pp. 790-802
    • Migneault, I.1    Dartiguenave, C.2    Bertrand, M.J.3    Waldron, K.C.4
  • 192
    • 84861899828 scopus 로고    scopus 로고
    • Versatility of glutaraldehyde to immobilize lipases: Effect of the immobilization protocol on the properties of lipase b from candida antarctica
    • Barbosa, O.; Torres, R.; Ortiz, C.; Fernandez-Lafuente, R. Versatility of glutaraldehyde to immobilize lipases: Effect of the immobilization protocol on the properties of lipase b from candida antarctica. Process Biochem. 2012, 47, 1220-1227.
    • (2012) Process Biochem. , vol.47 , pp. 1220-1227
    • Barbosa, O.1    Torres, R.2    Ortiz, C.3    Fernandez-Lafuente, R.4
  • 193
    • 0347297355 scopus 로고    scopus 로고
    • Influence of different silica derivatives in the immobilization and stabilization of a bacillus licheniformis protease (subtilisin carlsberg)
    • Ferreira, L.; Ramos, M.A.; Dordick, J.S.; Gil, M.H. Influence of different silica derivatives in the immobilization and stabilization of a bacillus licheniformis protease (subtilisin carlsberg). J. Mol. Catal. B Enzym. 2003, 21, 189-199.
    • (2003) J. Mol. Catal. B Enzym. , vol.21 , pp. 189-199
    • Ferreira, L.1    Ramos, M.A.2    Dordick, J.S.3    Gil, M.H.4
  • 194
    • 77649225940 scopus 로고    scopus 로고
    • Covalent anchoring of chloroperoxidase and glucose oxidase on the mesoporous molecular sieve sba-15
    • Jung, D.; Streb, C.; Hartmann, M. Covalent anchoring of chloroperoxidase and glucose oxidase on the mesoporous molecular sieve sba-15. Int. J. Mol. Sci. 2010, 11, 762-778.
    • (2010) Int. J. Mol. Sci. , vol.11 , pp. 762-778
    • Jung, D.1    Streb, C.2    Hartmann, M.3
  • 196
    • 55249126836 scopus 로고    scopus 로고
    • Covalent immobilization of proteins on carbon nanotubes using the cross-linker 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide-A critical assessment
    • Gao, Y.; Kyratzis, I. Covalent immobilization of proteins on carbon nanotubes using the cross-linker 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide-A critical assessment. Bioconjug. Chem. 2008, 19, 1945-1950.
    • (2008) Bioconjug. Chem. , vol.19 , pp. 1945-1950
    • Gao, Y.1    Kyratzis, I.2
  • 197
    • 0022512416 scopus 로고
    • Enhancement of n-hydroxysulfosuccinimide of water-soluble carbodiimide-mediated coupling reactions
    • Staros, J.V.; Wright, R.W.; Swingle, D.M. Enhancement of n-hydroxysulfosuccinimide of water-soluble carbodiimide-mediated coupling reactions. Anal. Biochem. 1986, 156, 220-222.
    • (1986) Anal. Biochem. , vol.156 , pp. 220-222
    • Staros, J.V.1    Wright, R.W.2    Swingle, D.M.3
  • 198
    • 0028281399 scopus 로고
    • A method for the high efficiency of water-soluble carbodiimide-mediated amidation
    • Sehgal, D.; Vijay, I.K. A method for the high efficiency of water-soluble carbodiimide-mediated amidation. Anal. Biochem. 1994, 218, 87-91.
    • (1994) Anal. Biochem. , vol.218 , pp. 87-91
    • Sehgal, D.1    Vijay, I.K.2
  • 199
    • 0020154559 scopus 로고
    • Radiation grafted polyethylene as carrier for protein immobilization-2. Covalent immobilization of antibodies against thyroxine
    • Müller-Schulte, D.; Horster, F.A. Radiation grafted polyethylene as carrier for protein immobilization-2. Covalent immobilization of antibodies against thyroxine. Polym. Bull. 1982, 7, 395-399.
    • (1982) Polym. Bull. , vol.7 , pp. 395-399
    • Müller-Schulte, D.1    Horster, F.A.2
  • 200
    • 84896897096 scopus 로고    scopus 로고
    • Covalent immobilization of porcine pancreatic lipase on carboxyl-activated magnetic nanoparticles: Characterization and application for enzymatic inhibition assays
    • Zhu, Y.T.; Ren, X.Y.; Liu, Y.M.; Wei, Y.; Qing, L.S.; Liao, X. Covalent immobilization of porcine pancreatic lipase on carboxyl-activated magnetic nanoparticles: Characterization and application for enzymatic inhibition assays. Mater. Sci. Eng. C 2014, 38, 278-285.
    • (2014) Mater. Sci. Eng. C , vol.38 , pp. 278-285
    • Zhu, Y.T.1    Ren, X.Y.2    Liu, Y.M.3    Wei, Y.4    Qing, L.S.5    Liao, X.6
  • 201
    • 84899483815 scopus 로고    scopus 로고
    • Immobilization of gamma globulins and polyclonal antibodies of class igg onto carbon-encapsulated iron nanoparticles functionalized with various surface linkers
    • Poplawska, M.; Bystrzejewski, M.; Grudziński, I.P.; Cywińska, M.A.; Ostapko, J.; Cieszanowski, A. Immobilization of gamma globulins and polyclonal antibodies of class igg onto carbon-encapsulated iron nanoparticles functionalized with various surface linkers. Carbon 2014, 74, 180-194.
    • (2014) Carbon , vol.74 , pp. 180-194
    • Poplawska, M.1    Bystrzejewski, M.2    Grudziński, I.P.3    Cywińska, M.A.4    Ostapko, J.5    Cieszanowski, A.6
  • 202
    • 78751604056 scopus 로고    scopus 로고
    • A versatile method for functionalizing surfaces with bioactive glycans
    • Cheng, F.; Shang, J.; Ratner, D.M. A versatile method for functionalizing surfaces with bioactive glycans. Bioconjug. Chem. 2010, 22, 50-57.
    • (2010) Bioconjug. Chem. , vol.22 , pp. 50-57
    • Cheng, F.1    Shang, J.2    Ratner, D.M.3
  • 203
    • 0030135376 scopus 로고    scopus 로고
    • Preparation of characterization of poly(ethylene glycol) vinyl sulfone
    • Morpurgo, M.; Veronese, F.M.; Kachensky, D.; Harris, J.M. Preparation of characterization of poly(ethylene glycol) vinyl sulfone. Bioconjug. Chem. 1996, 7, 363-368.
    • (1996) Bioconjug. Chem. , vol.7 , pp. 363-368
    • Morpurgo, M.1    Veronese, F.M.2    Kachensky, D.3    Harris, J.M.4
  • 205
    • 77956204999 scopus 로고    scopus 로고
    • Post-immobilization of modified macromolecular reagents using assembled penicillin acylase for microenvironmental regulation of nanopores and enhancement of enzyme stability
    • Zhou, C.; Zhu, S.; Wu, X.; Jiang, B.; Cen, T.; Shen, S. Post-immobilization of modified macromolecular reagents using assembled penicillin acylase for microenvironmental regulation of nanopores and enhancement of enzyme stability. Biotechnol. Bioprocess Eng. 2010, 15, 376-382.
    • (2010) Biotechnol. Bioprocess Eng. , vol.15 , pp. 376-382
    • Zhou, C.1    Zhu, S.2    Wu, X.3    Jiang, B.4    Cen, T.5    Shen, S.6
  • 206
    • 79957489784 scopus 로고    scopus 로고
    • Affinity covalent immobilization of glucoamylase onto ρ-benzoquinone activated alginate beads: I. Beads preparation and characterization
    • Eldin, M.S.M.; Seuror, E.I.; Nasr, M.A.; El-Aassar, M.R.; Tieama, H.A. Affinity covalent immobilization of glucoamylase onto ρ-benzoquinone activated alginate beads: I. Beads preparation and characterization. Appl. Biochem. Biotechnol. 2011, 164, 10-22.
    • (2011) Appl. Biochem. Biotechnol. , vol.164 , pp. 10-22
    • Eldin, M.S.M.1    Seuror, E.I.2    Nasr, M.A.3    El-Aassar, M.R.4    Tieama, H.A.5
  • 208
    • 0031277606 scopus 로고    scopus 로고
    • Capacitive monitoring of protein immobilization and antigen-antibody reactions on monomolecular alkylthiol films on gold electrodes
    • Mirsky, V.M.; Riepl, M.; Wolfbeis, O.S. Capacitive monitoring of protein immobilization and antigen-antibody reactions on monomolecular alkylthiol films on gold electrodes. Biosens. Bioelectron. 1997, 12, 977-989.
    • (1997) Biosens. Bioelectron. , vol.12 , pp. 977-989
    • Mirsky, V.M.1    Riepl, M.2    Wolfbeis, O.S.3
  • 209
    • 84876736948 scopus 로고    scopus 로고
    • Catalytic activity and thermostability of enzymes immobilized on silanized surface: Influence of the crosslinking agent
    • Aissaoui, N.; Landoulsi, J.; Bergaoui, L.; Boujday, S.; Lambert, J.-F. Catalytic activity and thermostability of enzymes immobilized on silanized surface: Influence of the crosslinking agent. Enzym. Microb. Technol. 2013, 52, 336-343.
    • (2013) Enzym. Microb. Technol. , vol.52 , pp. 336-343
    • Aissaoui, N.1    Landoulsi, J.2    Bergaoui, L.3    Boujday, S.4    Lambert, J.-F.5
  • 210
    • 4444340445 scopus 로고    scopus 로고
    • Development and evaluation of n-hydroxysuccinimide-activated silica for immobilizing human serum albumin in liquid chromatography columns
    • Kim, H.S.; Kye, Y.S.; Hage, D.S. Development and evaluation of n-hydroxysuccinimide-activated silica for immobilizing human serum albumin in liquid chromatography columns. J. Chromatogr. 2004, 1049, 51-61.
    • (2004) J. Chromatogr. , vol.1049 , pp. 51-61
    • Kim, H.S.1    Kye, Y.S.2    Hage, D.S.3
  • 211
    • 0023078036 scopus 로고
    • Covalent immobilization of proteins by techniques which permit subsequent release
    • Horton, H.R.; Swaisgood, H.E. Covalent immobilization of proteins by techniques which permit subsequent release. Methods Enzymol. 1987, 135, 130-141.
    • (1987) Methods Enzymol. , vol.135 , pp. 130-141
    • Horton, H.R.1    Swaisgood, H.E.2
  • 212
    • 84867816058 scopus 로고    scopus 로고
    • Surface modification of siliceous materials using maleimidation and various functional polymers synthesized by reversible addition-fragmentation chain transfer polymerization
    • Seto, H.; Takara, M.; Yamashita, C.; Murakami, T.; Hasegawa, T.; Hoshino, Y.; Miura, Y. Surface modification of siliceous materials using maleimidation and various functional polymers synthesized by reversible addition-fragmentation chain transfer polymerization. ACS Appl. Mater. Interfaces 2012, 4, 5125-5133.
    • (2012) ACS Appl. Mater. Interfaces , vol.4 , pp. 5125-5133
    • Seto, H.1    Takara, M.2    Yamashita, C.3    Murakami, T.4    Hasegawa, T.5    Hoshino, Y.6    Miura, Y.7
  • 213
    • 77149169752 scopus 로고    scopus 로고
    • Investigations of chemical modifications of amino-terminated organic films on silicon substrates and controlled protein immobilization
    • Kim, J.; Cho, J.; Seidler, P.M.; Kurland, N.E.; Yadavalli, V.K. Investigations of chemical modifications of amino-terminated organic films on silicon substrates and controlled protein immobilization. Langmuir 2010, 26, 2599-2608.
    • (2010) Langmuir , vol.26 , pp. 2599-2608
    • Kim, J.1    Cho, J.2    Seidler, P.M.3    Kurland, N.E.4    Yadavalli, V.K.5
  • 214
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfidebond stability
    • Lester, P., Ed.; Academic Press: Waltham, MA, USA
    • Gilbert, H.F. Thiol/disulfide exchange equilibria and disulfidebond stability. In Methods in Enzymology; Lester, P., Ed.; Academic Press: Waltham, MA, USA, 1995; Volume 251, pp. 8-28.
    • (1995) Methods in Enzymology , vol.251 , pp. 8-28
    • Gilbert, H.F.1
  • 215
    • 0023079383 scopus 로고
    • 1,1′-carbonyldiimidazole-mediated immobilization of enzymes and affinity ligands
    • Hearn, M.T.W. 1,1′-Carbonyldiimidazole-mediated immobilization of enzymes and affinity ligands. Methods Enzymol. 1987, 135, 102-117.
    • (1987) Methods Enzymol. , vol.135 , pp. 102-117
    • Hearn, M.T.W.1
  • 217
    • 0141824397 scopus 로고
    • Optimization of protein immobilization on 1,1'-carbonyldiimidazole-activated diol-bonded silica
    • Crowley, S.C.; Chan, K.C.; Walters, R.R. Optimization of protein immobilization on 1,1'-carbonyldiimidazole-activated diol-bonded silica. J. Chromatogr. 1986, 359, 359-368.
    • (1986) J. Chromatogr. , vol.359 , pp. 359-368
    • Crowley, S.C.1    Chan, K.C.2    Walters, R.R.3
  • 219
    • 15744368372 scopus 로고    scopus 로고
    • Preparation and characterization of trypsin immobilized on silica gel supported macroporous chitosan bead
    • Xi, F.; Wu, J.; Jia, Z.; Lin, X. Preparation and characterization of trypsin immobilized on silica gel supported macroporous chitosan bead. Process Biochem. 2005, 40, 2833-2840.
    • (2005) Process Biochem. , vol.40 , pp. 2833-2840
    • Xi, F.1    Wu, J.2    Jia, Z.3    Lin, X.4
  • 220
    • 0343389697 scopus 로고
    • Peg activation and ligand binding for the affinity partitioning of proteins in aqueous two-phase systems
    • Andrews, B.A.; Head, D.M.; Dunthorne, P.; Asenjo, J.A. Peg activation and ligand binding for the affinity partitioning of proteins in aqueous two-phase systems. Biotechnol. Tech. 1990, 4, 49-54.
    • (1990) Biotechnol. Tech. , vol.4 , pp. 49-54
    • Andrews, B.A.1    Head, D.M.2    Dunthorne, P.3    Asenjo, J.A.4
  • 221
    • 79952198691 scopus 로고    scopus 로고
    • Nanoporous silica glass for the immobilization of interactive enzyme systems
    • Buthe, A.; Wu, S.; Wang, P. Nanoporous silica glass for the immobilization of interactive enzyme systems. Methods Mol. Biol. 2011, 679, 37-48.
    • (2011) Methods Mol. Biol. , vol.679 , pp. 37-48
    • Buthe, A.1    Wu, S.2    Wang, P.3
  • 222
    • 84862816196 scopus 로고    scopus 로고
    • Preparation of superparamagnetic sodium alginate nanoparticles for covalent immobilization of candida rugosa lipase
    • Liu, X.; Chen, X.; Li, Y.; Cui, Y.; Zhu, H.; Zhu, W. Preparation of superparamagnetic sodium alginate nanoparticles for covalent immobilization of candida rugosa lipase. J. Nanopart. Res. 2012, 14, doi:10.1007/s11051-012-0763-2.
    • (2012) J. Nanopart. Res. , vol.14
    • Liu, X.1    Chen, X.2    Li, Y.3    Cui, Y.4    Zhu, H.5    Zhu, W.6
  • 223
    • 29144499454 scopus 로고    scopus 로고
    • Amperometric flow-injection determination of phenolic compounds using a biosensor with immobilized laccase, peroxidase and tyrosinase
    • Solná, R.; Skládal, P. Amperometric flow-injection determination of phenolic compounds using a biosensor with immobilized laccase, peroxidase and tyrosinase. Electroanalysis 2005, 17, 2137-2146.
    • (2005) Electroanalysis , vol.17 , pp. 2137-2146
    • Solná, R.1    Skládal, P.2
  • 224
    • 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
  • 225
    • 0033365866 scopus 로고    scopus 로고
    • Influence of activation on the multipoint immobilization of penicillin g acylase on macroporous silica
    • Cardias, H.; Grininger, C.; Trevisan, H.; Guisan, J.; Giordano, R. Influence of activation on the multipoint immobilization of penicillin g acylase on macroporous silica. Braz. J. Chem. Eng. 1999, 16, 141-148.
    • (1999) Braz. J. Chem. Eng. , vol.16 , pp. 141-148
    • Cardias, H.1    Grininger, C.2    Trevisan, H.3    Guisan, J.4    Giordano, R.5
  • 226
    • 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


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