메뉴 건너뛰기




Volumn 26, Issue 5-6, 2000, Pages 342-347

Influence of water activity and aqueous solvent ordering on enzyme kinetics of alcohol dehydrogenase, lysozyme, and β-galactosidase

Author keywords

Enzyme kinetics; Enzyme substrate affinity; Hydrophobic interaction; Solvent ordering; Water activity

Indexed keywords

ADDITION REACTIONS; ALCOHOLS; ELECTROLYTES; HYDROPHOBICITY; ORGANIC SOLVENTS; SOLUTIONS; SUBSTRATES; SUGARS; THERMODYNAMIC PROPERTIES; UREA; WATER;

EID: 0033996124     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(99)00182-9     Document Type: Article
Times cited : (21)

References (28)
  • 2
    • 0022726316 scopus 로고
    • Water activity: A possible external regulator in biotechnical processes
    • Harn-Hagerdal B. Water activity a possible external regulator in biotechnical processes . Enzyme Microbiol Technol. 8:1986;322-327.
    • (1986) Enzyme Microbiol Technol , vol.8 , pp. 322-327
    • Harn-Hagerdal, B.1
  • 3
    • 0023224261 scopus 로고
    • Enzyme action in polymer and salt solutions. II. Activity of penicillin acylase in poly (ethylen glycol) and potassium phosphate solutions in relation to water activity
    • Andersson E., Harn-Hagerdal B. Enzyme action in polymer and salt solutions. II. Activity of penicillin acylase in poly (ethylen glycol) and potassium phosphate solutions in relation to water activity. Biochim Biophys Acta. 912:1987;325-328.
    • (1987) Biochim Biophys Acta , vol.912 , pp. 325-328
    • Andersson, E.1    Harn-Hagerdal, B.2
  • 4
    • 0024061584 scopus 로고    scopus 로고
    • Effect of thermodynamic water activity on thermolysin-catalyzed peptide synthesis in organic two-phase systems
    • Cassells J.M., Halling P.J. Effect of thermodynamic water activity on thermolysin-catalyzed peptide synthesis in organic two-phase systems. Enzyme Microb Technol. 10:1998;486-491.
    • (1998) Enzyme Microb Technol , vol.10 , pp. 486-491
    • Cassells, J.M.1    Halling, P.J.2
  • 5
    • 85022445806 scopus 로고
    • Physical-chemical nature of low water systems for biocatalysis: Especially phase behavior, water activity and pH
    • J. Tramper. New York: Elsevier Science Pub
    • Halling P.J., Valivery R.H. Physical-chemical nature of low water systems for biocatalysis especially phase behavior, water activity and pH . Tramper J. Biocatalysis in Non-conventional Media. 1992;13-21 Elsevier Science Pub, New York.
    • (1992) Biocatalysis in Non-conventional Media , pp. 13-21
    • Halling, P.J.1    Valivery, R.H.2
  • 6
    • 0032032060 scopus 로고    scopus 로고
    • Lipase-catalyzed enantioselective esterification of ibuprofen in organic solvents under controlled water activity
    • Ducret A., Trani M., Lortie R. Lipase-catalyzed enantioselective esterification of ibuprofen in organic solvents under controlled water activity. Enzyme Microb Technol. 22:1998;212-216.
    • (1998) Enzyme Microb Technol , vol.22 , pp. 212-216
    • Ducret, A.1    Trani, M.2    Lortie, R.3
  • 7
    • 50749132202 scopus 로고
    • Water activity: A credible measure of food safety and quality?
    • Franks F. Water activity a credible measure of food safety and quality? Trends Food Sci Technol. 1991;68-73.
    • (1991) Trends Food Sci Technol , pp. 68-73
    • Franks, F.1
  • 8
    • 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
    • Bell G., Janssen A.E.M., Halling P.J. 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
  • 9
    • 0021699812 scopus 로고
    • Effect of water activity on enzyme action and stability
    • Monsan P., Combes D. Effect of water activity on enzyme action and stability. Ann NY Acad Sci. 434:1984;48-60.
    • (1984) Ann NY Acad Sci , vol.434 , pp. 48-60
    • Monsan, P.1    Combes, D.2
  • 11
    • 0023274228 scopus 로고
    • Enzyme action in polymer and salt solutions. I. Stability of penicillin acylase in poly(ethylene glycol) and potassium phosphate solutions in relation to water activity
    • Andersson E., Harn-Hagerdal B. Enzyme action in polymer and salt solutions. I. Stability of penicillin acylase in poly(ethylene glycol) and potassium phosphate solutions in relation to water activity. Biochim Biophys Acta. 912:1987;317-324.
    • (1987) Biochim Biophys Acta , vol.912 , pp. 317-324
    • Andersson, E.1    Harn-Hagerdal, B.2
  • 12
    • 0029035407 scopus 로고
    • Effect of water activity on enzyme hydration and enzyme reaction rate in organic solvents
    • Lee S.B., Kim K.J. 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
  • 13
    • 0013807126 scopus 로고
    • On the conformational stability of globular proteins
    • Von Hippel P.H., Wong K.-Y. On the conformational stability of globular proteins. J Biol Chem. 240:1965;3909-3923.
    • (1965) J Biol Chem , vol.240 , pp. 3909-3923
    • Von Hippel, P.H.1    Wong, K.-Y.2
  • 14
    • 33745503743 scopus 로고
    • Ion effects on the solution structure on biological macromolecules
    • Von Hippel P.H., Schleich T. Ion effects on the solution structure on biological macromolecules. Acc Chem Res. 2:1969;257-265.
    • (1969) Acc Chem Res , vol.2 , pp. 257-265
    • Von Hippel, P.H.1    Schleich, T.2
  • 15
    • 0023663689 scopus 로고
    • Hydrophobic stabilization of chiton hemocyanins: Effects of ureas, Hofmeister salts and pH on their dissociation
    • Herskovits T.T., Hamilton M.G. Hydrophobic stabilization of chiton hemocyanins effects of ureas, Hofmeister salts and pH on their dissociation . Biochim Biophys Acta. 915:1987;157-167.
    • (1987) Biochim Biophys Acta , vol.915 , pp. 157-167
    • Herskovits, T.T.1    Hamilton, M.G.2
  • 16
    • 0025963927 scopus 로고
    • The effect of salt on the michaelis menten constant of the HIV-I protease correlates with the Hofmeister series
    • Wondrak E.M., Louis J.M., Oroszlan S. The effect of salt on the michaelis menten constant of the HIV-I protease correlates with the Hofmeister series. FEBS Lett. 2:1991;344-346.
    • (1991) FEBS Lett , vol.2 , pp. 344-346
    • Wondrak, E.M.1    Louis, J.M.2    Oroszlan, S.3
  • 17
    • 84988122198 scopus 로고
    • The effect of Hofmeister anions and protein concentration on the activity and stability of some immobilized NAD-dehydrogenases
    • Carrea G., Bovara R., Pasta P. The effect of Hofmeister anions and protein concentration on the activity and stability of some immobilized NAD-dehydrogenases. Biotechnol Bioeng. 24:1982;1-7.
    • (1982) Biotechnol Bioeng , vol.24 , pp. 1-7
    • Carrea, G.1    Bovara, R.2    Pasta, P.3
  • 18
    • 0030994063 scopus 로고    scopus 로고
    • Activity and activity coefficient of water in aqueous solutions and their relationships with solution structure parameters
    • Miyawaki O., Saito A., Matsuo T., Nakamura K. Activity and activity coefficient of water in aqueous solutions and their relationships with solution structure parameters. Biosci Biotech Biochem. 61:1997;466-469.
    • (1997) Biosci Biotech Biochem , vol.61 , pp. 466-469
    • Miyawaki, O.1    Saito, A.2    Matsuo, T.3    Nakamura, K.4
  • 19
    • 36849096669 scopus 로고
    • Solute-solute interactions in aqueous solutions
    • Kozak J.J., Knight W.S., Kauzmann W. Solute-solute interactions in aqueous solutions. J Phys Chem. 48:1968;675-690.
    • (1968) J Phys Chem , vol.48 , pp. 675-690
    • Kozak, J.J.1    Knight, W.S.2    Kauzmann, W.3
  • 20
    • 37049042891 scopus 로고
    • Ion-solvent interaction and the viscosity of strong-electrolyte solutions
    • Kaminsky M. Ion-solvent interaction and the viscosity of strong-electrolyte solutions. Discus Faraday Soc. 24:1957;171-179.
    • (1957) Discus Faraday Soc , vol.24 , pp. 171-179
    • Kaminsky, M.1
  • 21
    • 33947087378 scopus 로고
    • Viscosity studies of aqueous solutions of alcohols, ureas, and amides
    • Herskovits T.T., Kelly T.M. Viscosity studies of aqueous solutions of alcohols, ureas, and amides. J Phys Chem. 77:1973;381-388.
    • (1973) J Phys Chem , vol.77 , pp. 381-388
    • Herskovits, T.T.1    Kelly, T.M.2
  • 22
    • 0002317448 scopus 로고
    • Natural-abundance oxygen-17 magnetic relaxation in aqueous solutions of carbohydrates
    • Uedaira H., Ikura M., Uedaira H. Natural-abundance oxygen-17 magnetic relaxation in aqueous solutions of carbohydrates. Bull Chem Soc Jpn. 62:1989;1-4.
    • (1989) Bull Chem Soc Jpn , vol.62 , pp. 1-4
    • Uedaira, H.1    Ikura, M.2    Uedaira, H.3
  • 24
    • 0000572928 scopus 로고    scopus 로고
    • Dielectric relaxation of aqueous solution with low-molecular-weight nonelectrolytes and its relationship with solution structure
    • Saito A., Miyawaki O., Nakamura K. Dielectric relaxation of aqueous solution with low-molecular-weight nonelectrolytes and its relationship with solution structure. Biosci Biotech Biochem. 61:1997;1831-1835.
    • (1997) Biosci Biotech Biochem , vol.61 , pp. 1831-1835
    • Saito, A.1    Miyawaki, O.2    Nakamura, K.3
  • 25
    • 0030021877 scopus 로고    scopus 로고
    • Computational method for relative binding energies of enzyme-substrate complexes
    • Zhang T., Koshland D.E. Computational method for relative binding energies of enzyme-substrate complexes. Protein Sci. 5:1996;348-356.
    • (1996) Protein Sci , vol.5 , pp. 348-356
    • Zhang, T.1    Koshland, D.E.2
  • 26
    • 0001691414 scopus 로고
    • Effects of sugar solutions on the activity coefficients of aromatic amino acids and their N-acetyl ethyl esters
    • Lakshmi T.S., Nandi P.K. Effects of sugar solutions on the activity coefficients of aromatic amino acids and their N-acetyl ethyl esters. J Phys Chem. 80:1976;249-252.
    • (1976) J Phys Chem , vol.80 , pp. 249-252
    • Lakshmi, T.S.1    Nandi, P.K.2
  • 27
    • 78651119214 scopus 로고
    • The solubility of amino acids and related compounds in aqueous urea solutions
    • Nozaki Y., Tanford C. The solubility of amino acids and related compounds in aqueous urea solutions. J Biol Chem. 238:1963;4074-4081.
    • (1963) J Biol Chem , vol.238 , pp. 4074-4081
    • Nozaki, Y.1    Tanford, C.2
  • 28
    • 0029417045 scopus 로고
    • Thermodynamics of denaturation of α-chymotrypsinogen A in aqueous urea and alkyl urea solutions
    • Poklar N., Vesnaver G., Lapanje S. Thermodynamics of denaturation of α-chymotrypsinogen A in aqueous urea and alkyl urea solutions. J Protein Chem. 14:1995;709-719.
    • (1995) J Protein Chem , vol.14 , pp. 709-719
    • Poklar, N.1    Vesnaver, G.2    Lapanje, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.