메뉴 건너뛰기




Volumn 56, Issue 3, 1997, Pages 340-344

Thermodynamic analysis of solvent effect on substrate specificity of lyophilized enzymes suspended in organic media

Author keywords

Chymotrypsin; Lyophilized enzymes; Organic solvents; Stereoselectivity; Substrate specificity; Subtilisin

Indexed keywords

COMPOSITION EFFECTS; ENZYMES; ORGANIC SOLVENTS; THERMOANALYSIS;

EID: 0031555162     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19971105)56:3<340::AID-BIT12>3.0.CO;2-K     Document Type: Article
Times cited : (27)

References (37)
  • 2
    • 0028855057 scopus 로고
    • Role of solvents in the control of enzyme selectivity in organic media
    • Carrea, G., Ottolina, G., Riva, S. 1995. Role of solvents in the control of enzyme selectivity in organic media. Trends Biotechnol. 13: 63-70.
    • (1995) Trends Biotechnol. , vol.13 , pp. 63-70
    • Carrea, G.1    Ottolina, G.2    Riva, S.3
  • 3
    • 84990106353 scopus 로고
    • General aspects and optimization of enantio-selective biocatalysis in organic solvents
    • Chen, C.-S., Sih, C. J. 1989. General aspects and optimization of enantio-selective biocatalysis in organic solvents. Angew. Chem. Int. Ed. Engl. 28: 695-707.
    • (1989) Angew. Chem. Int. Ed. Engl. , vol.28 , pp. 695-707
    • Chen, C.-S.1    Sih, C.J.2
  • 4
    • 0028875052 scopus 로고
    • Fourier-transform infrared spectroscopic investigation of protein stability in the lyophilized form
    • Costantino, H. R., Griebenow, K., Mishra, P., Langer, R., Klibanov, A. M. 1995. Fourier-transform infrared spectroscopic investigation of protein stability in the lyophilized form. Biochim. Biophys. Acta 1253: 69-74.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 69-74
    • Costantino, H.R.1    Griebenow, K.2    Mishra, P.3    Langer, R.4    Klibanov, A.M.5
  • 5
    • 0029278809 scopus 로고
    • Assessing the structural integrity of a lyophilized protein in organic solvents
    • Desai, U. R., Klibanov, A. M. 1995. Assessing the structural integrity of a lyophilized protein in organic solvents. J. Am. Chem. Soc. 117: 3940-3945.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3940-3945
    • Desai, U.R.1    Klibanov, A.M.2
  • 6
    • 0028029812 scopus 로고
    • Protein structure in the lyophilized state: A hydrogen isotope exchange/NMR study with bovine pancreatic trypsin inhibitor
    • Desai, U. R., Osterhout, J. J., Klibanov, A. M. 1994. Protein structure in the lyophilized state: A hydrogen isotope exchange/NMR study with bovine pancreatic trypsin inhibitor. J. Am. Chem. Soc. 116: 9420-9422.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9420-9422
    • Desai, U.R.1    Osterhout, J.J.2    Klibanov, A.M.3
  • 7
    • 0026892825 scopus 로고
    • Designing enzymes for use in organic solvents
    • Dordick, J. S. 1992. Designing enzymes for use in organic solvents. Biotechnol. Prog. 1992: 259-267.
    • (1992) Biotechnol. Prog. , vol.1992 , pp. 259-267
    • Dordick, J.S.1
  • 10
    • 0028304966 scopus 로고
    • X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile
    • Fitzpatrick, P. A., Ringe, D., Klibanov, A. M. 1994. X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile. Biochem. Biophys. Res. Commun. 198: 675-681.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 675-681
    • Fitzpatrick, P.A.1    Ringe, D.2    Klibanov, A.M.3
  • 13
    • 0028847040 scopus 로고
    • Lyophilization-induced reversible changes in the secondary structure of proteins
    • Griebenow, K., Klibanov, A. M. 1995. Lyophilization-induced reversible changes in the secondary structure of proteins. Proc. Natl. Acad. Sci. USA 92: 10969-10976.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10969-10976
    • Griebenow, K.1    Klibanov, A.M.2
  • 14
    • 0026517617 scopus 로고
    • Enzyme function in organic solvents
    • Gupta, M. N. 1992. Enzyme function in organic solvents. Eur. J. Biochem. 203: 25-30.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 25-30
    • Gupta, M.N.1
  • 15
    • 0028396938 scopus 로고
    • Thermodynamic predictions for biocatalysis in non-conventional media: Theory, tests, and recommendations for experimental design and analysis
    • Halling, P. J. 1994. Thermodynamic predictions for biocatalysis in non-conventional media: Theory, tests, and recommendations for experimental design and analysis. Enzyme Microb. Technol. 16: 178-206.
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 178-206
    • Halling, P.J.1
  • 16
    • 0026244317 scopus 로고
    • Vaporliquid equilibria by UNIFAC group contribution. 5. Revision and extension
    • Hansen, H. K., Rasmussen, P., Schiller, M., Gmehling, J. 1991. Vaporliquid equilibria by UNIFAC group contribution. 5. Revision and extension. Ind. Eng. Chem. Res. 30: 2352-2355.
    • (1991) Ind. Eng. Chem. Res. , vol.30 , pp. 2352-2355
    • Hansen, H.K.1    Rasmussen, P.2    Schiller, M.3    Gmehling, J.4
  • 17
    • 0029959897 scopus 로고    scopus 로고
    • Prediction of the solvent dependence of enzymatic prochiral selectivity by means of structure-based thermodynamic calculations
    • Ke, T., Wescott, C. R., Klibanov, A. M. 1996. Prediction of the solvent dependence of enzymatic prochiral selectivity by means of structure-based thermodynamic calculations. J. Am. Chem. Soc. 118: 3366-3374.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3366-3374
    • Ke, T.1    Wescott, C.R.2    Klibanov, A.M.3
  • 18
    • 0024653016 scopus 로고
    • Enzymatic catalysis in anhydrous organic solvents
    • Klibanov, A. M. 1989. Enzymatic catalysis in anhydrous organic solvents. Trends Biochem. Sci. 14: 141-144.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 141-144
    • Klibanov, A.M.1
  • 19
    • 0642367795 scopus 로고
    • Asymmetric transformations catalyzed by enzymes in organic solvents
    • Klibanov, A. M. 1990. Asymmetric transformations catalyzed by enzymes in organic solvents. Acc. Chem. Res. 23: 114-120.
    • (1990) Acc. Chem. Res. , vol.23 , pp. 114-120
    • Klibanov, A.M.1
  • 24
    • 0027588112 scopus 로고
    • Enzymes in the synthesis of chiral drugs
    • Margolin, A. L. 1993. Enzymes in the synthesis of chiral drugs. Enzyme Microb. Technol. 15: 266-280.
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 266-280
    • Margolin, A.L.1
  • 26
    • 0027176042 scopus 로고
    • Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization
    • Prestrelski, S. J., Arakawa, T., Carpenter, J. F. 1993a. Separation of freezing-and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. Arch. Biochem. Biophys. 303: 465-473.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 465-473
    • Prestrelski, S.J.1    Arakawa, T.2    Carpenter, J.F.3
  • 27
    • 0027163348 scopus 로고
    • Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers
    • Prestrelski, S. J., Tedeschi, N., Arakawa, T., Carpenter, J. F. 19936. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophys. J. 65: 661-671.
    • (1993) Biophys. J. , vol.65 , pp. 661-671
    • Prestrelski, S.J.1    Tedeschi, N.2    Arakawa, T.3    Carpenter, J.F.4
  • 28
    • 0019927981 scopus 로고
    • Vapor-liquid equilibria by UNIFAC group contribution. Revision and extension. 2
    • Rasmussen, P., Fredenslund, A. 1982. Vapor-liquid equilibria by UNIFAC group contribution. Revision and extension. 2. Ind. Eng. Chem. Process Des. Dev. 21: 118-127.
    • (1982) Ind. Eng. Chem. Process Des. Dev. , vol.21 , pp. 118-127
    • Rasmussen, P.1    Fredenslund, A.2
  • 32
    • 0023238148 scopus 로고
    • Vapor-liquid equilibria by UNIFAC group contribution. 4. Revision and extension
    • Teigs, D., Gmehling, J., Rasmussen, P., Fredenslund, A. 1987. Vapor-liquid equilibria by UNIFAC group contribution. 4. Revision and extension. Ind. Eng. Chem. Res. 26: 159-161.
    • (1987) Ind. Eng. Chem. Res. , vol.26 , pp. 159-161
    • Teigs, D.1    Gmehling, J.2    Rasmussen, P.3    Fredenslund, A.4
  • 33
    • 0000764219 scopus 로고
    • Solvent variation inverts substrate specificity of an enzyme
    • Wescott, C. R., Klibanov, A. M. 1993a. Solvent variation inverts substrate specificity of an enzyme. J. Am. Chem. Soc. 115: 1629-1631.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 1629-1631
    • Wescott, C.R.1    Klibanov, A.M.2
  • 34
    • 12044253973 scopus 로고
    • Predicting the solvent dependence of enzymatic substrate specificity using semiempirical thermodynamic calculations
    • Wescott, C. R., Klibanov, A. M. 1993b. Predicting the solvent dependence of enzymatic substrate specificity using semiempirical thermodynamic calculations. J. Am. Chem. Soc. 115: 10362-10363.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 10362-10363
    • Wescott, C.R.1    Klibanov, A.M.2
  • 35
    • 0028302684 scopus 로고
    • The solvent dependence of enzyme specificity
    • Wescott, C. R., Klibanov, A. M. 1994. The solvent dependence of enzyme specificity. Biochim. Biophys. Acta 1206: 1-9.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 1-9
    • Wescott, C.R.1    Klibanov, A.M.2
  • 36
    • 0029818293 scopus 로고    scopus 로고
    • Rational control of enzymatic selectivity through solvation thermodynamics
    • Wescott, C. R., Noritomi, H., Klibanov, A. M. 1996. Rational control of enzymatic selectivity through solvation thermodynamics. J. Am. Chem. Soc. 118: 10365-10370.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10365-10370
    • Wescott, C.R.1    Noritomi, H.2    Klibanov, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.