메뉴 건너뛰기




Volumn 1750, Issue 1, 2005, Pages 17-29

Effect of dioxane on the structure and hydration-dehydration of α-chymotrypsin as measured by FTIR spectroscopy

Author keywords

Bovine pancreatic chymotrypsin; Enzyme hydration; Fourier transform infrared spectroscopy; Hysteresis phenomenon; Organic solvent sorption; Secondary structure; Thin film

Indexed keywords

CHYMOTRYPSIN A; DIOXANE; ORGANIC SOLVENT; PANCREAS ENZYME; WATER;

EID: 20444366969     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.02.010     Document Type: Article
Times cited : (37)

References (61)
  • 2
  • 3
    • 0016022523 scopus 로고
    • Hydration of proteins and polypeptides
    • I.D. Kuntz, and W. Kauzmann Hydration of proteins and polypeptides Adv. Protein Chem. 28 1974 239 345
    • (1974) Adv. Protein Chem. , vol.28 , pp. 239-345
    • Kuntz, I.D.1    Kauzmann, W.2
  • 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
    • 0041152088 scopus 로고    scopus 로고
    • Properties and synthetic applications of enzymes in organic solvents
    • G. Carrea, and S. Riva Properties and synthetic applications of enzymes in organic solvents Angew. Chem. Int. Ed. 39 2000 2226 2254
    • (2000) Angew. Chem. Int. Ed. , vol.39 , pp. 2226-2254
    • Carrea, G.1    Riva, S.2
  • 7
    • 0028396938 scopus 로고
    • Thermodynamic predictions for biocatalysis in nonconventional media: Theory, tests, and recommendations for design and analysis
    • P.J. Halling Thermodynamic predictions for biocatalysis in nonconventional media: theory, tests, and recommendations for design and analysis Enzyme Microb. Technol. 16 1994 178 206
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 178-206
    • Halling, P.J.1
  • 8
    • 0006578611 scopus 로고    scopus 로고
    • A. Straathof P. Adlercreutz 2nd Ed. Harwood Academic Publishers
    • P. Adlercreutz A. Straathof P. Adlercreutz Applied Biocatalysis 2nd Ed. 2000 Harwood Academic Publishers 295 316
    • (2000) Applied Biocatalysis , pp. 295-316
    • Adlercreutz, P.1
  • 9
    • 0034254270 scopus 로고    scopus 로고
    • Thermometric sensing of peroxide in organic media. Application to monitor the stability RBP-Retinol-HRP complex
    • K. Ramanathan, B.R. Jonsson, and B. Danielsson Thermometric sensing of peroxide in organic media. Application to monitor the stability RBP-Retinol-HRP complex Anal. Chem. 72 2000 3443 3448
    • (2000) Anal. Chem. , vol.72 , pp. 3443-3448
    • Ramanathan, K.1    Jonsson, B.R.2    Danielsson, B.3
  • 10
    • 0034303549 scopus 로고    scopus 로고
    • Construction and analytical application of a biosensor based on stearic acid-graphite powder modified with sweet potato tissue in organic solvents
    • O. Fatibello-Filho, and I. Cruz Viera Construction and analytical application of a biosensor based on stearic acid-graphite powder modified with sweet potato tissue in organic solvents Fresenius' J. Anal. Chem. 368 2000 338 343
    • (2000) Fresenius' J. Anal. Chem. , vol.368 , pp. 338-343
    • Fatibello-Filho, O.1    Cruz Viera, I.2
  • 11
    • 0000983403 scopus 로고
    • Induced stereoselectivity and substrate selectivity of bio-imprinted α-chymotrypsin in anhydrous organic media
    • M. Stahl, U. Jeppson-Wistrand, M.-O. Mansson, and K. Mosbach Induced stereoselectivity and substrate selectivity of bio-imprinted α-chymotrypsin in anhydrous organic media J. Am. Chem. Soc. 113 1991 9366 9368
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9366-9368
    • Stahl, M.1    Jeppson-Wistrand, U.2    Mansson, M.-O.3    Mosbach, K.4
  • 12
    • 0026501337 scopus 로고
    • Molecular imprinting of proteins and other macromolecules resulting in new adsorbents
    • K. Dabulis, and A.M. Klibanov Molecular imprinting of proteins and other macromolecules resulting in new adsorbents Biotechnol. Bioeng. 39 1992 176 185
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 176-185
    • Dabulis, K.1    Klibanov, A.M.2
  • 13
    • 0030038897 scopus 로고    scopus 로고
    • Study of tryptophan fluorescence and catalytic activity of α-chymotrypsin in aqueous organic media
    • T. Kijima, S. Yamamoto, and H. Kise Study of tryptophan fluorescence and catalytic activity of α-chymotrypsin in aqueous organic media Enzyme Microb. Technol. 18 1996 2 6
    • (1996) Enzyme Microb. Technol. , vol.18 , pp. 2-6
    • Kijima, T.1    Yamamoto, S.2    Kise, H.3
  • 14
    • 0034811393 scopus 로고    scopus 로고
    • Structure and activity of α-chymotrypsin and trypsin in aqueous organic media
    • L.M. Simon, M. Kotorman, G. Garab, and I. Laczko Structure and activity of α-chymotrypsin and trypsin in aqueous organic media Biochem. Biophys. Res. Commun. 280 2001 1367 1371
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 1367-1371
    • Simon, L.M.1    Kotorman, M.2    Garab, G.3    Laczko, I.4
  • 15
    • 0032549603 scopus 로고    scopus 로고
    • On enzymatic activity in organic solvents as a function of enzyme hystory
    • T. Ke, and A.M. Klibanov On enzymatic activity in organic solvents as a function of enzyme hystory Biotechnol. Bioeng. 57 1998 746 750
    • (1998) Biotechnol. Bioeng. , vol.57 , pp. 746-750
    • Ke, T.1    Klibanov, A.M.2
  • 16
    • 0030450709 scopus 로고    scopus 로고
    • Exploiting hydration hysteresis for high activity of cross-linked subtilisin crystals in acetonitrile
    • J. Partridge, G.A. Hutcheon, B.D. Moore, and P.J. Halling Exploiting hydration hysteresis for high activity of cross-linked subtilisin crystals in acetonitrile J. Am. Chem. Soc. 118 1996 12873 12877
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12873-12877
    • Partridge, J.1    Hutcheon, G.A.2    Moore, B.D.3    Halling, P.J.4
  • 17
    • 0024287893 scopus 로고
    • The effect of water on enzyme action in organic media
    • A. Zaks, and A.M. Klibanov The effect of water on enzyme action in organic media J. Biol. Chem. 263 1988 8017 8021
    • (1988) J. Biol. Chem. , vol.263 , pp. 8017-8021
    • Zaks, A.1    Klibanov, A.M.2
  • 20
    • 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
  • 21
    • 0029636507 scopus 로고
    • Measuring enzyme hydration in nonpolar organic solvents using NMR
    • M.C. Parker, B.D. Moore, and A.J. Blacker Measuring enzyme hydration in nonpolar organic solvents using NMR Biotechnol. Bioeng. 46 1995 452 458
    • (1995) Biotechnol. Bioeng. , vol.46 , pp. 452-458
    • Parker, M.C.1    Moore, B.D.2    Blacker, A.J.3
  • 22
    • 0024997533 scopus 로고
    • High-affinity binding of water by proteins is similar in air and in organic solvents
    • P.J. Halling High-affinity binding of water by proteins is similar in air and in organic solvents Biochim. Biophys. Acta 1040 1990 225 228
    • (1990) Biochim. Biophys. Acta , vol.1040 , pp. 225-228
    • Halling, P.J.1
  • 23
    • 0029035407 scopus 로고
    • Effect of water activity on enzyme hydration and enzyme reaction rate in organic solvents
    • S.B. Lee, and K.-J. Kim Effect of water activity on enzyme hydration and enzyme reaction rate in organic solvents J. Ferment. Bioeng. 79 1995 473 478
    • (1995) J. Ferment. Bioeng. , vol.79 , pp. 473-478
    • Lee, S.B.1    Kim, K.-J.2
  • 24
    • 0001719326 scopus 로고    scopus 로고
    • Interaction of water with human serum albumin suspended in water-organic mixtures
    • M.D. Borisover, V.A. Sirotkin, and B.N. Solomonov Interaction of water with human serum albumin suspended in water-organic mixtures Thermochim. Acta 284 1996 263 277
    • (1996) Thermochim. Acta , vol.284 , pp. 263-277
    • Borisover, M.D.1    Sirotkin, V.A.2    Solomonov, B.N.3
  • 25
    • 0031468585 scopus 로고    scopus 로고
    • Effect of chain length on interactions of aliphatic alcohols with suspended human serum albumin
    • V.A. Sirotkin, M.D. Borisover, and B.N. Solomonov Effect of chain length on interactions of aliphatic alcohols with suspended human serum albumin Biophys. Chemist. 69 1997 239 248
    • (1997) Biophys. Chemist. , vol.69 , pp. 239-248
    • Sirotkin, V.A.1    Borisover, M.D.2    Solomonov, B.N.3
  • 26
    • 0002538905 scopus 로고
    • Isotherm of water sorption by human serum albumin in dioxane: Comparison with calorimetric data
    • M.D. Borisover, V.A. Sirotkin, and B.N. Solomonov Isotherm of water sorption by human serum albumin in dioxane: comparison with calorimetric data J. Phys. Org. Chem. 8 1995 84 88
    • (1995) J. Phys. Org. Chem. , vol.8 , pp. 84-88
    • Borisover, M.D.1    Sirotkin, V.A.2    Solomonov, B.N.3
  • 28
    • 0027163348 scopus 로고
    • Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers
    • S.J. Prestrelsky, N. Tedeschi, T. Arakawa, and J.F. Carpenter Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers Biophys. J. 65 1993 661 671
    • (1993) Biophys. J. , vol.65 , pp. 661-671
    • Prestrelsky, S.J.1    Tedeschi, N.2    Arakawa, T.3    Carpenter, J.F.4
  • 29
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization-induced and temperature-induced protein aggregation
    • A. Dong, S.J. Prestrelsky, S.D. Alison, and J.F. Carpenter Infrared spectroscopic studies of lyophilization-induced and temperature-induced protein aggregation J. Pharm. Sci. 84 1995 415 424
    • (1995) J. Pharm. Sci. , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelsky, S.J.2    Alison, S.D.3    Carpenter, J.F.4
  • 30
    • 0028847040 scopus 로고
    • Lyophilization-induced reversible changes in the secondary structure of proteins
    • K. Griebenow, and A.M. Klibanov Lyophilization-induced reversible changes in the secondary structure of proteins Proc. Natl. Acad. Sci. U. S. A. 92 1995 10969 10976
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 10969-10976
    • Griebenow, K.1    Klibanov, A.M.2
  • 31
    • 0345085739 scopus 로고    scopus 로고
    • Fourier-transform infrared spectroscopy study of dehydrated lipases from Candida antarctica B and Pseudomonas cepacia
    • G. Vecchio, F. Zambianchi, P. Zacchetti, F. Secundo, and G. Carrea Fourier-transform infrared spectroscopy study of dehydrated lipases from Candida antarctica B and Pseudomonas cepacia Biotechnol. Bioeng. 64 1999 545 551
    • (1999) Biotechnol. Bioeng. , vol.64 , pp. 545-551
    • Vecchio, G.1    Zambianchi, F.2    Zacchetti, P.3    Secundo, F.4    Carrea, G.5
  • 32
    • 0035887070 scopus 로고    scopus 로고
    • Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling and stress factors
    • M. van de Weert, P.I. Harvez, W.E. Hennink, and D.J.A. Crommelin Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling and stress factors Anal. Biochem. 297 2001 160 169
    • (2001) Anal. Biochem. , vol.297 , pp. 160-169
    • Van De Weert, M.1    Harvez, P.I.2    Hennink, W.E.3    Crommelin, D.J.A.4
  • 33
    • 0035141750 scopus 로고    scopus 로고
    • Bovine serum albumin observed by infrared spectrometry: I. Methodology, structural investigation, and water uptake
    • J. Grdadolnik, and Y. Marechal Bovine serum albumin observed by infrared spectrometry: I. Methodology, structural investigation, and water uptake Biopolymers 62 2001 40 53
    • (2001) Biopolymers , vol.62 , pp. 40-53
    • Grdadolnik, J.1    Marechal, Y.2
  • 34
    • 0028539766 scopus 로고
    • Secondary structure estimation of proteins using the Amide III region of Fourier transform infrared spectroscopy: Application to analyze calcium-binding-induced structural changes in calsequestrin
    • F.-N. Fu, D.B. DeOlivera, W.R. Trumble, H.K. Sarkar, and B.R. Singh Secondary structure estimation of proteins using the Amide III region of Fourier transform infrared spectroscopy: application to analyze calcium-binding-induced structural changes in calsequestrin Appl. Spectrosc. 48 1994 1432 1441
    • (1994) Appl. Spectrosc. , vol.48 , pp. 1432-1441
    • Fu, F.-N.1    Deolivera, D.B.2    Trumble, W.R.3    Sarkar, H.K.4    Singh, B.R.5
  • 36
    • 0342275236 scopus 로고    scopus 로고
    • Can conformational changes be responsible for solvent and excipient effects on the catalytic behavior of subtilisin Carlsberg in organic solvents?
    • K. Griebenow, and A.M. Klibanov Can conformational changes be responsible for solvent and excipient effects on the catalytic behavior of subtilisin Carlsberg in organic solvents? Biotechnol. Bioeng. 53 1997 351 362
    • (1997) Biotechnol. Bioeng. , vol.53 , pp. 351-362
    • Griebenow, K.1    Klibanov, A.M.2
  • 38
    • 0035844690 scopus 로고    scopus 로고
    • Calorimetric and Fourier transform infrared spectroscopic study of solid proteins immersed in low water organic solvents
    • V.A Sirotkin, A.N. Zinatullin, B.N. Solomonov, D.A. Faizullin, and V.D. Fedotov Calorimetric and Fourier transform infrared spectroscopic study of solid proteins immersed in low water organic solvents Biochim. Biophys. Acta 1547 2001 359 369
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 359-369
    • Sirotkin, V.A.1    Zinatullin, A.N.2    Solomonov, B.N.3    Faizullin, D.A.4    Fedotov, V.D.5
  • 39
    • 0037203793 scopus 로고    scopus 로고
    • Interaction enthalpies of solid bovine pancreatic α-chymotrypsin with organic solvents: Comparison with FTIR spectroscopic data
    • V.A. Sirotkin, A.N. Zinatullin, B.N. Solomonov, D.A. Faizullin, and V.D. Fedotov Interaction enthalpies of solid bovine pancreatic α-chymotrypsin with organic solvents: comparison with FTIR spectroscopic data Thermochim. Acta 382 2002 151 160
    • (2002) Thermochim. Acta , vol.382 , pp. 151-160
    • Sirotkin, V.A.1    Zinatullin, A.N.2    Solomonov, B.N.3    Faizullin, D.A.4    Fedotov, V.D.5
  • 47
    • 0034558508 scopus 로고    scopus 로고
    • IR spectroscopic study of the state of water in dioxane and acetonitrile: Relationship with thermodynamic activity of water
    • V.A. Sirotkin, B.N. Solomonov, D.A. Faizullin, and V.D. Fedotov IR spectroscopic study of the state of water in dioxane and acetonitrile: relationship with thermodynamic activity of water J. Struct. Chem. 41 2000 997 1003
    • (2000) J. Struct. Chem. , vol.41 , pp. 997-1003
    • Sirotkin, V.A.1    Solomonov, B.N.2    Faizullin, D.A.3    Fedotov, V.D.4
  • 48
    • 2342479757 scopus 로고    scopus 로고
    • Interaction enthalpies of solid human serum albumin with water-dioxane mixtures: Comparison with water and organic solvent vapor sorption
    • V.A. Sirotkin, and D.A. Faizullin Interaction enthalpies of solid human serum albumin with water-dioxane mixtures: comparison with water and organic solvent vapor sorption Thermochim. Acta 415 2004 127 133
    • (2004) Thermochim. Acta , vol.415 , pp. 127-133
    • Sirotkin, V.A.1    Faizullin, D.A.2
  • 49
  • 51
    • 12444272525 scopus 로고
    • Adsorption of gases in multimolecular layers
    • S. Brunauer, P.H. Emmet, 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    Emmet, P.H.2    Teller, E.3
  • 52
    • 84985676118 scopus 로고
    • Thermodynamic functions of biopolymer hydration: I. Their determination by vapor pressure studies, discussed in an analysis of the primary hydration process
    • M. Luscher-Mattli, and M. Ruegg Thermodynamic functions of biopolymer hydration: I. Their determination by vapor pressure studies, discussed in an analysis of the primary hydration process Biopolymers 21 1982 403 418
    • (1982) Biopolymers , vol.21 , pp. 403-418
    • Luscher-Mattli, M.1    Ruegg, M.2
  • 54
    • 0001676491 scopus 로고
    • Adsorption of water vapor by proteins
    • H.B. Bull Adsorption of water vapor by proteins J. Am. Chem. Soc. 66 1944 1499 1507
    • (1944) J. Am. Chem. Soc. , vol.66 , pp. 1499-1507
    • Bull, H.B.1
  • 55
    • 0025870959 scopus 로고
    • On the importance of the support material for enzymatic synthesis in organic media. Support effects at controlled water activity
    • P. Adlercreutz On the importance of the support material for enzymatic synthesis in organic media. Support effects at controlled water activity Eur. J. Biochem. 199 1991 609 614
    • (1991) Eur. J. Biochem. , vol.199 , pp. 609-614
    • Adlercreutz, P.1
  • 56
    • 0023645793 scopus 로고
    • Time-domain reflectrometry studies of water binding and structural flexibility in chymotrypsin
    • S. Bone Time-domain reflectrometry studies of water binding and structural flexibility in chymotrypsin Biochim. Biophys. Acta 916 1987 128 134
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 128-134
    • Bone, S.1
  • 57
    • 0031573469 scopus 로고    scopus 로고
    • Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution
    • A. Dong, B. Kendrick, L. Kreigard, J. Matsuura, M.C. Manning, and J.F. Carpenter Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution Arch. Biochem. Biophys. 347 1997 213 220
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 213-220
    • Dong, A.1    Kendrick, B.2    Kreigard, L.3    Matsuura, J.4    Manning, M.C.5    Carpenter, J.F.6
  • 58
    • 0034801424 scopus 로고    scopus 로고
    • Native-like enzyme properties are important for optimum activity in neat organic solvents
    • K. Griebenow, M. Vidal, C. Baez, A.M. Santos, and G. Barletta Native-like enzyme properties are important for optimum activity in neat organic solvents J. Am. Chem. Soc. 123 2001 5380 5381
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5380-5381
    • Griebenow, K.1    Vidal, M.2    Baez, C.3    Santos, A.M.4    Barletta, G.5
  • 59
    • 0017745594 scopus 로고
    • Study of solid-state enzyme reactions: 2. Chymotryptic hydrolysis of N-succinyl-l-phenylalanine-p-nitroanilide
    • Y.I. Khurgin, N.V. Medvedeva, and V.Y. Roslyakov Study of solid-state enzyme reactions: 2. Chymotryptic hydrolysis of N-succinyl-l-phenylalanine-p- nitroanilide Biofizika 22 1977 1010 1014
    • (1977) Biofizika , vol.22 , pp. 1010-1014
    • Khurgin, Y.I.1    Medvedeva, N.V.2    Roslyakov, V.Y.3
  • 60
    • 0036117612 scopus 로고    scopus 로고
    • Chemical modification causes similar change in dependence on water activity of chymotrypsin hydration and catalysis in hexane
    • D.G. Rees, I.I. Gerashchenko, E.V. Kudryshova, V.V. Mozhaev, and P.J. Halling Chemical modification causes similar change in dependence on water activity of chymotrypsin hydration and catalysis in hexane Biocatal. Biotransform. 20 2002 161 166
    • (2002) Biocatal. Biotransform. , vol.20 , pp. 161-166
    • Rees, D.G.1    Gerashchenko, I.I.2    Kudryshova, E.V.3    Mozhaev, V.V.4    Halling, P.J.5
  • 61
    • 21844470225 scopus 로고    scopus 로고
    • Practical route to high activity enzyme preparations for synthesis in organic media
    • J. Partridge, P.J. Halling, and B.D. Moore Practical route to high activity enzyme preparations for synthesis in organic media Chem. Commun. 1998 841 842
    • (1998) Chem. Commun. , pp. 841-842
    • Partridge, J.1    Halling, P.J.2    Moore, B.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.