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Volumn 63, Issue , 2012, Pages 180-186

Structural behavior of Candida antarctica lipase B in water and supercritical carbon dioxide: A molecular dynamic simulation study

Author keywords

Lipase B; Molecular dynamic simulation; Secondary structure; Supercritical CO 2

Indexed keywords

CANDIDA ANTARCTICA LIPASE B; CONTACT MAPS; ENZYME STRUCTURES; MOLECULAR DYNAMIC SIMULATIONS; RADIUS OF GYRATION; RANDOM COIL; ROOT MEAN SQUARE DEVIATIONS; SECONDARY STRUCTURES; STRUCTURAL BEHAVIORS; STRUCTURAL VARIATIONS; SUPERCRITICAL CARBON DIOXIDES; SUPERCRITICAL CO; TERTIARY STRUCTURES;

EID: 84857657780     PISSN: 08968446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.supflu.2011.12.010     Document Type: Article
Times cited : (46)

References (87)
  • 1
    • 0036669425 scopus 로고    scopus 로고
    • Lipases for biotechnology
    • DOI 10.1016/S0958-1669(02)00341-5
    • K.E. Jaeger, and T. Eggert Lipases for biotechnology Current Opinion in Biotechnology 13 2002 390 397 (Pubitemid 35254099)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.4 , pp. 390-397
    • Jaeger, K.-E.1    Eggert, T.2
  • 2
    • 63549102137 scopus 로고    scopus 로고
    • A review of the current state of biodiesel production using enzymatic transesterification
    • L. Fjerbaek, K.V. Christensen, and B. Norddahl A review of the current state of biodiesel production using enzymatic transesterification Biotechnology and Bioengineering 102 2009 1298 1315
    • (2009) Biotechnology and Bioengineering , vol.102 , pp. 1298-1315
    • Fjerbaek, L.1    Christensen, K.V.2    Norddahl, B.3
  • 3
    • 78649709520 scopus 로고    scopus 로고
    • Kinetic resolution of (R/S)-propranolol (1-isopropylamino-3-(1-naphtoxy)- 2-propanolol) catalyzed by immobilized preparations of Candida antarctica lipase B (CAL-B)
    • O. Barbosa, C. Ariza, C. Ortiz, and R. Torres Kinetic resolution of (R/S)-propranolol (1-isopropylamino-3-(1-naphtoxy)-2-propanolol) catalyzed by immobilized preparations of Candida antarctica lipase B (CAL-B) New Biotechnology 27 6 2010 844 850
    • (2010) New Biotechnology , vol.27 , Issue.6 , pp. 844-850
    • Barbosa, O.1    Ariza, C.2    Ortiz, C.3    Torres, R.4
  • 6
    • 0028773288 scopus 로고
    • The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
    • J. Uppenberg, M.T. Hansen, S. Patkar, and T.A. Jones The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica Structure 2 1994 293 308
    • (1994) Structure , vol.2 , pp. 293-308
    • Uppenberg, J.1    Hansen, M.T.2    Patkar, S.3    Jones, T.A.4
  • 7
    • 33744784809 scopus 로고    scopus 로고
    • Candida antarctica lipase B: An ideal biocatalyst for the preparation of nitrogenated organic compounds
    • DOI 10.1002/adsc.200606057
    • V. Gotor-Fernandez, E. Busto, and V. Gotor Candida antarctica lipase B: an ideal biocatalyst for the preparation of nitrogenated organic compounds Advanced Synthesis & Catalysis 348 2006 797 812 (Pubitemid 43829182)
    • (2006) Advanced Synthesis and Catalysis , vol.348 , Issue.7-8 , pp. 797-812
    • Gotor-Fernandez, V.1    Busto, E.2    Gotor, V.3
  • 9
    • 78650092281 scopus 로고    scopus 로고
    • Mutated variant of Candida antarctica lipase B in (S)-selective dynamic kinetic resolution of secondary alcohols
    • K. Engström, M. Vallin, P.-O. Syrén, K. Hult, and J.-E. Bäckvall Mutated variant of Candida antarctica lipase B in (S)-selective dynamic kinetic resolution of secondary alcohols Organic and Biomolecular Chemistry 9 2011 81 82
    • (2011) Organic and Biomolecular Chemistry , vol.9 , pp. 81-82
    • Engström, K.1    Vallin, M.2    Syrén, P.-O.3    Hult, K.4    Bäckvall, J.-E.5
  • 10
    • 79959407879 scopus 로고    scopus 로고
    • Rational redesign of Candida antarctica lipase B for the ring opening polymerization of d,d-lactide
    • M. Takwa, M.W. Larsen, K. Hult, and M. Martinelle Rational redesign of Candida antarctica lipase B for the ring opening polymerization of d,d-lactide Chemical Communication 47 2011 7392 7394
    • (2011) Chemical Communication , vol.47 , pp. 7392-7394
    • Takwa, M.1    Larsen, M.W.2    Hult, K.3    Martinelle, M.4
  • 11
    • 1842765645 scopus 로고    scopus 로고
    • Improved activity and thermostability of Candida antarctica lipase B by DNA family shuffling
    • DOI 10.1093/protein/gzh017
    • W.C. Suen, N. Zhang, L. Xiao, V. Madison, and A. Zaks Improved activity and thermostability of Candida antarctica lipase B by DNA family shuffling Protein Engineering Design and Selection 17 2004 133 140 (Pubitemid 38477740)
    • (2004) Protein Engineering, Design and Selection , vol.17 , Issue.2 , pp. 133-140
    • Suen, W.-C.1    Zhang, N.2    Xiao, L.3    Madison, V.4    Zaks, A.5
  • 12
    • 0035496145 scopus 로고    scopus 로고
    • Improved enantioselectivity of a lipase by rational protein engineering
    • D. Rotticci, J.C. Rotticci-Mulder, S. Denman, T. Norin, and K. Hult Improved enantioselectivity of a lipase by rational protein engineering ChemBioChem 2 2001 766 770 (Pubitemid 33722631)
    • (2001) ChemBioChem , vol.2 , Issue.10 , pp. 766-770
    • Rotticci, D.1    Rotticci-Mulder, J.C.2    Denman, S.3    Norin, T.4    Hult, K.5
  • 13
    • 60349109395 scopus 로고    scopus 로고
    • Understanding the plasticity of the alpha/beta hydrolase fold: Lid swapping on the Candida antarctica lipase B results in chimeras with interesting biocatalytic properties
    • M. Skjot, L. De Maria, R. Chatterjee, A. Svendsen, S.A. Patkar, P.R. Ostergaard, and J. Brask Understanding the plasticity of the alpha/beta hydrolase fold: lid swapping on the Candida antarctica lipase B results in chimeras with interesting biocatalytic properties ChemBioChem 10 2009 520 527
    • (2009) ChemBioChem , vol.10 , pp. 520-527
    • Skjot, M.1    De Maria, L.2    Chatterjee, R.3    Svendsen, A.4    Patkar, S.A.5    Ostergaard, P.R.6    Brask, J.7
  • 15
    • 25844525807 scopus 로고    scopus 로고
    • Improving the catalytic activity of Candida antarctica lipase B by circular permutation
    • DOI 10.1021/ja053932h
    • Z. Qian, and S. Lutz Improving the catalytic activity of Candida antarctica lipase B by circular permutation J. American Chemical Society 127 2005 13466 13467 (Pubitemid 41401178)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.39 , pp. 13466-13467
    • Qian, Z.1    Lutz, S.2
  • 16
    • 37549058473 scopus 로고    scopus 로고
    • Investigating the structural and functional consequences of circular permutation on lipase B from Candida antarctica
    • Z. Qian, C.J. Fields, and S. Lutz Investigating the structural and functional consequences of circular permutation on lipase B from Candida antarctica ChemBioChem 8 2007 1989 1996
    • (2007) ChemBioChem , vol.8 , pp. 1989-1996
    • Qian, Z.1    Fields, C.J.2    Lutz, S.3
  • 17
    • 70349255505 scopus 로고    scopus 로고
    • Structural redesign of lipase B from Candida antarctica by circular permutation and incremental truncation
    • Z. Qian, J.R. Horton, X. Cheng, and S. Lutz Structural redesign of lipase B from Candida antarctica by circular permutation and incremental truncation J. Molecular Biology 393 2009 191 201
    • (2009) J. Molecular Biology , vol.393 , pp. 191-201
    • Qian, Z.1    Horton, J.R.2    Cheng, X.3    Lutz, S.4
  • 18
    • 78649448002 scopus 로고    scopus 로고
    • Engineering of Candida antarctica lipase B for hydrolysis of bulky carboxylic acid esters
    • P.B. Juhla, K. Dodererb, F. Hollmannc, O. Thumd, and J. Pleiss Engineering of Candida antarctica lipase B for hydrolysis of bulky carboxylic acid esters J. Biotechnology 15 2010 474 480
    • (2010) J. Biotechnology , vol.15 , pp. 474-480
    • Juhla, P.B.1    Dodererb, K.2    Hollmannc, F.3    Thumd, O.4    Pleiss, J.5
  • 19
    • 73949098126 scopus 로고    scopus 로고
    • Improved triglyceride transesterification by circular permuted Candida antarctica Lipase B
    • Y. Yu, and S. Lutz Improved triglyceride transesterification by circular permuted Candida antarctica Lipase B Biotechnology and Bioengineering 105 1 2010 44 50
    • (2010) Biotechnology and Bioengineering , vol.105 , Issue.1 , pp. 44-50
    • Yu, Y.1    Lutz, S.2
  • 22
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • DOI 10.1038/nsb0902-646
    • M. Karplus, and J.A. McCammon Molecular dynamics simulations of biomolecules Nature Structural Biology 9 9 2002 646 652 (Pubitemid 34977295)
    • (2002) Nature Structural Biology , vol.9 , Issue.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 23
    • 0033988125 scopus 로고    scopus 로고
    • Solvent mobility and the protein 'glass' transition
    • DOI 10.1038/71231
    • D. Vitkup, D. Ringe, G.A. Petsko, and M. Karplus Solvent mobility and the protein glass transition Nature Structural Biology 7 2000 34 38 (Pubitemid 30043245)
    • (2000) Nature Structural Biology , vol.7 , Issue.1 , pp. 34-38
    • Vitkup, D.1    Ringe, D.2    Petsko, G.A.3    Karplus, M.4
  • 25
    • 0036267045 scopus 로고    scopus 로고
    • Enhanced enantioselectivity of lipase from Pseudomonas sp. at high temperatures and fixed water activity in the ionic liquid, 1-butyl-3- methylimidazolium bis[(trifluoromethyl)sulfonyl]amide
    • DOI 10.1023/A:1015563801977
    • M.W. Eckstein, P. Wasserscheid, and U. Kragl Enhanced enantioselectivity of lipase from Pseudomonas sp. at high temperatures and fixed water activity in the ionic liquid, 1-butyl-3 methylimidazolium bis[(trifluoromethyl)sulfonyl] amide Biotechnology Letter 24 2002 763 767 (Pubitemid 34594846)
    • (2002) Biotechnology Letters , vol.24 , Issue.10 , pp. 763-767
    • Eckstein, M.1    Wasserscheid, P.2    Kragl, U.3
  • 26
    • 0032344066 scopus 로고    scopus 로고
    • Biocatalytic esterification in supercritical carbon dioxide by using a lipid-coated lipase
    • T. Mori, A. Kobayashi, and Y. Okahata Biocatalytic esterification in supercritical carbon dioxide by using a lipid-coated lipase Chemistry Letter 1998 921 922
    • (1998) Chemistry Letter , pp. 921-922
    • Mori, T.1    Kobayashi, A.2    Okahata, Y.3
  • 27
    • 0027112426 scopus 로고
    • Biocatalytic synthesis of acrylates in organic solvents and supercritical fluids: I. Optimization of enzyme environment
    • S. Kamat, J. Barrera, E.J. Beckman, and A.J. Russell Biocatalytic synthesis of acrylates in organic solvents and supercritical fluids: I. Optimization of enzyme environment Biotechnology and Bioengineering 40 1992 158 166
    • (1992) Biotechnology and Bioengineering , vol.40 , pp. 158-166
    • Kamat, S.1    Barrera, J.2    Beckman, E.J.3    Russell, A.J.4
  • 28
    • 40949165824 scopus 로고    scopus 로고
    • Lipase-catalyzed regioselective acylation of tritylglycosides in supercritical carbon dioxide
    • C. Palocci, M. Falconi, L. Chronopoulou, and E. Cernia Lipase-catalyzed regioselective acylation of tritylglycosides in supercritical carbon dioxide J. Supercritical Fluids 8 2008 8 93
    • (2008) J. Supercritical Fluids , vol.8 , pp. 8-93
    • Palocci, C.1    Falconi, M.2    Chronopoulou, L.3    Cernia, E.4
  • 30
    • 0038645392 scopus 로고    scopus 로고
    • Control of enantioselectivity of lipase-catalyzed esterification in supercritical carbon dioxide by tuning the pressure and temperature
    • DOI 10.1016/S0957-4166(03)00431-2
    • T. Matsuda, R. Kanamaru, K. Watanabe, T. Kamitanaka, T. Harada, and K. Nakamura Control of enantioselectivity of lipase-catalyzed esterification in supercritical carbon dioxide by tuning the pressure and temperature Tetrahedron: Asymmetry 14 2003 2087 2091 (Pubitemid 36835953)
    • (2003) Tetrahedron Asymmetry , vol.14 , Issue.14 , pp. 2087-2091
    • Matsuda, T.1    Kanamaru, R.2    Watanabe, K.3    Kamitanaka, T.4    Harada, T.5    Nakamura, K.6
  • 32
    • 33947602594 scopus 로고    scopus 로고
    • Improvement of enzyme activity, stability and selectivity via immobilization techniques
    • DOI 10.1016/j.enzmictec.2007.01.018, PII S0141022907000506
    • C. Mateo, J.M. Palomo, G.G. Fernandez-Lorente, and J.M. R. Fernandez-Lafuente Improvement of enzyme activity, stability and selectivity via immobilization techniques Enzyme and Microbial Technology 40 2007 1451 1463 (Pubitemid 46482654)
    • (2007) Enzyme and Microbial Technology , vol.40 , Issue.6 , pp. 1451-1463
    • Mateo, C.1    Palomo, J.M.2    Fernandez-Lorente, G.3    Guisan, J.M.4    Fernandez-Lafuente, R.5
  • 33
    • 77953522374 scopus 로고    scopus 로고
    • Methods for stabilizing and activating enzymes in ionic liquids - A review
    • H. Zhao Methods for stabilizing and activating enzymes in ionic liquids - a review J. Chemical Technology and Biotechnology 85 2010 891 907
    • (2010) J. Chemical Technology and Biotechnology , vol.85 , pp. 891-907
    • Zhao, H.1
  • 34
    • 58149333139 scopus 로고    scopus 로고
    • Enzymatic reactions in dense gases
    • Enzymatic reactions in dense gases J. Supercritical Fluids 47 2009 357 372
    • (2009) J. Supercritical Fluids , vol.47 , pp. 357-372
  • 35
  • 37
    • 33947307011 scopus 로고    scopus 로고
    • Lipase-catalyzed long chain fatty ester synthesis in dense carbon dioxide: Kinetics and thermodynamics
    • DOI 10.1016/j.supflu.2006.08.011, PII S0896844606002233
    • C.G. Laudani, M. Habulin, Z. Kneza, G.D. Porta, and E. Reverchon Lipase-catalyzed long chain fatty ester synthesis in dense carbon dioxide: kinetics and thermodynamics J. Supercritical Fluids 41 2007 92 101 (Pubitemid 46441769)
    • (2007) Journal of Supercritical Fluids , vol.41 , Issue.1 , pp. 92-101
    • Laudani, C.G.1    Habulin, M.2    Knez, Z.3    Porta, G.D.4    Reverchon, E.5
  • 38
    • 0000137876 scopus 로고    scopus 로고
    • Molecular dynamics of microperoxidases in aqueous and nonaqueous solutions
    • S. Melchionna, M. Barteri, and G. Ciccotti Molecular dynamics of microperoxidases in aqueous and nonaqueous solutions J. Physical Chemistry 100 1996 19241 19250 (Pubitemid 126786952)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.50 , pp. 19241-19250
    • Melchionna, S.1    Barteri, M.2    Ciccotti, G.3
  • 39
    • 45949094932 scopus 로고    scopus 로고
    • Molecular dynamics study of triosephosphate isomerase from Trypanosoma cruzi in water/decane mixtures
    • N. Diaz-Vergara, and A. Pineiro Molecular dynamics study of triosephosphate isomerase from Trypanosoma cruzi in water/decane mixtures J. Physical Chemistry B 112 2008 3529 3539
    • (2008) J. Physical Chemistry B , vol.112 , pp. 3529-3539
    • Diaz-Vergara, N.1    Pineiro, A.2
  • 40
    • 0037342275 scopus 로고    scopus 로고
    • Protein structure and dynamics in nonaqueous solvents: Insights from molecular dynamics simulation studies
    • C.M. Soares, V.H.Teixeira, and A.M. Baptista Protein structure and dynamics in nonaqueous solvents: insights from molecular dynamics simulation studies Biophysical J. 84 2003 1628 1641 (Pubitemid 36322927)
    • (2003) Biophysical Journal , vol.84 , Issue.3 , pp. 1628-1641
    • Soares, C.M.1    Teixeira, V.H.2    Baptista, A.M.3
  • 41
    • 41549135319 scopus 로고    scopus 로고
    • Protein structure and dynamics in ionic liquids. Insights from molecular dynamics simulation studies
    • DOI 10.1021/jp0766050
    • N.M. Micaelo, and C.M. Soares Protein structure and dynamics in ionic liquids. Insights from molecular dynamics simulation studies J. Physical Chemistry B 112 2008 2566 2572 (Pubitemid 351472962)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.9 , pp. 2566-2572
    • Micaelo, N.M.1    Soares, C.M.2
  • 42
    • 33748267512 scopus 로고    scopus 로고
    • Protein under pressure: Molecular dynamics simulation of the Arc Repressor
    • DOI 10.1002/prot.21034
    • D. Trzesniak, R.D. Lins, and W.F.v. Gunsteren1 Protein under pressure: molecular dynamics simulation of the arc repressor Proteins: Structure, Function, and Bioinformatics 65 2006 136 144 (Pubitemid 44320623)
    • (2006) Proteins: Structure, Function and Genetics , vol.65 , Issue.1 , pp. 136-144
    • Trzesniak, D.1    Lins, R.D.2    Van Gunsteren, W.F.3
  • 43
    • 0036286862 scopus 로고    scopus 로고
    • Orientation and conformation of a lipase at an interface studied by molecular dynamics simulations
    • M.Ø. Jensen, T.R. Jensen, K. Kjaer, T. Bjørnholm, O.G. Mouritsen, and G.H. Peters Orientation and conformation of a lipase at an interface studied by molecular dynamics simulations Biophysical J. 83 2002 98 111 (Pubitemid 34694723)
    • (2002) Biophysical Journal , vol.83 , Issue.1 , pp. 98-111
    • Jensen, M.O.1    Jensen, T.R.2    Kjaer, K.3    Bjornholm, T.4    Mouritsen, O.G.5    Peters, G.H.6
  • 44
    • 0242292035 scopus 로고    scopus 로고
    • Brute-force molecular dynamics simulations of Villin headpiece: Comparison with NMR parameters
    • D.v.d. Spoel, and E. Lindahl Brute-force molecular dynamics simulations of Villin headpiece: comparison with NMR parameters J. Physical Chemistry B 107 2003 11178 11187
    • (2003) J. Physical Chemistry B , vol.107 , pp. 11178-11187
    • Spoel, D.V.D.1    Lindahl, E.2
  • 45
    • 52349085543 scopus 로고    scopus 로고
    • Systematic comparison of empirical forcefields for molecular dynamic simulation o insulin
    • N. Todorova, F.S. Legge, H. Treutlein, and I. Yarovsky Systematic comparison of empirical forcefields for molecular dynamic simulation o insulin J. Physical Chemistry B 112 2008 11137 11146
    • (2008) J. Physical Chemistry B , vol.112 , pp. 11137-11146
    • Todorova, N.1    Legge, F.S.2    Treutlein, H.3    Yarovsky, I.4
  • 46
    • 34250312085 scopus 로고    scopus 로고
    • How sensitive are nanosecond molecular dynamics simulations of proteins to changes in the force field?
    • DOI 10.1021/jp068580v
    • A. Villa, H. Fan, T. Wassenaar, and A.E. Mark How sensitive are nanosecond molecular dynamics simulations of proteins to changes in the force field? J. Physical Chemistry B 111 2007 6015 6025 (Pubitemid 46918232)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.21 , pp. 6015-6025
    • Villa, A.1    Fan, H.2    Wassenaar, T.3    Mark, A.E.4
  • 50
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An Nlog(N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald: an Nlog(N) method for Ewald sums in large systems J. Chemical Physics 98 1993 10089 10092
    • (1993) J. Chemical Physics , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 53
    • 9744256949 scopus 로고    scopus 로고
    • Structural stability of wild type and mutated α-keratin fragments: Molecular dynamics and free energy calculations
    • DOI 10.1021/bm049788u
    • C. Danciulescu, B. Nike, and F.J. Wortmann Structural stability of wide type and mutated a-Keratin fragments: molecular dynamics and free energy calculations Biomacromolecules 5 2004 2165 2175 (Pubitemid 39585268)
    • (2004) Biomacromolecules , vol.5 , Issue.6 , pp. 2165-2175
    • Danciulescu, C.1    Nick, B.2    Wortmann, F.-J.3
  • 54
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • R. Fraczkiewicz, and W. Braun Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules J. Computational Chemistry 19 1998 319 333 (Pubitemid 128592649)
    • (1998) Journal of Computational Chemistry , vol.19 , Issue.3 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 55
    • 0037426344 scopus 로고    scopus 로고
    • Extending the structure of an ABC transporter to atomic resolution: Modeling and simulation studies of MsbA
    • DOI 10.1021/bi027337t
    • J.D. Campbell, P.C. Biggin, M. Baaden, and M.S.P. Sansom Extending the structure of an ABC transporter to atomic resolution: modeling and simulation studies of MsbA Biochemistry 42 2003 3666 3673 (Pubitemid 36406372)
    • (2003) Biochemistry , vol.42 , Issue.13 , pp. 3666-3673
    • Campbell, J.D.1    Biggin, P.C.2    Baaden, M.3    Sansom, M.S.P.4
  • 56
    • 40449100818 scopus 로고    scopus 로고
    • Modeling structure and flexibility of Candida antarctica lipase B in organic solvents
    • P. Trodler, and J. Pleiss Modeling structure and flexibility of Candida antarctica lipase B in organic solvents BMC Structural Biology 8 2008 9
    • (2008) BMC Structural Biology , vol.8 , pp. 9
    • Trodler, P.1    Pleiss, J.2
  • 57
    • 0032901423 scopus 로고    scopus 로고
    • Mechanics and dynamics of B1 domain of protein G: Role of packing and surface hydrophobic residues
    • M. Ceruso, A. Amadei, and A. Nola Mechanics and dynamics of B1 domain of protein G: role of packing and surface hydrophobic residues Protein Science 8 1999 147 160 (Pubitemid 29035528)
    • (1999) Protein Science , vol.8 , Issue.1 , pp. 147-160
    • Ceruso, M.A.1    Amadei, A.2    Di Nola, A.3
  • 58
    • 49549109406 scopus 로고    scopus 로고
    • Radius of gyration as an indicator of protein structure compactness
    • M.Y. Lobanov, N.S. Bogatyreva, and O.V. Galzitskaya Radius of gyration as an indicator of protein structure compactness Molecular Biology 42 4 2008 623 628
    • (2008) Molecular Biology , vol.42 , Issue.4 , pp. 623-628
    • Lobanov, M.Y.1    Bogatyreva, N.S.2    Galzitskaya, O.V.3
  • 59
    • 0030662088 scopus 로고    scopus 로고
    • The concept of solvent compatibility and its impact on protein stability and activity enhancement in nonaqueous solvents
    • DOI 10.1021/ja970629a
    • S. Toba, and K.M. Merz The concept of solvent compatibility and its impact on protein stability and activity enhancement in nonaqueous solvents J. American Chemical Society 119 1997 9939 9948 (Pubitemid 27478782)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.42 , pp. 9939-9948
    • Toba, S.1    Merz Jr., K.M.2
  • 60
    • 0000203019 scopus 로고    scopus 로고
    • Inactivation of Enzymes and Decomposition of α-Helix Structure by Supercritical Carbon Dioxide Microbubble Method
    • H. Ishikawa, M. Shimoda, A. Yonekura, and Y. Osajima Inactivation of enzymes and decomposition of alpha-helix structure by supercritical carbon dioxide microbubble method J. Agricultural Food Chemistry 44 1996 2646 2649 (Pubitemid 126453555)
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , Issue.9 , pp. 2646-2649
    • Ishikawa, H.1    Shimoda, M.2    Yonekura, A.3    Osajima, Y.4
  • 61
    • 0035198407 scopus 로고    scopus 로고
    • Activity and stability of lipases from different sources in supercritical carbon dioxide and near-critical propane
    • DOI 10.1002/jctb.514
    • M. Habulin, and Z. Knez Activity and stability of lipases from different sources in supercritical carbon dioxide and near-critical propane J. Chemical Technology and Biotechnology 76 2001 1260 1266 (Pubitemid 33123210)
    • (2001) Journal of Chemical Technology and Biotechnology , vol.76 , Issue.12 , pp. 1260-1266
    • Habulin, M.1    Knez, Z.2
  • 64
    • 28644433271 scopus 로고    scopus 로고
    • Inactivation and reactivation of horseradish peroxidase treated with supercritical carbon dioxide
    • DOI 10.1007/s00217-005-0152-5
    • F. Gui, Z. Wang, J. Wu, F. Chen, X. Liao, and X. Hu Inactivation and reactivation of horseradish peroxidase treated with supercritical carbon dioxide European Food Research and Technology 222 2006 105 111 (Pubitemid 41750763)
    • (2006) European Food Research and Technology , vol.222 , Issue.1-2 , pp. 105-111
    • Gui, F.1    Wang, Z.2    Wu, J.3    Chen, F.4    Liao, X.5    Hu, X.6
  • 66
    • 64549141148 scopus 로고    scopus 로고
    • Alterations in the activity and structure of pectin methylesterase treated by high pressure carbon dioxide
    • L. Zhou, J. Wu, X. Hu, X. Zhi, and X. Liao Alterations in the activity and structure of pectin methylesterase treated by high pressure carbon dioxide J. Agricultural and Food Chemistry 57 2009 1890 1895
    • (2009) J. Agricultural and Food Chemistry , vol.57 , pp. 1890-1895
    • Zhou, L.1    Wu, J.2    Hu, X.3    Zhi, X.4    Liao, X.5
  • 67
    • 59349116975 scopus 로고    scopus 로고
    • Molecular modeling and experimental verification of lipase-catalyzed enantioselective esterification of racemic naproxen in supercritical carbon dioxide
    • C.H. Kwon, J.Y. Jeong, and J.W. Kang Molecular modeling and experimental verification of lipase-catalyzed enantioselective esterification of racemic naproxen in supercritical carbon dioxide Korean J. of Chemical Engineering 26 2009 214 219
    • (2009) Korean J. of Chemical Engineering , vol.26 , pp. 214-219
    • Kwon, C.H.1    Jeong, J.Y.2    Kang, J.W.3
  • 68
    • 2942748486 scopus 로고    scopus 로고
    • Molecular dynamics simulations to determine the effect of supercritical carbon dioxide on the structural integrity of hen egg white lysozyme
    • DOI 10.1021/bp034313k
    • H.-L. Liu, W.-C. Hsieh, and H.-S. Liu Molecular dynamics simulations to determine the effect of supercritical carbon dioxide on the structural integrity of hen egg white lysozyme Biotechnology Progress 20 2004 930 938 (Pubitemid 38784034)
    • (2004) Biotechnology Progress , vol.20 , Issue.3 , pp. 930-938
    • Liu, H.-L.1    Hsieh, W.-C.2    Liu, H.-S.3
  • 69
    • 0026918456 scopus 로고
    • In situ studies of protein conformation in supercritical fluids. Trypsin in in carbon dioxide
    • J. Zagrobelny, and F.V. Bright In situ studies of protein conformation in supercritical fluids: trypsin in carbon dioxide Biotechnology Progress 8 1992 421 423 (Pubitemid 23576651)
    • (1992) Biotechnology Progress , vol.8 , Issue.5 , pp. 421-423
    • Zagrobelny JoAnn1    Bright Frank, V.2
  • 71
    • 79952740870 scopus 로고    scopus 로고
    • Aggregation and homogenization, surface charge and structural change, and inactivation of mushroom tyrosinase in an aqueous system by subcritical/supercritical carbon dioxide
    • W. Hu, Y. Zhang, Y. Wang, L. Zhou, X. Leng, X. Liao, and X. Hu Aggregation and homogenization, surface charge and structural change, and inactivation of mushroom tyrosinase in an aqueous system by subcritical/ supercritical carbon dioxide Langmuir 27 2011 909 916
    • (2011) Langmuir , vol.27 , pp. 909-916
    • Hu, W.1    Zhang, Y.2    Wang, Y.3    Zhou, L.4    Leng, X.5    Liao, X.6    Hu, X.7
  • 74
    • 0026550733 scopus 로고
    • Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase
    • U. Derewenda, A.M. Brzozowski, D.M. Lawson, and Z.S. Derewenda Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase Biochemistry 31 1992 1532 1541
    • (1992) Biochemistry , vol.31 , pp. 1532-1541
    • Derewenda, U.1    Brzozowski, A.M.2    Lawson, D.M.3    Derewenda, Z.S.4
  • 75
    • 0031023666 scopus 로고    scopus 로고
    • 'Interfacial activation' of lipases: Facts and artifacts
    • DOI 10.1016/S0167-7799(96)10064-0, PII S0167779996100640
    • R. Verger Interfacial activation of lipases: facts and artifacts Trends in Biotechnology 15 1997 32 38 (Pubitemid 27067151)
    • (1997) Trends in Biotechnology , vol.15 , Issue.1 , pp. 32-38
    • Verger, R.1
  • 76
    • 0037010728 scopus 로고    scopus 로고
    • Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): Immobilization, hyperactivation and stabilization of the open form of lipases
    • DOI 10.1016/S1381-1177(02)00178-9, PII S1381117702001789
    • J.M. Palomo, G. Muñoz, G. Fernández-Lorente, C. Mateo, R. Fernández-Lafuente, and J.M. Guisán Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases J. Molecular Catalysis B: Enzymatic 19 2002 279 286 (Pubitemid 35304745)
    • (2002) Journal of Molecular Catalysis B: Enzymatic , vol.19-20 , pp. 279-286
    • Palomo, J.M.1    Muoz, G.2    Fernandez-Lorente, G.3    Mateo, C.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 77
    • 34547537549 scopus 로고    scopus 로고
    • Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports
    • DOI 10.1016/j.enzmictec.2007.05.004, PII S0141022907001780
    • G. Fernandez-Lorente, J.M. Palomo, Z. Cabrera, J.M. Guisan, and R. Fernandez-Lafuente Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports Enzyme and Microbial Technology 41 2007 565 569 (Pubitemid 47187851)
    • (2007) Enzyme and Microbial Technology , vol.41 , Issue.5 , pp. 565-569
    • Fernandez-Lorente, G.1    Palomo, J.M.2    Cabrera, Z.3    Guisan, J.M.4    Fernandez-Lafuente, R.5
  • 78
    • 50449108577 scopus 로고    scopus 로고
    • Interfacially activated lipases against hydrophobic supports: Effect of the support nature on the biocatalytic properties
    • G. Fernandez-Lorente, Z. Cabrera, C. Godoy, R. Fernandez-Lafuente, J.M. Palomo, and J.M. Guisan Interfacially activated lipases against hydrophobic supports: effect of the support nature on the biocatalytic properties Process Biochemistry 43 2008 1061 1067
    • (2008) Process Biochemistry , vol.43 , pp. 1061-1067
    • Fernandez-Lorente, G.1    Cabrera, Z.2    Godoy, C.3    Fernandez-Lafuente, R.4    Palomo, J.M.5    Guisan, J.M.6
  • 81
    • 0141814774 scopus 로고    scopus 로고
    • Silica aerogels as supports for lipase catalyzed esterifications at sub- and supercritical conditions
    • Z. Novak, M. Habulin, V. Krmelj, and Ž. Knez Silica aerogels as supports for lipase catalyzed esterifications at sub- and supercritical conditions The J. Supercritical Fluids 27 2003 169 178
    • (2003) The J. Supercritical Fluids , vol.27 , pp. 169-178
    • Novak, Z.1    Habulin, M.2    Krmelj, V.3    Knez, Ž.4
  • 82
    • 26844518011 scopus 로고    scopus 로고
    • Rate enhancement of lipase-catalyzed reaction in supercritical carbon dioxide
    • DOI 10.1246/cl.2005.1102
    • T. Matsuda, K. Tsuji, T. Kamitanaka, T. Harada, K. Nakamura, and T. Ikariya Rate enhancement of lipase-catalyzed reaction in supercritical carbon dioxide Chemistry Letters 34 2005 1102 1103 (Pubitemid 41463119)
    • (2005) Chemistry Letters , vol.34 , Issue.8 , pp. 1102-1103
    • Matsuda, T.1    Tsuji, K.2    Kamitanaka, T.3    Harada, T.4    Nakamura, K.5    Ikariya, T.6
  • 84
    • 27444442189 scopus 로고    scopus 로고
    • Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide
    • DOI 10.1016/j.supflu.2005.06.007, PII S0896844605001397
    • C. Blattner, M. Zoumpanioti, J. Kröner, G. Schmeer, A. Xenakis, and W. Kunz Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide J. Supercritical Fluids 36 2006 182 193 (Pubitemid 41531226)
    • (2006) Journal of Supercritical Fluids , vol.36 , Issue.3 , pp. 182-193
    • Blattner, C.1    Zoumpanioti, M.2    Kroner, J.3    Schmeer, G.4    Xenakis, A.5    Kunz, W.6
  • 86
    • 77957857042 scopus 로고    scopus 로고
    • Lipase catalysis in ionic liquids/supercritical carbon dioxide and its applications
    • Y. Fan, and J. Qian Lipase catalysis in ionic liquids/supercritical carbon dioxide and its applications J. Molecular Catalysis B: Enzymatic 66 2010 1 7
    • (2010) J. Molecular Catalysis B: Enzymatic , vol.66 , pp. 1-7
    • Fan, Y.1    Qian, J.2
  • 87
    • 0037360305 scopus 로고    scopus 로고
    • Lipase catalysis in ionic liquids and supercritical carbon dioxide at 150°C
    • DOI 10.1021/bp025759o
    • P.a. Lozano, T.a. De Diego, D.b. Carrié, M.b. Vaultier, and J.L. Iborra Lipase catalysis in ionic liquids and supercritical carbon dioxide at 150 °C Biotechnology Progress 19 2003 380 382 (Pubitemid 36420986)
    • (2003) Biotechnology Progress , vol.19 , Issue.2 , pp. 380-382
    • Lozano, P.1    De Diego, T.2    Carrie, D.3    Vaultier, M.4    Iborra, J.L.5


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