메뉴 건너뛰기




Volumn 35, Issue 1, 2005, Pages 62-69

Cutinase activity in supercritical and organic media: Water activity, solvation and acid-base effects

Author keywords

Activity coefficients; Cutinase; Enzyme protonation state; Organic solvents; Supercritical fluids; Zeolites

Indexed keywords

ACETONITRILE; ACIDITY; ALKALINITY; ENZYME IMMOBILIZATION; ENZYMES; ESTERIFICATION; ETHANE; HYDRATES; HYDROLYSIS; ORGANIC SOLVENTS; SUPERCRITICAL FLUIDS; WATER; ZEOLITES;

EID: 21244445702     PISSN: 08968446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.supflu.2004.10.011     Document Type: Article
Times cited : (19)

References (53)
  • 1
    • 0037008481 scopus 로고    scopus 로고
    • Practical approaches to green solvents
    • J.M. DeSimone Practical approaches to green solvents Science 297 2002 799 803
    • (2002) Science , vol.297 , pp. 799-803
    • Desimone, J.M.1
  • 4
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • A.M. Klibanov Improving enzymes by using them in organic solvents Nature 409 2001 241 246
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 5
    • 0036844979 scopus 로고    scopus 로고
    • Developments and trends in enzyme catalysis in nonconventional media
    • S.H. Krishna Developments and trends in enzyme catalysis in nonconventional media Biotechnol. Adv. 20 2002 239 266
    • (2002) Biotechnol. Adv. , vol.20 , pp. 239-266
    • Krishna, S.H.1
  • 7
    • 0028243728 scopus 로고
    • X-ray crystal structure of γ-chymotrypsin in hexane
    • N.H. Yennawar, H.P. Yennawar, and G.K. Farber X-ray crystal structure of γ-chymotrypsin in hexane Biochemistry 33 1994 7326 7337
    • (1994) Biochemistry , vol.33 , pp. 7326-7337
    • Yennawar, N.H.1    Yennawar, H.P.2    Farber, G.K.3
  • 8
    • 0030970824 scopus 로고    scopus 로고
    • Crystal Structure of subtilisin Carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile
    • J.L. Schmitke, L.J. Stern, and A.M. Klibanov Crystal Structure of subtilisin Carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile Proc. Natl. Acad. Sci. USA 94 1997 4250 4255
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4250-4255
    • Schmitke, J.L.1    Stern, L.J.2    Klibanov, A.M.3
  • 9
    • 0029902287 scopus 로고    scopus 로고
    • On protein denaturation in aqueous-organic mixtures but not in pure organic solvents
    • K. Griebenow, and A.M. Klibanvov On protein denaturation in aqueous-organic mixtures but not in pure organic solvents J. Am. Chem. Soc. 47 1996 11695 11700
    • (1996) J. Am. Chem. Soc. , vol.47 , pp. 11695-11700
    • Griebenow, K.1    Klibanvov, A.M.2
  • 11
  • 13
    • 0028396938 scopus 로고
    • Thermodynamic predictions for biocatalysis in nonconventional media:theory, tests and recommendations for experimental design and analysis
    • P.J. Halling Thermodynamic predictions for biocatalysis in nonconventional media:theory, tests and recommendations for experimental design and analysis Enzyme Microb. Technol. 16 1994 178 206
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 178-206
    • Halling, P.J.1
  • 14
    • 0031149286 scopus 로고    scopus 로고
    • Water activity fails to predict critical hydration level for enzyme activity in polar organic solvents: Interconversion of water concentrations and activities
    • G. Bell, A.E.M. Janssen, and P.J. Halling Water activity fails to predict critical hydration level for enzyme activity in polar organic solvents: interconversion of water concentrations and activities Enzyme Microb. Technol. 20 1997 471 477
    • (1997) Enzyme Microb. Technol. , vol.20 , pp. 471-477
    • Bell, G.1    Janssen, A.E.M.2    Halling, P.J.3
  • 15
    • 0027641057 scopus 로고
    • The hydration of proteins in nearly anhydrous organic solvent suspensions
    • J.H. McMinn, M.J. Sowa, S.B. Charnick, and M.E. Paulaitis The hydration of proteins in nearly anhydrous organic solvent suspensions Biopolymers 33 1993 1213 1224
    • (1993) Biopolymers , vol.33 , pp. 1213-1224
    • McMinn, J.H.1    Sowa, M.J.2    Charnick, S.B.3    Paulaitis, M.E.4
  • 16
    • 0028282678 scopus 로고
    • Relationship between water activity and catalytic activity of lipases in organic media. Effects of supports, loading and enzyme preparation
    • R.H. Valivety, P.J. Halling, A.D. Peilow, and A.R. Macrae Relationship between water activity and catalytic activity of lipases in organic media. Effects of supports, loading and enzyme preparation Eur J. Biochem. 222 1994 461 466
    • (1994) Eur J. Biochem. , vol.222 , pp. 461-466
    • Valivety, R.H.1    Halling, P.J.2    Peilow, A.D.3    MacRae, A.R.4
  • 19
    • 0032575262 scopus 로고    scopus 로고
    • Activity and mobility of subtilisin in low water organic media: Hydration is more important than solvent dielectric
    • J. Partridge, P.R. Dennison, B.D. Moore, and P.J. Halling Activity and mobility of subtilisin in low water organic media: hydration is more important than solvent dielectric Biochim. Biophys. Acta 1386 1998 79 89
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 79-89
    • Partridge, J.1    Dennison, P.R.2    Moore, B.D.3    Halling, P.J.4
  • 20
    • 0029945733 scopus 로고    scopus 로고
    • Solvation and dynamics of chymotrypsin in hexane
    • S. Toba, D.S. Hartsough, and K.M. Merz Solvation and dynamics of chymotrypsin in hexane J. Am. Chem. Soc. 118 1996 6490 6498
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6490-6498
    • Toba, S.1    Hartsough, D.S.2    Merz, K.M.3
  • 21
    • 0029636270 scopus 로고
    • Factors affecting the esterification of lauric acid using an immobilized biocatalyst: Enzyme characterization and studies in a well-mixed reactor
    • F. Vázquez Lima, D.L. Pyle, and J.A. Asenjo Factors affecting the esterification of lauric acid using an immobilized biocatalyst: Enzyme characterization and studies in a well-mixed reactor Biotechnol. Bioeng. 46 1995 69 97
    • (1995) Biotechnol. Bioeng. , vol.46 , pp. 69-97
    • Vázquez Lima, F.1    Pyle, D.L.2    Asenjo, J.A.3
  • 22
    • 0001469909 scopus 로고    scopus 로고
    • Solvent effects on the catalytic activity of subtilisin suspended in compressed gases
    • I. Borges de Carvalho, T. Corrêa de Sampaio, and S. Barreiros Solvent effects on the catalytic activity of subtilisin suspended in compressed gases Biotechnol. Bioeng. 49 1996 399 404
    • (1996) Biotechnol. Bioeng. , vol.49 , pp. 399-404
    • Borges De Carvalho, I.1    Corrêa De Sampaio, T.2    Barreiros, S.3
  • 24
    • 0032478326 scopus 로고    scopus 로고
    • Effect of pressure on the catalytic activity of subtilisin carlsberg suspended in compressed gases
    • N. Fontes, E. Nogueiro, A.M. Elvas, T. Corrêa de Sampaio, and S. Barreiros Effect of pressure on the catalytic activity of subtilisin carlsberg suspended in compressed gases Biochim. Biophys. Acta 1383 1998 165 174
    • (1998) Biochim. Biophys. Acta , vol.1383 , pp. 165-174
    • Fontes, N.1    Nogueiro, E.2    Elvas, A.M.3    Corrêa De Sampaio, T.4    Barreiros, S.5
  • 25
    • 0037023905 scopus 로고    scopus 로고
    • Esterification by immobilized lipase in solvent-free media: Kinetic and thermodynamic arguments
    • G. Sandoval, J.S. Condoret, P. Monsan, and A. Marty Esterification by immobilized lipase in solvent-free media: kinetic and thermodynamic arguments Biotechnol. Bioeng. 78 2002 313 320
    • (2002) Biotechnol. Bioeng. , vol.78 , pp. 313-320
    • Sandoval, G.1    Condoret, J.S.2    Monsan, P.3    Marty, A.4
  • 26
    • 0034606636 scopus 로고    scopus 로고
    • Intrinsic effects of solvent polarity on enzymic activation energies
    • J. Kim, D.S. Clark, and J.S. Dordick Intrinsic effects of solvent polarity on enzymic activation energies Biotechnol. Bioeng. 67 2000 112 116
    • (2000) Biotechnol. Bioeng. , vol.67 , pp. 112-116
    • Kim, J.1    Clark, D.S.2    Dordick, J.S.3
  • 27
    • 0032551728 scopus 로고    scopus 로고
    • Organic solvent binding to crystalline subtilisin in mostly aqueous media and in the neat solvents
    • J.L. Schmitke, L.J. Stern, and A.M. Klibanov Organic solvent binding to crystalline subtilisin in mostly aqueous media and in the neat solvents Biochem. Biophys. Res. Commun. 248 1998 273 277
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 273-277
    • Schmitke, J.L.1    Stern, L.J.2    Klibanov, A.M.3
  • 28
    • 0036861431 scopus 로고    scopus 로고
    • Enhancement of enzyme activity in supercritical carbon dioxide via changes in acid-base conditions
    • N. Harper, and S. Barreiros Enhancement of enzyme activity in supercritical carbon dioxide via changes in acid-base conditions Biotechnol. Prog. 18 2002 1451 1454
    • (2002) Biotechnol. Prog. , vol.18 , pp. 1451-1454
    • Harper, N.1    Barreiros, S.2
  • 30
    • 0033965918 scopus 로고    scopus 로고
    • Biocatalysis in low-water media: Understanding effects of reaction conditions
    • P.J. Halling Biocatalysis in low-water media: understanding effects of reaction conditions Curr. Opin. Chem. Biol. 4 2000 74 80
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 74-80
    • Halling, P.J.1
  • 31
    • 0000321692 scopus 로고
    • Enzyme-catalyzed processes in organic solvents
    • A. Zaks, and A.M. Klinanov Enzyme-catalyzed processes in organic solvents Proc. Natl Acad. Sci. USA 82 1985 3192 3196
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 3192-3196
    • Zaks, A.1    Klinanov, A.M.2
  • 32
    • 0029858946 scopus 로고    scopus 로고
    • PH control of the catalytic activity of cross-linked enzyme crystals in organic solvents
    • K. Xu, and A.M. Klibanov pH control of the catalytic activity of cross-linked enzyme crystals in organic solvents J. Am. Chem. Soc. 118 1996 9815 9819
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9815-9819
    • Xu, K.1    Klibanov, A.M.2
  • 33
    • 0242710531 scopus 로고    scopus 로고
    • Control of enzyme ionization state in supercritical ethane by sodium/proton solid-state acid-base buffers
    • N. Fontes, P.J. Halling, and S. Barreiros Control of enzyme ionization state in supercritical ethane by sodium/proton solid-state acid-base buffers Enzyme Microb. Technol. 33 2003 938 941
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 938-941
    • Fontes, N.1    Halling, P.J.2    Barreiros, S.3
  • 34
    • 0034595811 scopus 로고    scopus 로고
    • Acid-base control for biocatalysis in organic media: New solid-state proton/cation buffers and an indicator
    • N. Harper, M. Dolman, B.D. Moore, and P.J. Halling Acid-base control for biocatalysis in organic media: new solid-state proton/cation buffers and an indicator Chem. Eur. J. 6 2000 1923 1929
    • (2000) Chem. Eur. J. , vol.6 , pp. 1923-1929
    • Harper, N.1    Dolman, M.2    Moore, B.D.3    Halling, P.J.4
  • 35
    • 0034160970 scopus 로고    scopus 로고
    • Solid-state proton/sodium buffers: 'Chemical pH stats' for biocatalysts in organic solvents
    • J. Partridge, P.J. Halling, and B.D. Moore Solid-state proton/sodium buffers: 'chemical pH stats' for biocatalysts in organic solvents J. Chem. Soc., Perkin Trans. 2 2000 465 471
    • (2000) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 465-471
    • Partridge, J.1    Halling, P.J.2    Moore, B.D.3
  • 36
    • 0001485535 scopus 로고    scopus 로고
    • Control of enzyme activity in organic media by solid-state acid-base buffers
    • E. Zacharis, B.D. Moore, and P.J. Halling Control of enzyme activity in organic media by solid-state acid-base buffers J. Am. Chem. Soc. 119 1997 12396 12397
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 12396-12397
    • Zacharis, E.1    Moore, B.D.2    Halling, P.J.3
  • 43
    • 51249163381 scopus 로고
    • Salt hydrates for water activity control with biocatalysts in organic media
    • P.J. Halling Salt hydrates for water activity control with biocatalysts in organic media Biotechnol. Tech. 6 1992 271 276
    • (1992) Biotechnol. Tech. , vol.6 , pp. 271-276
    • Halling, P.J.1
  • 44
    • 0035809235 scopus 로고    scopus 로고
    • Zeolite molecular sieves have dramatic acid-base effects on enzymes in nonaqueous media
    • N. Fontes, J. Partridge, P.J. Halling, and S. Barreiros Zeolite molecular sieves have dramatic acid-base effects on enzymes in nonaqueous media Biotechnol. Bioeng. 77 2002 296 305
    • (2002) Biotechnol. Bioeng. , vol.77 , pp. 296-305
    • Fontes, N.1    Partridge, J.2    Halling, P.J.3    Barreiros, S.4
  • 45
    • 0034921545 scopus 로고    scopus 로고
    • Supercritical fluids are superior media for catalysis by cross-linked enzyme microcrystals of subtilisin Carlsberg
    • N. Fontes, M.C. Almeida, S. Garcia, C. Peres, J. Partridge, P.J. Halling, and S. Barreiros Supercritical fluids are superior media for catalysis by cross-linked enzyme microcrystals of subtilisin Carlsberg Biotechnol. Prog. 17 2001 355 358
    • (2001) Biotechnol. Prog. , vol.17 , pp. 355-358
    • Fontes, N.1    Almeida, M.C.2    Garcia, S.3    Peres, C.4    Partridge, J.5    Halling, P.J.6    Barreiros, S.7
  • 46
    • 0017437920 scopus 로고
    • Humidity fixed points of binary saturated aqueous solutions
    • L. Greenspan Humidity fixed points of binary saturated aqueous solutions J. Res. Nat. Bur. Stand. - A. Phys. Chem. 81A 1977 89 96
    • (1977) J. Res. Nat. Bur. Stand. - A. Phys. Chem. , vol.81 , pp. 89-96
    • Greenspan, L.1
  • 47
    • 0031455616 scopus 로고    scopus 로고
    • The enantiomeric ratio: Origin, determination and prediction
    • A.J.J. Straathof, and J.A. Jongejan The enantiomeric ratio: origin, determination and prediction Enzyme Microb. Technol. 21 1997 559 571
    • (1997) Enzyme Microb. Technol. , vol.21 , pp. 559-571
    • Straathof, A.J.J.1    Jongejan, J.A.2
  • 48
    • 0023455795 scopus 로고
    • A modified UNIFAC group-contribution model for prediction of phase equilibria and heat of mixing
    • B.L. Larsen, P. Rasmussen, and A. Fredenslund A modified UNIFAC group-contribution model for prediction of phase equilibria and heat of mixing Ind. Eng. Chem. Res. 26 1987 2274 2286
    • (1987) Ind. Eng. Chem. Res. , vol.26 , pp. 2274-2286
    • Larsen, B.L.1    Rasmussen, P.2    Fredenslund, A.3
  • 49
    • 0026205276 scopus 로고
    • The MHV2 model: A UNIFAC-based equation of state model for prediction of gas solubility and vapor liquid equilibria at low and high pressures
    • S. Dahl, A. Fredenslund, and P. Rasmussen The MHV2 model: A UNIFAC-based equation of state model for prediction of gas solubility and vapor liquid equilibria at low and high pressures Ind. Eng. Chem. Res. 30 1991 1936 1945
    • (1991) Ind. Eng. Chem. Res. , vol.30 , pp. 1936-1945
    • Dahl, S.1    Fredenslund, A.2    Rasmussen, P.3
  • 50
    • 0025555405 scopus 로고
    • High pressure vapor-liquid equilibrium with a UNIFAC based equation of state
    • S. Dahl, and M.L. Michelsen High pressure vapor-liquid equilibrium with a UNIFAC based equation of state Fluid Phase Equilib. 36 1990 1829 1836
    • (1990) Fluid Phase Equilib. , vol.36 , pp. 1829-1836
    • Dahl, S.1    Michelsen, M.L.2
  • 51
    • 0037572324 scopus 로고    scopus 로고
    • Salt hydrates for in-situ water activity control have acid-base effects on enzymes in nonaqueous media
    • N. Fontes, N. Harper, P.J. Halling, and S. Barreiros Salt hydrates for in-situ water activity control have acid-base effects on enzymes in nonaqueous media Biotechnol. Bioeng. 82 2003 802 808
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 802-808
    • Fontes, N.1    Harper, N.2    Halling, P.J.3    Barreiros, S.4
  • 52
    • 21244437263 scopus 로고    scopus 로고
    • Peres et al., to be published
    • Peres et al., to be published.
  • 53
    • 0037721268 scopus 로고    scopus 로고
    • Effect of solid-state buffers on the catalytic activity of papain in low-water media
    • T. Theppakorn, P. Kanasawud, and P.J. Halling Effect of solid-state buffers on the catalytic activity of papain in low-water media Enzyme Microb. Technol. 32 2003 828 836
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 828-836
    • Theppakorn, T.1    Kanasawud, P.2    Halling, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.