메뉴 건너뛰기




Volumn 205, Issue , 2014, Pages 339-360

Enzymes immobilized in mesoporous silica: A physical-chemical perspective

Author keywords

Biocatalysis; Enzyme immobilization; Mesoporous silica; Microenvironment; Pore filling

Indexed keywords

BIOCATALYSIS; IMMOBILIZATION CONDITIONS; IMMOBILIZATION PROCESS; MESOPOROUS SILICA; MICROENVIRONMENTS; OPTIMAL ENZYME ACTIVITY; PORE FILLING; PROTEIN CONCENTRATIONS;

EID: 84900347565     PISSN: 00018686     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cis.2013.08.010     Document Type: Review
Times cited : (218)

References (170)
  • 2
    • 63349105153 scopus 로고    scopus 로고
    • Mesoporous materials for encapsulating enzymes
    • C.-H. Lee, T.-S. Lin, and C.-Y. Mou Mesoporous materials for encapsulating enzymes Nano Today 4 2009 165 179
    • (2009) Nano Today , vol.4 , pp. 165-179
    • Lee, C.-H.1    Lin, T.-S.2    Mou, C.-Y.3
  • 3
    • 45449104267 scopus 로고    scopus 로고
    • Thermal stability of mesoporous SBA-15 and Sn-SBA-15 molecular sieves: An in situ HTXRD study
    • P. Shah, and V. Ramaswamy Thermal stability of mesoporous SBA-15 and Sn-SBA-15 molecular sieves: An in situ HTXRD study Microporous Mesoporous Mater 114 2008 270 280
    • (2008) Microporous Mesoporous Mater , vol.114 , pp. 270-280
    • Shah, P.1    Ramaswamy, V.2
  • 4
    • 79952061878 scopus 로고    scopus 로고
    • Inorganic nanomaterial-based biocatalysts
    • S.Y. Lee, J. Lee, J.H. Chang, and J.H. Lee Inorganic nanomaterial-based biocatalysts BMB Rep 44 2011 77 86
    • (2011) BMB Rep , vol.44 , pp. 77-86
    • Lee, S.Y.1    Lee, J.2    Chang, J.H.3    Lee, J.H.4
  • 5
    • 26244462959 scopus 로고    scopus 로고
    • Enzymes supported on ordered mesoporous solids: A special case of an inorganic-organic hybrid
    • DOI 10.1039/b506090g
    • H.H.P. Yiu, and P.A. Wright Enzymes supported on ordered mesoporous solids: a special case of an inorganic-organic hybrid J Mater Chem 15 2005 3690 3700 (Pubitemid 41417055)
    • (2005) Journal of Materials Chemistry , vol.15 , Issue.35-36 , pp. 3690-3700
    • Yiu, H.H.P.1    Wright, P.A.2
  • 6
    • 57849086401 scopus 로고    scopus 로고
    • Enzyme-functionalized mesoporous silica for bioanalytical applications
    • DOI 10.1007/s00216-008-2250-2
    • C. Ispas, I. Sokolov, and S. Andreescu Enzyme-functionalized mesoporous silica for bioanalytical applications Anal Bioanal Chem 393 2009 543 554 (Pubitemid 50214397)
    • (2009) Analytical and Bioanalytical Chemistry , vol.393 , Issue.2 , pp. 543-554
    • Ispas, C.1    Sokolov, I.2    Andreescu, S.3
  • 7
    • 84882945349 scopus 로고    scopus 로고
    • Progress in enzyme immobilization in ordered mesoporous materials and related applications
    • Z. Zhou, and M. Hartmann Progress in enzyme immobilization in ordered mesoporous materials and related applications Chem Soc Rev 42 2013 3894 3912
    • (2013) Chem Soc Rev , vol.42 , pp. 3894-3912
    • Zhou, Z.1    Hartmann, M.2
  • 8
    • 84871851300 scopus 로고    scopus 로고
    • Recent progress in biocatalysis with enzymes immobilized on mesoporous hosts
    • Z. Zhou, and M. Hartmann Recent progress in biocatalysis with enzymes immobilized on mesoporous hosts Top Catal 55 2012 1081 1100
    • (2012) Top Catal , vol.55 , pp. 1081-1100
    • Zhou, Z.1    Hartmann, M.2
  • 9
    • 27544472308 scopus 로고    scopus 로고
    • Methodology for the immobilization of enzymes onto mesoporous materials
    • DOI 10.1021/jp052102n
    • S. Hudson, E. Magner, J. Cooney, and B.K. Hodnett Methodology for the immobilization of enzymes onto mesoporous materials J Phys Chem B 109 2005 19496 19506 (Pubitemid 41541159)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.41 , pp. 19496-19506
    • Hudson, S.1    Magner, E.2    Cooney, J.3    Kieran, B.4
  • 10
    • 48149114862 scopus 로고    scopus 로고
    • Octadecanoic acid/silica particles synthesis for enzyme immobilization: Characterization and evaluation of biocatalytic activity
    • R.S. Prakasham, P.R. Likhar, K. Rajyalaxmi, C.S. Rao, and B. Sreedhar Octadecanoic acid/silica particles synthesis for enzyme immobilization: Characterization and evaluation of biocatalytic activity J Mol Catal B: Enzym 55 2008 43 48
    • (2008) J Mol Catal B: Enzym , vol.55 , pp. 43-48
    • Prakasham, R.S.1    Likhar, P.R.2    Rajyalaxmi, K.3    Rao, C.S.4    Sreedhar, B.5
  • 11
    • 33846813429 scopus 로고    scopus 로고
    • Adsorption myoglobin over mesoporous silica molecular sieves: Pore size effect and pore-filling model
    • DOI 10.1016/j.msec.2006.05.012, PII S0928493106000713
    • M. Miyahara, A. Vinu, and K. Ariga Adsorption myoglobin over mesoporous silica molecular sieves: pore size effect and pore-filling model Mater Sci Eng C 27 2007 232 236 (Pubitemid 46205294)
    • (2007) Materials Science and Engineering C , vol.27 , Issue.2 , pp. 232-236
    • Miyahara, M.1    Vinu, A.2    Ariga, K.3
  • 13
    • 40049111883 scopus 로고    scopus 로고
    • Design, synthesis, and properties of inorganic and hybrid thin films having periodically organized nanoporosity
    • DOI 10.1021/cm702100t
    • C. Sanchez, C. Boissière, D. Grosso, C. Laberty, and L. Nicole Design, synthesis, and properties of inorganic and hybrid thin films having periodically organized nanoporosity Chem Mater 20 2008 682 737 (Pubitemid 351320467)
    • (2008) Chemistry of Materials , vol.20 , Issue.3 , pp. 682-737
    • Sanchez, C.1    Boissiere, C.2    Grosso, D.3    Laberty, C.4    Nicole, L.5
  • 14
    • 0037803446 scopus 로고    scopus 로고
    • Pore size determination in modified micro- and mesoporous materials. Pitfalls and limitations in gas adsorption data analysis
    • DOI 10.1016/S1387-1811(03)00339-1
    • J.C. Groen, L.A.A. Peffer, and J. Perez-Ramirez Pore size determination in modified micro- and mesoporous materials. Pitfalls and limitations in gas adsorption data analysis Microporous Mesoporous Mater 60 2003 1 17 (Pubitemid 36775048)
    • (2003) Microporous and Mesoporous Materials , vol.60 , Issue.1-3 , pp. 1-17
    • Groen, J.C.1    Peffer, L.A.A.2    Perez-Ramirez, J.3
  • 15
    • 0032559316 scopus 로고    scopus 로고
    • Triblock copolymer syntheses of mesoporous silica with periodic 50 to 300 angstrom pores
    • DOI 10.1126/science.279.5350.548
    • D.Y. Zhao, J.L. Feng, Q.S. Huo, N. Melosh, G.H. Fredrickson, and B.F. Chmelka et al. Triblock copolymer syntheses of mesoporous silica with periodic 50 to 300 Angstrom pores Science 279 1998 548 552 (Pubitemid 28067280)
    • (1998) Science , vol.279 , Issue.5350 , 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
  • 16
    • 1642356865 scopus 로고    scopus 로고
    • Formation of mesostructured titania thin films using isopropoxide precursors
    • DOI 10.1016/j.cap.2003.10.021, PII S1567173903001676
    • I. Kartini, P. Meredith, J.C.D. da Costa, J.D. Riches, and G.Q.M. Lu Formation of mesostructured titania thin films using isopropoxide precursors Curr Appl Phys 4 2004 160 162 (Pubitemid 38360841)
    • (2004) Current Applied Physics , vol.4 , Issue.2-4 , pp. 160-162
    • Kartini, I.1    Meredith, P.2    Diniz Da Costa, J.C.3    Riches, J.D.4    Lu, G.Q.M.5
  • 17
    • 0032511881 scopus 로고    scopus 로고
    • Generalized syntheses of large-pore mesoporous metal oxides with semicrystalline frameworks
    • DOI 10.1038/24132
    • P.D. Yang, D.Y. Zhao, D.I. Margolese, B.F. Chmelka, and G.D. Stucky Generalized syntheses of large-pore mesoporous metal oxides with semicrystalline frameworks Nature 396 1998 152 155 (Pubitemid 28523613)
    • (1998) Nature , vol.396 , Issue.6707 , pp. 152-155
    • Yang, P.1    Zhao, D.2    Margolese, D.I.3    Chmelka, B.F.4    Stucky, G.D.5
  • 18
    • 79959620549 scopus 로고    scopus 로고
    • Immobilization of feruloyl esterases in mesoporous materials leads to improved transesterification yield
    • C. Thörn, H. Gustafsson, and L. Olsson Immobilization of feruloyl esterases in mesoporous materials leads to improved transesterification yield J Mol Catal B: Enzym 72 2011 57 64
    • (2011) J Mol Catal B: Enzym , vol.72 , pp. 57-64
    • Thörn, C.1    Gustafsson, H.2    Olsson, L.3
  • 19
    • 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
    • H. Gustafsson, E.M. Johansson, A. Barrabino, M. Odén, and K. Holmberg Immobilization of lipase from Mucor miehei and Rhizopus oryzae into mesoporous silica - the effect of varied particle size and morphology Colloids Surf B 100 2012 22 30
    • (2012) Colloids Surf B , vol.100 , pp. 22-30
    • Gustafsson, H.1    Johansson, E.M.2    Barrabino, A.3    Odén, M.4    Holmberg, K.5
  • 20
    • 39849092414 scopus 로고    scopus 로고
    • Mesoporous materials as host for an entrapped enzyme
    • DOI 10.1016/j.micromeso.2007.06.025, PII S1387181107003770
    • P. Reis, T. Witula, and K. Holmberg Mesoporous materials as host for an entrapped enzyme Microporous Mesoporous Mater 110 2008 355 362 (Pubitemid 351318329)
    • (2008) Microporous and Mesoporous Materials , vol.110 , Issue.2-3 , pp. 355-362
    • Reis, P.1    Witula, T.2    Holmberg, K.3
  • 21
    • 84874923445 scopus 로고    scopus 로고
    • Large-pore ordered mesoporous materials templated from non-Pluronic amphiphilic block copolymers
    • Y. Deng, J. Wei, Z. Sun, and D. Zhao Large-pore ordered mesoporous materials templated from non-Pluronic amphiphilic block copolymers Chem Soc Rev 42 2013 4054 4070
    • (2013) Chem Soc Rev , vol.42 , pp. 4054-4070
    • Deng, Y.1    Wei, J.2    Sun, Z.3    Zhao, D.4
  • 22
    • 2342642030 scopus 로고    scopus 로고
    • Functionalization of mesoporous silica for lipase immobilization: Characterization of the support and the catalysts
    • DOI 10.1016/j.molcatb.2004.03.012, PII S1381117704001201
    • R.M. Blanco, P. Terreros, M. Fernández-Pérez, C. Otero, and G. Díaz-González Functionalization of mesoporous silica for lipase immobilization: characterization of the support and the catalysts J Mol Catal B: Enzym 30 2004 83 93 (Pubitemid 38597105)
    • (2004) Journal of Molecular Catalysis B: Enzymatic , vol.30 , Issue.2 , pp. 83-93
    • Blanco, R.M.1    Terreros, P.2    Fernandez-Perez, M.3    Otero, C.4    Diaz-Gonzalez, G.5
  • 23
    • 0026931265 scopus 로고
    • Ordered mesoporous molecular sieves synthesized by a liquid-crystal template mechanism
    • DOI 10.1038/359710a0
    • C.T. Kresge, M.E. Leonowicz, W.J. Roth, J.C. Vartuli, and J.S. Beck Ordered mesoporous molecular sieves synthesized by a liquid-crystal template mechanism Nature 359 1992 710 712 (Pubitemid 23589384)
    • (1992) Nature , vol.359 , Issue.6397 , pp. 710-712
    • Kresge, C.T.1    Leonowicz, M.E.2    Roth, W.J.3    Vartuli, J.C.4    Beck, J.S.5
  • 26
    • 12444272525 scopus 로고
    • Adsorption of gases in multimolecular layers
    • S. Brunauer, P.H. Emmett, and E. Teller Adsorption of gases in multimolecular layers J Am Chem Soc 60 1938 309 319
    • (1938) J Am Chem Soc , vol.60 , pp. 309-319
    • Brunauer, S.1    Emmett, P.H.2    Teller, E.3
  • 27
    • 0342445773 scopus 로고
    • The determination of pore volume and area distributions in porous substances. 1. Computations from nitrogen isotherms
    • E.P. Barrett, L.G. Joyner, and P.P. Halenda The determination of pore volume and area distributions in porous substances. 1. Computations from nitrogen isotherms J Am Chem Soc 73 1951 373 380
    • (1951) J Am Chem Soc , vol.73 , pp. 373-380
    • Barrett, E.P.1    Joyner, L.G.2    Halenda, P.P.3
  • 28
    • 33845246929 scopus 로고
    • Studies on pore systems in catalysts: IX. Calculation of pore distributions from the adsorption branch of nitrogen sorption isotherms in the case of open cylindrical pores A. Fundamental equations
    • J.C.P. Broekhoff, and J.H. de Boer Studies on pore systems in catalysts: IX. Calculation of pore distributions from the adsorption branch of nitrogen sorption isotherms in the case of open cylindrical pores A. Fundamental equations J Catal 9 1967 8 14
    • (1967) J Catal , vol.9 , pp. 8-14
    • Broekhoff, J.C.P.1    De Boer, J.H.2
  • 29
    • 34249872888 scopus 로고
    • Studies on pore systems in catalysts: X. Calculations of pore distributions from the adsorption branch of nitrogen sorption isotherms in the case of open cylindrical pores B. Applications
    • J.C.P. Broekhoff, and J.H. de Boer Studies on pore systems in catalysts: X. Calculations of pore distributions from the adsorption branch of nitrogen sorption isotherms in the case of open cylindrical pores B. Applications J Catal 9 1967 15 27
    • (1967) J Catal , vol.9 , pp. 15-27
    • Broekhoff, J.C.P.1    De Boer, J.H.2
  • 30
    • 0032642669 scopus 로고    scopus 로고
    • Evaluating pore sizes in mesoporous materials: A simplified standard adsorption method and a simplified Broekhoff-de Boer method
    • W.W. Lukens, P. Schmidt-Winkel, D.Y. Zhao, J.L. Feng, and G.D. Stucky Evaluating pore sizes in mesoporous materials: a simplified standard adsorption method and a simplified Broekhoff-de Boer method Langmuir 15 1999 5403 5409
    • (1999) Langmuir , vol.15 , pp. 5403-5409
    • Lukens, W.W.1    Schmidt-Winkel, P.2    Zhao, D.Y.3    Feng, J.L.4    Stucky, G.D.5
  • 31
    • 0031270015 scopus 로고    scopus 로고
    • Application of large pore MCM-41 molecular sieves to improve pore size analysis using nitrogen adsorption measurements
    • M. Kruk, M. Jaroniec, and A. Sayari Application of large pore MCM-41 molecular sieves to improve pore size analysis using nitrogen adsorption measurements Langmuir 13 1997 6267 6273 (Pubitemid 127592029)
    • (1997) Langmuir , vol.13 , Issue.23 , pp. 6267-6273
    • Kruk, M.1    Jaroniec, M.2    Sayari, A.3
  • 32
    • 33751157144 scopus 로고
    • Effect of surfactant silica molar ratios on the formation of mesoporous molecular sieves: Inorganic mimicry of surfactant liquid-crystal phases and mechanistic implications
    • J.C. Vartuli, K.D. Schmitt, C.T. Kresge, W.J. Roth, M.E. Leonowicz, and S.B. Mccullen et al. Effect of surfactant silica molar ratios on the formation of mesoporous molecular sieves: inorganic mimicry of surfactant liquid-crystal phases and mechanistic implications Chem Mater 6 1994 2317 2326
    • (1994) Chem Mater , vol.6 , pp. 2317-2326
    • Vartuli, J.C.1    Schmitt, K.D.2    Kresge, C.T.3    Roth, W.J.4    Leonowicz, M.E.5    McCullen, S.B.6
  • 34
    • 0031801728 scopus 로고    scopus 로고
    • Nonionic triblock and star diblock copolymer and oligomeric sufactant syntheses of highly ordered, hydrothermally stable, mesoporous silica structures
    • DOI 10.1021/ja974025i
    • D.Y. Zhao, Q.S. Huo, J.L. Feng, B.F. Chmelka, and G.D. Stucky Nonionic triblock and star diblock copolymer and oligomeric surfactant syntheses of highly ordered, hydrothermally stable, mesoporous silica structures J Am Chem Soc 120 1998 6024 6036 (Pubitemid 28306987)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.24 , pp. 6024-6036
    • Zhao, D.1    Huo, Q.2    Feng, J.3    Chmelka, B.F.4    Stucky, G.D.5
  • 35
    • 68349154495 scopus 로고    scopus 로고
    • Synthesis and characterization of large mesoporous silica SBA-15 sheets with ordered accessible 18 nm pores
    • E.M. Johansson, J.M. Córdoba, and M. Odén Synthesis and characterization of large mesoporous silica SBA-15 sheets with ordered accessible 18 nm pores Mater Lett 63 2009 2129 2131
    • (2009) Mater Lett , vol.63 , pp. 2129-2131
    • Johansson, E.M.1    Córdoba, J.M.2    Odén, M.3
  • 36
    • 0035389295 scopus 로고    scopus 로고
    • Synthesis of SBA-15 with different pore sizes and the utilization as supports of high loading of cobalt catalysts
    • Y. Wang, M. Noguchi, Y. Takahashi, and Y. Ohtsuka Synthesis of SBA-15 with different pore sizes and the utilization as supports of high loading of cobalt catalysts Catal Today 68 2001 3 9
    • (2001) Catal Today , vol.68 , pp. 3-9
    • Wang, Y.1    Noguchi, M.2    Takahashi, Y.3    Ohtsuka, Y.4
  • 38
    • 0034295701 scopus 로고    scopus 로고
    • Hexagonal to mesocellular foam phase transition in polymer-templated mesoporous silicas
    • J.S. Lettow, Y.J. Han, P. Schmidt-Winkel, P.D. Yang, D.Y. Zhao, and G.D. Stucky et al. Hexagonal to mesocellular foam phase transition in polymer-templated mesoporous silicas Langmuir 16 2000 8291 8295
    • (2000) Langmuir , vol.16 , pp. 8291-8295
    • Lettow, J.S.1    Han, Y.J.2    Schmidt-Winkel, P.3    Yang, P.D.4    Zhao, D.Y.5    Stucky, G.D.6
  • 39
    • 60949086135 scopus 로고    scopus 로고
    • Synthesis of spherical mesoporous silica nanoparticles with nanometer-size controllable pores and outer diameters
    • A.B.D. Nandiyanto, S.G. Kim, F. Iskandar, and K. Okuyama Synthesis of spherical mesoporous silica nanoparticles with nanometer-size controllable pores and outer diameters Microporous Mesoporous Mater 120 2009 447 453
    • (2009) Microporous Mesoporous Mater , vol.120 , pp. 447-453
    • Nandiyanto, A.B.D.1    Kim, S.G.2    Iskandar, F.3    Okuyama, K.4
  • 40
    • 4644324496 scopus 로고    scopus 로고
    • Functionalized nanoporous silicas for the immobilization of penicillin acylase
    • A.S.M. Chong, and X.S. Zhao Functionalized nanoporous silicas for the immobilization of penicillin acylase Appl Surf Sci 237 2004 398 404
    • (2004) Appl Surf Sci , vol.237 , pp. 398-404
    • Chong, A.S.M.1    Zhao, X.S.2
  • 41
    • 0037174353 scopus 로고    scopus 로고
    • Entrapping enzyme in a functionalized nanoporous support
    • C.H. Lei, Y.S. Shin, J. Liu, and E.J. Ackerman Entrapping enzyme in a functionalized nanoporous support J Am Chem Soc 124 2002 11242 11243
    • (2002) J Am Chem Soc , vol.124 , pp. 11242-11243
    • Lei, C.H.1    Shin, Y.S.2    Liu, J.3    Ackerman, E.J.4
  • 42
    • 14844322204 scopus 로고    scopus 로고
    • Mesoporous silica spheres as supports for enzyme immobilization and encapsulation
    • DOI 10.1021/cm0483137
    • Y.J. Wang, and F. Caruso Mesoporous silica spheres as supports for enzyme immobilization and encapsulation Chem Mater 17 2005 953 961 (Pubitemid 40344018)
    • (2005) Chemistry of Materials , vol.17 , Issue.5 , pp. 953-961
    • Wang, Y.1    Caruso, F.2
  • 43
    • 0035820045 scopus 로고    scopus 로고
    • Adsorption and activity of cytochrome c on mesoporous silicates
    • J. Deere, E. Magner, J.G. Wall, and B.K. Hodnett Adsorption and activity of cytochrome c on mesoporous silicates Chem Commun 2001 465 466 (Pubitemid 32217405)
    • (2001) Chemical Communications , Issue.5 , pp. 465-466
    • Deere, J.1    Magner, E.2    Wall, J.G.3    Hodnett, B.K.4
  • 44
    • 4043075579 scopus 로고    scopus 로고
    • Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme
    • A.A. Vertegel, R.W. Siegel, and J.S. Dordick Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme Langmuir 20 2004 6800 6807
    • (2004) Langmuir , vol.20 , pp. 6800-6807
    • Vertegel, A.A.1    Siegel, R.W.2    Dordick, J.S.3
  • 45
    • 79960404832 scopus 로고    scopus 로고
    • A comparison of lipase and trypsin encapsulated in mesoporous materials with varying pore sizes and pH conditions
    • H. Gustafsson, C. Thörn, and K. Holmberg A comparison of lipase and trypsin encapsulated in mesoporous materials with varying pore sizes and pH conditions Colloids Surf B 87 2011 464 471
    • (2011) Colloids Surf B , vol.87 , pp. 464-471
    • Gustafsson, H.1    Thörn, C.2    Holmberg, K.3
  • 46
    • 84860347827 scopus 로고    scopus 로고
    • Synthesis of silica particles and their application as supports for alcohol dehydrogenases and cofactor immobilizations: Conformational changes that lead to switch in enzyme stereoselectivity
    • G.A. Petkova, K. Záruba, and V. Král Synthesis of silica particles and their application as supports for alcohol dehydrogenases and cofactor immobilizations: conformational changes that lead to switch in enzyme stereoselectivity Biochim Biophys Acta Proteins Proteomics 1824 2012 792 801
    • (2012) Biochim Biophys Acta Proteins Proteomics , vol.1824 , pp. 792-801
    • Petkova, G.A.1    Záruba, K.2    Král, V.3
  • 47
    • 77952700564 scopus 로고    scopus 로고
    • Cytochrome c covalently immobilized on mesoporous silicas as a peroxidase: Orientation effect
    • K.C. Kao, C.H. Lee, T.S. Lin, and C.Y. Mou Cytochrome c covalently immobilized on mesoporous silicas as a peroxidase: orientation effect J Mater Chem 20 2010 4653 4662
    • (2010) J Mater Chem , vol.20 , pp. 4653-4662
    • Kao, K.C.1    Lee, C.H.2    Lin, T.S.3    Mou, C.Y.4
  • 48
    • 84862787893 scopus 로고    scopus 로고
    • Improved activity and stability of lipase immobilized in cage-like large pore mesoporous organosilicas
    • Z. Zhou, A. Inayat, W. Schwieger, and M. Hartmann Improved activity and stability of lipase immobilized in cage-like large pore mesoporous organosilicas Microporous Mesoporous Mater 154 2012 133 141
    • (2012) Microporous Mesoporous Mater , vol.154 , pp. 133-141
    • Zhou, Z.1    Inayat, A.2    Schwieger, W.3    Hartmann, M.4
  • 50
    • 84874596746 scopus 로고    scopus 로고
    • Mesoporous material SBA-15 modified by amino acid ionic liquid to immobilize lipase via ionic bonding and cross-linking method
    • B. Zou, Y. Hu, L. Jiang, R. Jia, and H. Huang Mesoporous material SBA-15 modified by amino acid ionic liquid to immobilize lipase via ionic bonding and cross-linking method Ind Eng Chem Res 52 2013 2844 2851
    • (2013) Ind Eng Chem Res , vol.52 , pp. 2844-2851
    • Zou, B.1    Hu, Y.2    Jiang, L.3    Jia, R.4    Huang, H.5
  • 51
    • 33846044706 scopus 로고    scopus 로고
    • Characterization of functionalized nanoporous supports for protein confinement
    • DOI 10.1088/0957-4484/17/22/001, PII S0957448406293152, 001
    • C.H. Lei, Y. Shin, J.K. Magnuson, G. Fryxell, L.L. Lasure, and D.C. Elliott et al. Characterization of functionalized nanoporous supports for protein confinement Nanotechnology 17 2006 5531 5538 (Pubitemid 46069970)
    • (2006) Nanotechnology , vol.17 , Issue.22 , pp. 5531-5538
    • Lei, C.1    Shin, Y.2    Magnuson, J.K.3    Fryxell, G.4    Lasure, L.L.5    Elliott, D.C.6    Liu, J.7    Ackerman, E.J.8
  • 52
    • 33747097811 scopus 로고    scopus 로고
    • Chemically surface modified gel (CSMG): An excellent enzyme- immobilization matrix for industrial processes
    • DOI 10.1016/j.jbiotec.2006.03.019, PII S0168165606002124
    • A.E. David, N.S. Wang, V.C. Yang, and A.J. Yang Chemically surface modified gel (CSMG): an excellent enzyme-immobilization matrix for industrial processes J Biotechnol 125 2006 395 407 (Pubitemid 44223830)
    • (2006) Journal of Biotechnology , vol.125 , Issue.3 , pp. 395-407
    • David, A.E.1    Wang, N.S.2    Yang, V.C.3    Yang, A.J.4
  • 53
    • 34248199841 scopus 로고    scopus 로고
    • Synergetic effects of nanoporous support and urea on enzyme activity
    • DOI 10.1021/nl070255b
    • C.H. Lei, Y.S. Shin, J. Liu, and E.J. Ackerman Synergetic effects of nanoporous support and urea on enzyme activity Nano Lett 7 2007 1050 1053 (Pubitemid 46717758)
    • (2007) Nano Letters , vol.7 , Issue.4 , pp. 1050-1053
    • Lei, C.1    Shin, Y.2    Liu, J.3    Ackerman, E.J.4
  • 56
    • 31544474363 scopus 로고    scopus 로고
    • Encapsulation of myoglobin with a mesoporous silicate results in new capabilities
    • DOI 10.1021/bc050238i
    • T. Itoh, R. Ishii, T. Ebina, T. Hanaoka, Y. Fukushima, and F. Mizukami Encapsulation of myoglobin with a mesoporous silicate results in new capabilities Bioconjug Chem 17 2006 236 240 (Pubitemid 43157606)
    • (2006) Bioconjugate Chemistry , vol.17 , Issue.1 , pp. 236-240
    • Itoh, T.1    Ishii, R.2    Ebina, T.3    Hanaoka, T.4    Fukushima, Y.5    Mizukami, F.6
  • 57
    • 34250311284 scopus 로고    scopus 로고
    • Encapsulation of hemoglobin in mesoporous silica (FSM) - Enhanced thermal stability and resistance to denaturants
    • DOI 10.1002/cbic.200600486
    • Y. Urabe, T. Shiomi, T. Itoh, A. Kawai, T. Tsunoda, and F. Mizukami et al. Encapsulation of hemoglobin in mesoporous silica (FSM) - enhanced thermal stability and resistance to denaturants Chembiochem 8 2007 668 674 (Pubitemid 47194860)
    • (2007) ChemBioChem , vol.8 , Issue.6 , pp. 668-674
    • Urabe, Y.1    Shiomi, T.2    Itoh, T.3    Kawai, A.4    Tsunoda, T.5    Mizukami, F.6    Sakaguchi, K.7
  • 58
    • 52449093614 scopus 로고    scopus 로고
    • Click chemistry for high-density biofunctionalization of mesoporous silica
    • A. Schlossbauer, D. Schaffert, J. Kecht, E. Wagner, and T. Bein Click chemistry for high-density biofunctionalization of mesoporous silica J Am Chem Soc 130 2008 12558 12559
    • (2008) J Am Chem Soc , vol.130 , pp. 12558-12559
    • Schlossbauer, A.1    Schaffert, D.2    Kecht, J.3    Wagner, E.4    Bein, T.5
  • 60
    • 67349203634 scopus 로고    scopus 로고
    • Adsorption and catalytic activity of Porcine pancreatic lipase on rod-like SBA-15 mesoporous material
    • Y.J. Li, G.W. Zhou, C.J. Li, D.W. Qin, W.T. Qiao, and B. Chu Adsorption and catalytic activity of Porcine pancreatic lipase on rod-like SBA-15 mesoporous material Colloids Surf A 341 2009 79 85
    • (2009) Colloids Surf A , vol.341 , pp. 79-85
    • Li, Y.J.1    Zhou, G.W.2    Li, C.J.3    Qin, D.W.4    Qiao, W.T.5    Chu, B.6
  • 61
    • 34547729864 scopus 로고    scopus 로고
    • Resolution of 2-octanol by SBA-15 immobilized Pseudomonas sp. Lipase
    • DOI 10.1016/j.molcatb.2007.06.002, PII S1381117707001129
    • D.H. Yu, Z. Wang, L.F. Zhao, Y.M. Cheng, and S.G. Cao Resolution of 2-octanol by SBA-15 immobilized Pseudomonas sp. lipase J Mol Catal B: Enzym 48 2007 64 69 (Pubitemid 47239482)
    • (2007) Journal of Molecular Catalysis B: Enzymatic , vol.48 , Issue.3-4 , pp. 64-69
    • Yu, D.1    Wang, Z.2    Zhao, L.3    Cheng, Y.4    Cao, S.5
  • 62
    • 15444380461 scopus 로고    scopus 로고
    • Using mesoporous silica materials to immobilise biocatalysis-enzymes
    • DOI 10.1016/j.catcom.2005.02.005, PII S156673670500035X
    • D. Moelans, P. Cool, J. Baeyens, and E.F. Vansant Using mesoporous silica materials to immobilise biocatalysis-enzymes Catal Commun 6 2005 307 311 (Pubitemid 40394141)
    • (2005) Catalysis Communications , vol.6 , Issue.4 , pp. 307-311
    • Moelans, D.1    Cool, P.2    Baeyens, J.3    Vansant, E.F.4
  • 63
    • 4143110080 scopus 로고    scopus 로고
    • Analysis of protein adsorption characteristics to nano-pore silica particles by using confocal laser scanning microscopy
    • DOI 10.1016/j.jbiotec.2004.05.005, PII S0168165604002457
    • C.W. Suh, M.Y. Kim, J.B. Choo, J.K. Kim, H.K. Kim, and E.K. Lee Analysis of protein adsorption characteristics to nano-pore silica particles by using confocal laser scanning microscopy J Biotechnol 112 2004 267 277 (Pubitemid 39093959)
    • (2004) Journal of Biotechnology , vol.112 , Issue.3 , pp. 267-277
    • Suh, C.W.1    Kim, M.Y.2    Choo, J.B.3    Kim, J.K.4    Kim, H.K.5    Lee, E.K.6
  • 65
    • 79959437674 scopus 로고    scopus 로고
    • 3D vision of human lysozyme adsorbed onto a SBA-15 nanostructured matrix
    • M. Piras, A. Salis, M. Piludu, D. Steri, and M. Monduzzi 3D vision of human lysozyme adsorbed onto a SBA-15 nanostructured matrix Chem Commun 47 2011 7338 7340
    • (2011) Chem Commun , vol.47 , pp. 7338-7340
    • Piras, M.1    Salis, A.2    Piludu, M.3    Steri, D.4    Monduzzi, M.5
  • 67
    • 0030190422 scopus 로고    scopus 로고
    • Influence of the sorbate type on the XRD peak intensities of loaded MCM-41
    • PII S0927651396000168
    • B. Marler, U. Oberhagemann, S. Vortmann, and H. Gies Influence of the sorbate type on the XRD peak intensities of loaded MCM-41 Microporous Mater 6 1996 375 383 (Pubitemid 126828891)
    • (1996) Microporous Materials , vol.6 , Issue.5-6 , pp. 375-383
    • Marler, B.1    Oberhagemann, U.2    Vortmann, S.3    Gies, H.4
  • 68
    • 17044361862 scopus 로고    scopus 로고
    • Biomaterial immobilization in nanoporous carbon molecular sieves: Influence of solution pH, pore volume, and pore diameter
    • DOI 10.1021/jp050454o
    • A. Vinu, M. Miyahara, and K. Ariga Biomaterial immobilization in nanoporous carbon molecular sieves: influence of solution pH, pore volume, and pore diameter J Phys Chem B 109 2005 6436 6441 (Pubitemid 40496860)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.13 , pp. 6436-6441
    • Vinu, A.1    Miyahara, M.2    Ariga, K.3
  • 69
    • 79952439544 scopus 로고    scopus 로고
    • Immobilization of enzyme-encapsulated nanoporous material in a microreactor and reaction analysis
    • S.-i. Matsuura, R. Ishii, T. Itoh, S. Hamakawa, T. Tsunoda, and T. Hanaoka et al. Immobilization of enzyme-encapsulated nanoporous material in a microreactor and reaction analysis Chem Eng J 167 2011 744 749
    • (2011) Chem Eng J , vol.167 , pp. 744-749
    • Matsuura, S.-I.1    Ishii, R.2    Itoh, T.3    Hamakawa, S.4    Tsunoda, T.5    Hanaoka, T.6
  • 70
    • 84873714910 scopus 로고    scopus 로고
    • Location of enzyme in lipase-SBA-12 hybrid biocatalyst
    • M. Alvaro, M.B. Rosa, and D. Isabel Location of enzyme in lipase-SBA-12 hybrid biocatalyst J Mol Catal B: Enzym 90 2013 23 25
    • (2013) J Mol Catal B: Enzym , vol.90 , pp. 23-25
    • Alvaro, M.1    Rosa, M.B.2    Isabel, D.3
  • 71
    • 84876903749 scopus 로고    scopus 로고
    • QCM-D as a method for monitoring enzyme immobilization in mesoporous silica particles
    • C. Thörn, H. Gustafsson, and L. Olsson QCM-D as a method for monitoring enzyme immobilization in mesoporous silica particles Microporous Mesoporous Mater 176 2013 71 77
    • (2013) Microporous Mesoporous Mater , vol.176 , pp. 71-77
    • Thörn, C.1    Gustafsson, H.2    Olsson, L.3
  • 72
    • 0000083894 scopus 로고    scopus 로고
    • A simple setup to simultaneously measure the resonant frequency and the absolute dissipation factor of a quartz crystal microbalance
    • M. Rodahl, and B. Kasemo A simple setup to simultaneously measure the resonant frequency and the absolute dissipation factor of a quartz crystal microbalance Rev Sci Instrum 67 1996 3238 3241 (Pubitemid 126558570)
    • (1996) Review of Scientific Instruments , vol.67 , Issue.9 , pp. 3238-3241
    • Rodahl, M.1    Kasemo, B.2
  • 73
    • 84900350359 scopus 로고    scopus 로고
    • Carlsson N, Åkerman B. Unpublished.
    • Carlsson N, Åkerman B. Unpublished.
  • 75
    • 0037397160 scopus 로고    scopus 로고
    • The adsorption of basic dyes from aqueous solution on modified peat-resin particle
    • DOI 10.1016/S0043-1354(02)00520-1, PII S0043135402005201
    • Q. Sun, and L. Yang The adsorption of basic dyes from aqueous solution on modified peat-resin particle Water Res 37 2003 1535 1544 (Pubitemid 36207565)
    • (2003) Water Research , vol.37 , Issue.7 , pp. 1535-1544
    • Sun, Q.1    Yang, L.2
  • 76
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 78
    • 79959675860 scopus 로고    scopus 로고
    • Different size biomolecules anchoring on porous silicon surface: Fluorescence and reflectivity pores infiltration comparative studies
    • A.M. Giovannozzi, C. Renacco, M. Derosas, E. Enrico, A. Farano, and A.M. Rossi Different size biomolecules anchoring on porous silicon surface: fluorescence and reflectivity pores infiltration comparative studies Phys Status Solidi C 8 2011 1878 1882
    • (2011) Phys Status Solidi C , vol.8 , pp. 1878-1882
    • Giovannozzi, A.M.1    Renacco, C.2    Derosas, M.3    Enrico, E.4    Farano, A.5    Rossi, A.M.6
  • 79
    • 84863953604 scopus 로고    scopus 로고
    • Encapsulation of enzyme in large mesoporous material with small mesoporous windows
    • B. Malvi, and S. Sen Gupta Encapsulation of enzyme in large mesoporous material with small mesoporous windows Chem Commun 48 2012 7853 7855
    • (2012) Chem Commun , vol.48 , pp. 7853-7855
    • Malvi, B.1    Sen Gupta, S.2
  • 80
    • 84859615805 scopus 로고    scopus 로고
    • Chemistry of aqueous silica nanoparticle surfaces and the mechanism of selective peptide adsorption
    • S.V. Patwardhan, F.S. Emami, R.J. Berry, S.E. Jones, R.R. Naik, and O. Deschaume et al. Chemistry of aqueous silica nanoparticle surfaces and the mechanism of selective peptide adsorption J Am Chem Soc 134 2012 6244 6256
    • (2012) J Am Chem Soc , vol.134 , pp. 6244-6256
    • Patwardhan, S.V.1    Emami, F.S.2    Berry, R.J.3    Jones, S.E.4    Naik, R.R.5    Deschaume, O.6
  • 82
    • 0041734839 scopus 로고    scopus 로고
    • Rapid and high-capacity immobilization of enzymes based on mesoporous silicas with controlled morphologies
    • J. Fan, J. Lei, L.M. Wang, C.Z. Yu, B. Tu, and D.Y. Zhao Rapid and high-capacity immobilization of enzymes based on mesoporous silicas with controlled morphologies Chem Commun 2003 2140 2141 (Pubitemid 37076085)
    • (2003) Chemical Communications , Issue.17 , pp. 2140-2141
    • Fan, J.1    Lei, J.2    Wang, L.3    Yu, C.4    Tu, B.5    Zhao, D.6
  • 83
    • 80755143198 scopus 로고    scopus 로고
    • General description of the adsorption of proteins at their iso-electric point in nanoporous materials
    • L.-C. Sang, A. Vinu, and M.-O. Coppens General description of the adsorption of proteins at their iso-electric point in nanoporous materials Langmuir 27 2011 13828 13837
    • (2011) Langmuir , vol.27 , pp. 13828-13837
    • Sang, L.-C.1    Vinu, A.2    Coppens, M.-O.3
  • 84
    • 17944362995 scopus 로고    scopus 로고
    • Determination by x-ray reflectivity and small angle x-ray scattering of the porous properties of mesoporous silica thin films
    • S. Dourdain, J.F. Bardeau, M. Colas, B. Smarsly, A. Mehdi, and B.M. Ocko et al. Determination by x-ray reflectivity and small angle x-ray scattering of the porous properties of mesoporous silica thin films Appl Phys Lett 86 2005
    • (2005) Appl Phys Lett , vol.86
    • Dourdain, S.1    Bardeau, J.F.2    Colas, M.3    Smarsly, B.4    Mehdi, A.5    Ocko, B.M.6
  • 85
    • 27944470000 scopus 로고    scopus 로고
    • On the capillary condensation of water in mesoporous silica films measured by x-ray reflectivity
    • S. Dourdain, and A. Gibaud On the capillary condensation of water in mesoporous silica films measured by x-ray reflectivity Appl Phys Lett 87 2005 223105
    • (2005) Appl Phys Lett , vol.87 , pp. 223105
    • Dourdain, S.1    Gibaud, A.2
  • 86
    • 17044403825 scopus 로고    scopus 로고
    • Modeling the fractal growth of templated, mesoporous silica films
    • DOI 10.1021/jp045304c
    • K.J. Edler, M. Arrowsmith, M. Hamilton, and S.P. Rigby Modeling the fractal growth of templated, mesoporous silica films J Phys Chem B 109 2005 6294 6303 (Pubitemid 40496844)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.13 , pp. 6294-6303
    • Edler, K.J.1    Arrowsmith, M.2    Hamilton, M.3    Rigby, S.P.4
  • 87
    • 4544278751 scopus 로고    scopus 로고
    • Protein folding and binding in confined spaces and in crowded solutions
    • H.X. Zhou Protein folding and binding in confined spaces and in crowded solutions J Mol Recognit 17 2004 368 375
    • (2004) J Mol Recognit , vol.17 , pp. 368-375
    • Zhou, H.X.1
  • 88
    • 33646475011 scopus 로고    scopus 로고
    • Macromolecular crowding
    • A.P. Minton Macromolecular crowding Curr Biol 16 2006 R269 R271
    • (2006) Curr Biol , vol.16
    • Minton, A.P.1
  • 89
    • 0034853355 scopus 로고    scopus 로고
    • Kinetic and titration methods for determination of active site contents of enzyme and catalytic antibody preparations
    • DOI 10.1006/meth.2001.1176
    • K. Brocklehurst, M. Resmini, and C.M. Topham Kinetic and titration methods for determination of active site contents of enzyme and catalytic antibody preparations Methods 24 2001 153 167 (Pubitemid 32848415)
    • (2001) Methods , vol.24 , Issue.2 , pp. 153-167
    • Brocklehurst, K.1    Resmini, M.2    Topham, C.M.3
  • 90
    • 79751532621 scopus 로고    scopus 로고
    • Active-site titration analysis of surface influences on immobilized Candida antarctica lipase B activity
    • J.A. Laszlo, M. Jackson, and R.M. Blanco Active-site titration analysis of surface influences on immobilized Candida antarctica lipase B activity J Mol Catal B: Enzym 69 2011 60 65
    • (2011) J Mol Catal B: Enzym , vol.69 , pp. 60-65
    • Laszlo, J.A.1    Jackson, M.2    Blanco, R.M.3
  • 91
    • 0023451547 scopus 로고
    • Preparation of monodispersed colloidal particles
    • T. Sugimoto Preparation of monodispersed colloidal particles Adv Colloid Interface Sci 28 1987 65 108
    • (1987) Adv Colloid Interface Sci , vol.28 , pp. 65-108
    • Sugimoto, T.1
  • 92
    • 0029734498 scopus 로고    scopus 로고
    • Preparation of monodispersed polymer-modified colloidal silica particles of less than 50 nm diameter
    • K. Yoshinaga, K. Sueishi, and H. Karakawa Preparation of monodispersed polymer-modified colloidal silica particles of less than 50 nm diameter Polym Adv Technol 7 1996 53 56 (Pubitemid 126598025)
    • (1996) Polymers for Advanced Technologies , vol.7 , Issue.1 , pp. 53-56
    • Yoshinaga, K.1    Sueishi, K.2    Karakawa, H.3
  • 93
    • 67649361537 scopus 로고    scopus 로고
    • Bioanalytical applications of biomolecule-functionalized nanometer-sized doped silica particles
    • D. Knopp, D.P. Tang, and R. Niessner Bioanalytical applications of biomolecule-functionalized nanometer-sized doped silica particles Anal Chim Acta 647 2009 14 30
    • (2009) Anal Chim Acta , vol.647 , pp. 14-30
    • Knopp, D.1    Tang, D.P.2    Niessner, R.3
  • 94
    • 34648820025 scopus 로고    scopus 로고
    • Hydration of MCM-41 studied by sorption calorimetry
    • DOI 10.1021/jp072474r
    • V. Kocherbitov, and V. Alfredsson Hydration of MCM-41 studied by sorption calorimetry J Phys Chem C 111 2007 12906 12913 (Pubitemid 47459186)
    • (2007) Journal of Physical Chemistry C , vol.111 , Issue.35 , pp. 12906-12913
    • Kocherbitov, V.1    Alfredsson, V.2
  • 96
    • 84880113060 scopus 로고    scopus 로고
    • Conformational changes of enzymes upon immobilisation
    • F. Secundo Conformational changes of enzymes upon immobilisation Chem Soc Rev 42 2013 6250 6261
    • (2013) Chem Soc Rev , vol.42 , pp. 6250-6261
    • Secundo, F.1
  • 99
    • 70450263338 scopus 로고    scopus 로고
    • Probing mechanisms for enzymatic activity enhancement of organophosphorus hydrolase in functionalized mesoporous silica
    • B. Chen, C. Lei, Y. Shin, and J. Liu Probing mechanisms for enzymatic activity enhancement of organophosphorus hydrolase in functionalized mesoporous silica Biochem Biophys Res Commun 390 2009 1177 1181
    • (2009) Biochem Biophys Res Commun , vol.390 , pp. 1177-1181
    • Chen, B.1    Lei, C.2    Shin, Y.3    Liu, J.4
  • 100
    • 80052158470 scopus 로고    scopus 로고
    • Mesopores provide an amorphous state suitable for studying biomolecular structures at cryogenic temperatures
    • Y.-W. Huang, Y.-C. Lai, C.-J. Tsai, and Y.-W. Chiang Mesopores provide an amorphous state suitable for studying biomolecular structures at cryogenic temperatures Proc Natl Acad Sci U S A 108 2011 14145 14150
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14145-14150
    • Huang, Y.-W.1    Lai, Y.-C.2    Tsai, C.-J.3    Chiang, Y.-W.4
  • 101
    • 84860710932 scopus 로고    scopus 로고
    • Highly efficient immobilization of beta-lactoglobulin in functionalized mesoporous nanoparticles: A simple and useful approach for enhancement of protein stability
    • M. Falahati, A.A. Saboury, A. Shafiee, S.M. Sorkhabadi, E. Kachooei, and L. Ma'mani et al. Highly efficient immobilization of beta-lactoglobulin in functionalized mesoporous nanoparticles: a simple and useful approach for enhancement of protein stability Biophys Chem 165-166 2012 13 20
    • (2012) Biophys Chem , vol.165-166 , pp. 13-20
    • Falahati, M.1    Saboury, A.A.2    Shafiee, A.3    Sorkhabadi, S.M.4    Kachooei, E.5    Ma'Mani, L.6
  • 102
    • 84857559438 scopus 로고    scopus 로고
    • Enzyme structure and catalytic properties affected by the surface functional groups of mesoporous silica
    • K. Murai, T. Nonoyama, T. Saito, and K. Kato Enzyme structure and catalytic properties affected by the surface functional groups of mesoporous silica Catal Sci Technol 2 2012 310 315
    • (2012) Catal Sci Technol , vol.2 , pp. 310-315
    • Murai, K.1    Nonoyama, T.2    Saito, T.3    Kato, K.4
  • 103
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • J.T. Vivian, and P.R. Callis Mechanisms of tryptophan fluorescence shifts in proteins Biophys J 80 2001 2093 2109 (Pubitemid 32401976)
    • (2001) Biophysical Journal , vol.80 , Issue.5 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 104
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • M. Jackson, and H.H. Mantsch The use and misuse of FTIR spectroscopy in the determination of protein structure Crit Rev Biochem Mol Biol 30 1995 95 120
    • (1995) Crit Rev Biochem Mol Biol , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 105
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • DOI 10.1111/j.1745-7270.2007.00320.x
    • J. Kong, and S. Yu Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochim Biophys Sin 39 2007 549 559 (Pubitemid 47293710)
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , Issue.8 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 106
    • 2942700166 scopus 로고    scopus 로고
    • Adsorption of lysozyme over mesoporous molecular sieves MCM-41 and SBA-15: Influence of pH and aluminum incorporation
    • A. Vinu, V. Murugesan, and M. Hartmann Adsorption of lysozyme over mesoporous molecular sieves MCM-41 and SBA-15: influence of pH and aluminum incorporation J Phys Chem B 108 2004 7323 7330
    • (2004) J Phys Chem B , vol.108 , pp. 7323-7330
    • Vinu, A.1    Murugesan, V.2    Hartmann, M.3
  • 107
  • 108
    • 79952936113 scopus 로고    scopus 로고
    • Effects of surface curvature and surface chemistry on the structure and activity of proteins adsorbed in nanopores
    • L.C. Sang, and M.O. Coppens Effects of surface curvature and surface chemistry on the structure and activity of proteins adsorbed in nanopores Phys Chem Chem Phys 13 2011 6689 6698
    • (2011) Phys Chem Chem Phys , vol.13 , pp. 6689-6698
    • Sang, L.C.1    Coppens, M.O.2
  • 109
    • 34250793864 scopus 로고    scopus 로고
    • Enantioselective transacetylation of (R, S)-beta-citronellol by propanol rinsed immobilized Rhizomucor miehei lipase
    • A.B. Majumder, S. Shah, and M.N. Gupta Enantioselective transacetylation of (R, S)-beta-citronellol by propanol rinsed immobilized Rhizomucor miehei lipase Chem Cent J 1 2007
    • (2007) Chem Cent J , vol.1
    • Majumder, A.B.1    Shah, S.2    Gupta, M.N.3
  • 110
    • 0037183064 scopus 로고    scopus 로고
    • Spectroscopic characterization of nonnative conformational states of cytochrome c
    • DOI 10.1021/jp013841g
    • S. Oellerich, H. Wackerbarth, and P. Hildebrandt Spectroscopic characterization of nonnative conformational states of cytochrome c J Phys Chem B 106 2002 6566 6580 (Pubitemid 35289249)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.25 , pp. 6566-6580
    • Oellerich, S.1    Wackerbarth, H.2    Hildebrandt, P.3
  • 111
    • 0037173849 scopus 로고    scopus 로고
    • Mechanistic and structural features of protein adsorption onto mesoporous silicates
    • DOI 10.1021/jp0139484
    • J. Deere, E. Magner, J.G. Wall, and B.K. Hodnett Mechanistic and structural features of protein adsorption onto mesoporous silicates J Phys Chem B 106 2002 7340 7347 (Pubitemid 35383062)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.29 , pp. 7340-7347
    • Deere, J.1    Magner, E.2    Wall, J.G.3    Hodnett, B.K.4
  • 112
    • 0041508717 scopus 로고    scopus 로고
    • Oxidation of ABTS by silicate-immobilized cytochrome c in nonaqueous solutions
    • DOI 10.1021/bp0340537
    • J. Deere, E. Magner, J.G. Wall, and B.K. Hodnett Oxidation of ABTS by silicate-immobilized cytochrome c in nonaqueous solutions Biotechnol Prog 19 2003 1238 1243 (Pubitemid 37007605)
    • (2003) Biotechnology Progress , vol.19 , Issue.4 , pp. 1238-1243
    • Deere, J.1    Magner, E.2    Wall, J.G.3    Hodnett, B.K.4
  • 113
    • 84878824455 scopus 로고    scopus 로고
    • Understanding the pH-dependent immobilization efficacy of feruloyl esterase-C on mesoporous silica and its structure-activity changes
    • C. Thörn, D.B.R.K.G. Udatha, H. Zhou, P. Christakopoulos, E. Topakas, and L. Olsson Understanding the pH-dependent immobilization efficacy of feruloyl esterase-C on mesoporous silica and its structure-activity changes J Mol Catal B: Enzym 93 2013 65 72
    • (2013) J Mol Catal B: Enzym , vol.93 , pp. 65-72
    • Thörn, C.1    Udatha, D.B.R.K.G.2    Zhou, H.3    Christakopoulos, P.4    Topakas, E.5    Olsson, L.6
  • 114
    • 33646597782 scopus 로고    scopus 로고
    • Nanotube confinement denatures protein helices
    • DOI 10.1021/ja060917j
    • E.J. Sorin, and V.S. Pande Nanotube confinement denatures protein helices J Am Chem Soc 128 2006 6316 6317 (Pubitemid 43727259)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.19 , pp. 6316-6317
    • Sorin, E.J.1    Pande, V.S.2
  • 115
    • 79959394350 scopus 로고    scopus 로고
    • Simulations of the confinement of ubiquitin in self-assembled reverse micelles
    • J.H. Tian, and A.E. Garcia Simulations of the confinement of ubiquitin in self-assembled reverse micelles J Chem Phys 134 2011 11
    • (2011) J Chem Phys , vol.134 , pp. 11
    • Tian, J.H.1    Garcia, A.E.2
  • 116
    • 77956074837 scopus 로고    scopus 로고
    • Adsorption mechanism of ribosomal protein L2 onto a silica surface: A molecular dynamics simulation study
    • R. Tosaka, H. Yamamoto, I. Ohdomari, and T. Watanabe Adsorption mechanism of ribosomal protein L2 onto a silica surface: a molecular dynamics simulation study Langmuir 26 2010 9950 9955
    • (2010) Langmuir , vol.26 , pp. 9950-9955
    • Tosaka, R.1    Yamamoto, H.2    Ohdomari, I.3    Watanabe, T.4
  • 117
    • 79952925096 scopus 로고    scopus 로고
    • Enhanced initial protein adsorption on engineered nanostructured cubic zirconia
    • R.F. Sabirianov, A. Rubinstein, and F. Namavar Enhanced initial protein adsorption on engineered nanostructured cubic zirconia Phys Chem Chem Phys 13 2011 6597 6609
    • (2011) Phys Chem Chem Phys , vol.13 , pp. 6597-6609
    • Sabirianov, R.F.1    Rubinstein, A.2    Namavar, F.3
  • 119
    • 84859889749 scopus 로고    scopus 로고
    • basic2: Design of a heterogeneous D-amino acid oxidase catalyst on porous glass
    • basic2: design of a heterogeneous D-amino acid oxidase catalyst on porous glass Biotechnol Bioeng 109 2012 1490 1498
    • (2012) Biotechnol Bioeng , vol.109 , pp. 1490-1498
    • Bolivar, J.M.1    Nidetzky, B.2
  • 120
    • 77953439471 scopus 로고    scopus 로고
    • Confined polar mixtures within cylindrical nanocavities
    • J. Rodriguez, M.D. Elola, and D. Laria Confined polar mixtures within cylindrical nanocavities J Phys Chem B 114 2010 7900 7908
    • (2010) J Phys Chem B , vol.114 , pp. 7900-7908
    • Rodriguez, J.1    Elola, M.D.2    Laria, D.3
  • 121
    • 75649140553 scopus 로고    scopus 로고
    • The role of nonbonded interactions in the conformational dynamics of organophosphorous hydrolase adsorbed onto functionalized mesoporous silica surfaces
    • D.E.B. Gomes, R.D. Lins, P.G. Pascutti, C.H. Lei, and T.A. Soares The role of nonbonded interactions in the conformational dynamics of organophosphorous hydrolase adsorbed onto functionalized mesoporous silica surfaces J Phys Chem B 114 2010 531 540
    • (2010) J Phys Chem B , vol.114 , pp. 531-540
    • Gomes, D.E.B.1    Lins, R.D.2    Pascutti, P.G.3    Lei, C.H.4    Soares, T.A.5
  • 123
    • 0034736430 scopus 로고    scopus 로고
    • A new support for the immobilization of penicillin acylase
    • J. He, X. Li, D.G. Evans, X. Duan, and C. Li A new support for the immobilization of penicillin acylase J Mol Catal B: Enzym 11 2000 45 53
    • (2000) J Mol Catal B: Enzym , vol.11 , pp. 45-53
    • He, J.1    Li, X.2    Evans, D.G.3    Duan, X.4    Li, C.5
  • 124
    • 65249180872 scopus 로고    scopus 로고
    • Affinity scale for the interaction of amino acids with silica surfaces
    • A. Rimola, M. Sodupe, and P. Ugliengo Affinity scale for the interaction of amino acids with silica surfaces J Phys Chem C 113 2009 5741 5750
    • (2009) J Phys Chem C , vol.113 , pp. 5741-5750
    • Rimola, A.1    Sodupe, M.2    Ugliengo, P.3
  • 125
    • 55149112609 scopus 로고    scopus 로고
    • DFT study of the adsorption of microsolvated glycine on a hydrophilic amorphous silica surface
    • D. Costa, A. Tougerti, F. Tielens, C. Gervais, L. Stievano, and J.F. Lambert DFT study of the adsorption of microsolvated glycine on a hydrophilic amorphous silica surface Phys Chem Chem Phys 10 2008 6360 6368
    • (2008) Phys Chem Chem Phys , vol.10 , pp. 6360-6368
    • Costa, D.1    Tougerti, A.2    Tielens, F.3    Gervais, C.4    Stievano, L.5    Lambert, J.F.6
  • 126
    • 84877757895 scopus 로고    scopus 로고
    • Silica surface features and their role in the adsorption of biomolecules: Computational modeling and experiments
    • A. Rimola, D. Costa, M. Sodupe, J.-F. Lambert, and P. Ugliengo Silica surface features and their role in the adsorption of biomolecules: computational modeling and experiments Chem Rev 113 2013 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
  • 127
    • 84865692560 scopus 로고    scopus 로고
    • Dynamic deuterium magic angle spinning NMR of a molecule grafted at the inner surface of a mesoporous material
    • S. Jayanthi, V. Frydman, and S. Vega Dynamic deuterium magic angle spinning NMR of a molecule grafted at the inner surface of a mesoporous material J Phys Chem B 116 2012 10398 10405
    • (2012) J Phys Chem B , vol.116 , pp. 10398-10405
    • Jayanthi, S.1    Frydman, V.2    Vega, S.3
  • 128
    • 77953819767 scopus 로고    scopus 로고
    • A deuterium MAS NMR study of the local mobility of dissolved methionine and di-alanine at the inner surface of SBA-15
    • T. Amitay-Rosen, and S. Vega A deuterium MAS NMR study of the local mobility of dissolved methionine and di-alanine at the inner surface of SBA-15 Phys Chem Chem Phys 12 2010 6763 6773
    • (2010) Phys Chem Chem Phys , vol.12 , pp. 6763-6773
    • Amitay-Rosen, T.1    Vega, S.2
  • 129
    • 68349098894 scopus 로고    scopus 로고
    • Assigning large proteins in the solid state: A MAS NMR resonance assignment strategy using selectively and extensively C-13-labelled proteins
    • V.A. Higman, J. Flinders, M. Hiller, S. Jehle, S. Markovic, and S. Fiedler et al. Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively C-13-labelled proteins J Biomol NMR 44 2009 245 260
    • (2009) J Biomol NMR , vol.44 , pp. 245-260
    • Higman, V.A.1    Flinders, J.2    Hiller, M.3    Jehle, S.4    Markovic, S.5    Fiedler, S.6
  • 130
    • 74549115462 scopus 로고    scopus 로고
    • Biocatalysis with enzymes immobilized on mesoporous hosts: The status quo and future trends
    • M. Hartmann, and D. Jung Biocatalysis with enzymes immobilized on mesoporous hosts: the status quo and future trends J Mater Chem 20 2010 844 857
    • (2010) J Mater Chem , vol.20 , pp. 844-857
    • Hartmann, M.1    Jung, D.2
  • 132
    • 77649231779 scopus 로고    scopus 로고
    • Encapsulation of fluorescent proteins in folded-sheet mesoporous materials: Effect of pore size on energy-transfer efficiency
    • S.-i. Matsuura, T. Itoh, R. Ishii, T. Tsunoda, K. Sakaguchi, and T. Hanaoka et al. Encapsulation of fluorescent proteins in folded-sheet mesoporous materials: effect of pore size on energy-transfer efficiency Microporous Mesoporous Mater 131 2010 245 251
    • (2010) Microporous Mesoporous Mater , vol.131 , pp. 245-251
    • Matsuura, S.-I.1    Itoh, T.2    Ishii, R.3    Tsunoda, T.4    Sakaguchi, K.5    Hanaoka, T.6
  • 135
    • 79953766596 scopus 로고    scopus 로고
    • Solvation dynamics and proton transfer in nanoconfined liquids
    • W.H. Thompson Solvation dynamics and proton transfer in nanoconfined liquids Annu Rev Phys Chem 62 2011 599 619
    • (2011) Annu Rev Phys Chem , vol.62 , pp. 599-619
    • Thompson, W.H.1
  • 136
    • 84875241247 scopus 로고    scopus 로고
    • Shine a light on immobilized enzymes: Real-time sensing in solid supported biocatalysts
    • J.M. Bolivar, T. Consolati, T. Mayr, and B. Nidetzky Shine a light on immobilized enzymes: real-time sensing in solid supported biocatalysts Trends Biotechnol 31 2013 194 203
    • (2013) Trends Biotechnol , vol.31 , pp. 194-203
    • Bolivar, J.M.1    Consolati, T.2    Mayr, T.3    Nidetzky, B.4
  • 137
    • 42049123035 scopus 로고    scopus 로고
    • Microdomain pH gradient and kinetics inside composite polymeric membranes of pH and glucose sensitivity
    • H.Y. Huang, J. Shaw, C. Yip, and X.Y. Wu Microdomain pH gradient and kinetics inside composite polymeric membranes of pH and glucose sensitivity Pharm Res 25 2008 1150 1157
    • (2008) Pharm Res , vol.25 , pp. 1150-1157
    • Huang, H.Y.1    Shaw, J.2    Yip, C.3    Wu, X.Y.4
  • 138
    • 44749089037 scopus 로고    scopus 로고
    • Model discrimination for the propionic acid diffusion into hydrogel beads using lifetime confocal laser scanning microscopy
    • A.C. Spiess, M. Zavrel, M.B. Ansorge-Schumacher, C. Janzen, C. Michalik, and T.W. Schmidt et al. Model discrimination for the propionic acid diffusion into hydrogel beads using lifetime confocal laser scanning microscopy Chem Eng Sci 63 2008 3457 3465
    • (2008) Chem Eng Sci , vol.63 , pp. 3457-3465
    • Spiess, A.C.1    Zavrel, M.2    Ansorge-Schumacher, M.B.3    Janzen, C.4    Michalik, C.5    Schmidt, T.W.6
  • 139
    • 0348110620 scopus 로고    scopus 로고
    • New insights in the spatially resolved dynamic pH measurement in macroscopic large absorbent particles by confocal laser scanning microscopy
    • DOI 10.1016/j.chroma.2003.09.065
    • M. Heinemann, U. Limper, and J. Buchs New insights in the spatially resolved dynamic pH measurement in macroscopic large absorbent particles by confocal laser scanning microscopy J Chromatogr A 1024 2004 45 53 (Pubitemid 37532534)
    • (2004) Journal of Chromatography A , vol.1024 , Issue.1-2 , pp. 45-53
    • Heinemann, M.1    Limper, U.2    Buchs, J.3
  • 140
    • 79954515258 scopus 로고    scopus 로고
    • Acid-base equilibria inside amine-functionalized mesoporous silica
    • A. Yamaguchi, M. Namekawa, T. Kamijo, T. Itoh, and N. Teramae Acid-base equilibria inside amine-functionalized mesoporous silica Anal Chem 83 2011 2939 2946
    • (2011) Anal Chem , vol.83 , pp. 2939-2946
    • Yamaguchi, A.1    Namekawa, M.2    Kamijo, T.3    Itoh, T.4    Teramae, N.5
  • 141
    • 82455188696 scopus 로고    scopus 로고
    • Phenylboronic acid functionalized SBA-15 for sugar capture
    • Y.H. Zhao, and D.F. Shantz Phenylboronic acid functionalized SBA-15 for sugar capture Langmuir 27 2011 14554 14562
    • (2011) Langmuir , vol.27 , pp. 14554-14562
    • Zhao, Y.H.1    Shantz, D.F.2
  • 142
    • 4644332696 scopus 로고    scopus 로고
    • Protein encapsulation in mesoporous silicate: The effects of confinement on protein stability, hydration, and volumetric properties
    • DOI 10.1021/ja046900n
    • R. Ravindra, Z. Shuang, H. Gies, and R. Winter Protein encapsulation in mesoporous silicate: the effects of confinement on protein stability, hydration, and volumetric properties J Am Chem Soc 126 2004 12224 12225 (Pubitemid 39304879)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.39 , pp. 12224-12225
    • Ravindra, R.1    Zhao, S.2    Gies, H.3    Winter, R.4
  • 143
    • 0000308862 scopus 로고
    • Neues Verfahren zur maßanalytischen Bestimmung des Wassergehaltes von Flüssigkeiten und festen Körpern
    • K. Fischer Neues Verfahren zur maßanalytischen Bestimmung des Wassergehaltes von Flüssigkeiten und festen Körpern Angew Chem 48 1935 394 396
    • (1935) Angew Chem , vol.48 , pp. 394-396
    • Fischer, K.1
  • 144
    • 34948830089 scopus 로고    scopus 로고
    • Structural and dynamical properties of guest molecules confined in mesoporous silica materials revealed by NMR
    • G. Buntkowsky, H. Breitzke, A. Adamczyk, F. Roelofs, T. Emmler, and E. Gedat et al. Structural and dynamical properties of guest molecules confined in mesoporous silica materials revealed by NMR Phys Chem Chem Phys 9 2007 4843 4853
    • (2007) Phys Chem Chem Phys , vol.9 , pp. 4843-4853
    • Buntkowsky, G.1    Breitzke, H.2    Adamczyk, A.3    Roelofs, F.4    Emmler, T.5    Gedat, E.6
  • 145
    • 9244244180 scopus 로고    scopus 로고
    • Hydrogen bonding of water confined in mesoporous silica MCM-41 and SBA-15 studied by H-1 solid-state NMR
    • B. Grunberg, T. Emmler, E. Gedat, J. Shenderovich, G.H. Findenegg, and H.H. Limbach et al. Hydrogen bonding of water confined in mesoporous silica MCM-41 and SBA-15 studied by H-1 solid-state NMR Chem Eur J 10 2004 5689 5696
    • (2004) Chem Eur J , vol.10 , pp. 5689-5696
    • Grunberg, B.1    Emmler, T.2    Gedat, E.3    Shenderovich, J.4    Findenegg, G.H.5    Limbach, H.H.6
  • 147
    • 15444373775 scopus 로고    scopus 로고
    • Phase separation behavior of poly(methyl methacrylate-co- dimethylaminoethyl methacrylate)/methyl silsesquioxane hybrid nanocomposites studied by dansyl fluorescence
    • DOI 10.1021/cm048774s
    • Q.R. Huang, C.W. Frank, D. Mecerreyes, W. Volksen, and R.D. Miller Phase separation behavior of poly(methyl methacrylate-co-dimethylaminoethyl methacrylate)/methyl silsesquioxane hybrid nanocomposites studied by dansyl fluorescence Chem Mater 17 2005 1521 1528 (Pubitemid 40395721)
    • (2005) Chemistry of Materials , vol.17 , Issue.6 , pp. 1521-1528
    • Huang, Q.R.1    Frank, C.W.2    Mecerreyes, D.3    Volksen, W.4    Miller, R.D.5
  • 148
    • 57149138579 scopus 로고    scopus 로고
    • Solvation dynamics of Coumarin 153 in alcohols confined in silica nanochannels
    • T. Kamijo, A. Yamaguchi, S. Suzuki, N. Teramae, T. Itoh, and T. Ikeda Solvation dynamics of Coumarin 153 in alcohols confined in silica nanochannels J Phys Chem A 112 2008 11535 11542
    • (2008) J Phys Chem A , vol.112 , pp. 11535-11542
    • Kamijo, T.1    Yamaguchi, A.2    Suzuki, S.3    Teramae, N.4    Itoh, T.5    Ikeda, T.6
  • 149
    • 84861027953 scopus 로고    scopus 로고
    • Solvation and spectra of a charge transfer solute in ethanol confined within nanoscale silica pores
    • A.A. Vartia, and W.H. Thompson Solvation and spectra of a charge transfer solute in ethanol confined within nanoscale silica pores J Phys Chem B 116 2012 5414 5424
    • (2012) J Phys Chem B , vol.116 , pp. 5414-5424
    • Vartia, A.A.1    Thompson, W.H.2
  • 150
    • 80855128907 scopus 로고    scopus 로고
    • Structure and dynamics of water confined in silica nanopores
    • A.A. Milischuk, and B.M. Ladanyi Structure and dynamics of water confined in silica nanopores J Chem Phys 135 2011
    • (2011) J Chem Phys , vol.135
    • Milischuk, A.A.1    Ladanyi, B.M.2
  • 151
    • 0033944466 scopus 로고    scopus 로고
    • Water in enzyme reactions: Biophysical aspects of hydration-dehydration processes
    • Y. Pocker Water in enzyme reactions: biophysical aspects of hydration-dehydration processes Cell Mol Life Sci 57 2000 1008 1017 (Pubitemid 30496582)
    • (2000) Cellular and Molecular Life Sciences , vol.57 , Issue.7 , pp. 1008-1017
    • Pocker, Y.1
  • 152
    • 3042728278 scopus 로고    scopus 로고
    • Importance of water activity for enzyme catalysis in non-aqueous organic systems
    • M.N. Gupta, Birkhäuser Verlag Basel, Switzerland
    • T. Anthonsen, and B.J. Sjursnes Importance of water activity for enzyme catalysis in non-aqueous organic systems M.N. Gupta, Methods in non-aqueous enzymology 2000 Birkhäuser Verlag Basel, Switzerland 14 35
    • (2000) Methods in Non-aqueous Enzymology , pp. 14-35
    • Anthonsen, T.1    Sjursnes, B.J.2
  • 154
    • 34250731857 scopus 로고    scopus 로고
    • Molecular simulation of the phase behavior of water confined in silica nanopores
    • DOI 10.1021/jp067380g
    • K. Shirono, and H. Daiguji Molecular simulation of the phase behavior of water confined in silica nanopores J Phys Chem C 111 2007 7938 7946 (Pubitemid 46955486)
    • (2007) Journal of Physical Chemistry C , vol.111 , Issue.22 , pp. 7938-7946
    • Shirono, K.1    Daiguji, H.2
  • 155
    • 70449556521 scopus 로고    scopus 로고
    • Dynamic behavior of interfacial water at the silica surface
    • D. Argyris, D.R. Cole, and A. Striolo Dynamic behavior of interfacial water at the silica surface J Phys Chem C 113 2009 19591 19600
    • (2009) J Phys Chem C , vol.113 , pp. 19591-19600
    • Argyris, D.1    Cole, D.R.2    Striolo, A.3
  • 156
    • 27144463970 scopus 로고    scopus 로고
    • Pressure dependence of fragile-to-strong transition and a possible second critical point in supercooled confined water
    • L. Liu, S.H. Chen, A. Faraone, C.W. Yen, and C.Y. Mou Pressure dependence of fragile-to-strong transition and a possible second critical point in supercooled confined water Phys Rev Lett 95 2005
    • (2005) Phys Rev Lett , vol.95
    • Liu, L.1    Chen, S.H.2    Faraone, A.3    Yen, C.W.4    Mou, C.Y.5
  • 157
    • 84879725487 scopus 로고    scopus 로고
    • ESR study of interfacial hydration layers of polypeptides in water-filled nanochannels and in vitrified bulk solvents
    • Y.-C. Lai, Y.-F. Chen, and Y.-W. Chiang ESR study of interfacial hydration layers of polypeptides in water-filled nanochannels and in vitrified bulk solvents PLoS One 8 2013
    • (2013) PLoS One , vol.8
    • Lai, Y.-C.1    Chen, Y.-F.2    Chiang, Y.-W.3
  • 158
    • 79952577718 scopus 로고    scopus 로고
    • Post-synthetic activation of silanol covering in the mesostructured silicate materials MCM-41 and SBA-15
    • S.A. Kozlova, and S.D. Kirik Post-synthetic activation of silanol covering in the mesostructured silicate materials MCM-41 and SBA-15 Microporous Mesoporous Mater 133 2010 124 133
    • (2010) Microporous Mesoporous Mater , vol.133 , pp. 124-133
    • Kozlova, S.A.1    Kirik, S.D.2
  • 159
    • 35348959431 scopus 로고    scopus 로고
    • 1H MAS NMR
    • DOI 10.1016/j.micromeso.2007.02.030, PII S1387181107001096
    • Y.K. Bae, and O.H. Han Removal of copolymer template from SBA-15 studied by H-1 MAS NMR Microporous Mesoporous Mater 106 2007 304 307 (Pubitemid 47600069)
    • (2007) Microporous and Mesoporous Materials , vol.106 , Issue.1-3 , pp. 304-307
    • Bae, Y.K.1    Han, O.H.2
  • 160
    • 18844407024 scopus 로고    scopus 로고
    • Simultaneous removal of copolymer template from SBA-15 in the crystallization process
    • DOI 10.1016/j.micromeso.2005.01.023, PII S1387181105000600
    • L.M. Yang, Y.J. Wang, G.S. Luo, and Y.Y. Dai Simultaneous removal of copolymer template from SBA-15 in the crystallization process Microporous Mesoporous Mater 81 2005 107 114 (Pubitemid 40688520)
    • (2005) Microporous and Mesoporous Materials , vol.81 , Issue.1-3 , pp. 107-114
    • Yang, L.M.1    Wang, Y.J.2    Luo, G.S.3    Dai, Y.Y.4
  • 161
    • 0034634766 scopus 로고    scopus 로고
    • The surface chemistry of amorphous silica. Zhuravlev model
    • L.T. Zhuravlev The surface chemistry of amorphous silica. Zhuravlev model Colloids Surf A 173 2000 1 38
    • (2000) Colloids Surf A , vol.173 , pp. 1-38
    • Zhuravlev, L.T.1
  • 162
    • 84870878650 scopus 로고    scopus 로고
    • Quantification of silanol sites for the most common mesoporous ordered silicas and organosilicas: Total versus accessible silanols
    • M. Ide, M. El-Roz, E. De Canck, A. Vicente, T. Planckaert, and T. Bogaerts et al. Quantification of silanol sites for the most common mesoporous ordered silicas and organosilicas: total versus accessible silanols Phys Chem Chem Phys 15 2013 642 650
    • (2013) Phys Chem Chem Phys , vol.15 , pp. 642-650
    • Ide, M.1    El-Roz, M.2    De Canck, E.3    Vicente, A.4    Planckaert, T.5    Bogaerts, T.6
  • 163
    • 39849105068 scopus 로고    scopus 로고
    • Synthesis of functionalized SBA-15 with ordered large pore size and its adsorption properties of BSA
    • DOI 10.1016/j.micromeso.2007.06.054, PII S1387181107004076
    • T.P.B. Nguyen, J.-W. Lee, W.G. Shim, and H. Moon Synthesis of functionalized SBA-15 with ordered large pore size and its adsorption properties of BSA Microporous Mesoporous Mater 110 2008 560 569 (Pubitemid 351318355)
    • (2008) Microporous and Mesoporous Materials , vol.110 , Issue.2-3 , pp. 560-569
    • Nguyen, T.P.B.1    Lee, J.-W.2    Shim, W.G.3    Moon, H.4
  • 164
    • 0035361948 scopus 로고    scopus 로고
    • Immobilized enzymes in ordered mesoporous silica materials and improvement of their stability and catalytic activity in an organic solvent
    • DOI 10.1016/S1387-1811(01)00257-8, PII S1387181101002578, Proceedings of the 2nd ISMMS
    • H. Takahashi, B. Li, T. Sasaki, C. Miyazaki, T. Kajino, and S. Inagaki Immobilized enzymes in ordered mesoporous silica materials and improvement of their stability and catalytic activity in an organic solvent Microporous Mesoporous Mater 44 2001 755 762 (Pubitemid 32657177)
    • (2001) Microporous and Mesoporous Materials , vol.44-45 , pp. 755-762
    • Takahashi, H.1    Li, B.2    Sasaki, T.3    Miyazaki, C.4    Kajino, T.5    Inagaki, S.6
  • 165
    • 0018101119 scopus 로고
    • Characterization of proteins and other macromolecules by agarose gel chromatography
    • I. Axelsson Characterization of proteins and other macromolecules by agarose gel chromatography J Chromatogr 152 1978 21 32 (Pubitemid 8331723)
    • (1978) Journal of Chromatography , vol.152 , Issue.1 , pp. 21-32
    • Axelsson, I.1
  • 166
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • D.K. Wilkins, S.B. Grimshaw, V. Receveur, C.M. Dobson, J.A. Jones, and L.J. Smith Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques Biochemistry 38 1999 16424 16431
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 167
    • 30544434195 scopus 로고
    • Covalent linkage of glucose oxidase on modified glassy carbon electrodes. Kinetic phenomena
    • C. Bourdillon, J.P. Bourgeois, and D. Thomas Covalent linkage of glucose oxidase on modified glassy carbon electrodes. Kinetic phenomena J Am Chem Soc 102 1980 4231 4235
    • (1980) J Am Chem Soc , vol.102 , pp. 4231-4235
    • Bourdillon, C.1    Bourgeois, J.P.2    Thomas, D.3
  • 168
    • 0023530081 scopus 로고
    • The 3.0 Å crystal structure of xylose isomerase from Streptomyces olivochromogenes
    • G.K. Farber, G.A. Petsko, and D. Ringe The 3.0 Å crystal structure of xylose isomerase from Streptomyces olivochromogenes Protein Eng 1 1987 459 466
    • (1987) Protein Eng , vol.1 , pp. 459-466
    • Farber, G.K.1    Petsko, G.A.2    Ringe, D.3
  • 169
    • 0025604724 scopus 로고
    • Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and Frit-FAB LC/MS
    • K. Hirayama, S. Akashi, M. Furuya, and K.-i. Fukuhara Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and Frit-FAB LC/MS Biochem Biophys Res Commun 173 1990 639 646
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 639-646
    • Hirayama, K.1    Akashi, S.2    Furuya, M.3    Fukuhara, K.-I.4
  • 170
    • 20644467753 scopus 로고    scopus 로고
    • Glucose isomerase from Streptomyces rubiginosus - Potential molecular weight standard for small-angle X-ray scattering
    • DOI 10.1107/S0021889805010472
    • M. Kozak Glucose isomerase from Streptomyces rubiginosus - potential molecular weight standard for small-angle X-ray scattering J Appl Crystallogr 38 2005 555 558 (Pubitemid 40836343)
    • (2005) Journal of Applied Crystallography , vol.38 , Issue.3 , pp. 555-558
    • Kozak, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.