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Volumn , Issue , 2008, Pages 107-153

Homogeneous enzyme kinetics

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EID: 84890010855     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4020-8361-7_3     Document Type: Chapter
Times cited : (22)

References (65)
  • 1
    • 33749506414 scopus 로고    scopus 로고
    • Relations between biochemical themodyamics and biochemical kinetics
    • Alberty RA (2006) Relations between biochemical themodyamics and biochemical kinetics. Biophys Chem 124:11-17
    • (2006) Biophys Chem , vol.124 , pp. 11-17
    • Alberty, R.A.1
  • 2
    • 0033596744 scopus 로고    scopus 로고
    • Comparing the thermodynamic stabilities of a related thermophilic and mesophilic enzyme
    • Beadle BM, Baase WA, Wilson DB et al. (1999) Comparing the thermodynamic stabilities of a related thermophilic and mesophilic enzyme. Biochemistry 38(8):2570-2576
    • (1999) Biochemistry , vol.38 , Issue.8 , pp. 2570-2576
    • Beadle, B.M.1    Baase, W.A.2    Wilson, D.B.3
  • 3
    • 0019962812 scopus 로고
    • Effects of pH, ionic strength and temperature on activation by calmodulin and catalytic activity of myosin light chain kinase
    • Blumenthal DK, Stull JT (1982) Effects of pH, ionic strength and temperature on activation by calmodulin and catalytic activity of myosin light chain kinase. Biochemistry 21:2386-2391
    • (1982) Biochemistry , vol.21 , pp. 2386-2391
    • Blumenthal, D.K.1    Stull, J.T.2
  • 4
    • 28244497820 scopus 로고    scopus 로고
    • Established and novel tools to investigate biocatalyst stability
    • Bommarius AS, Broering JM (2005) Established and novel tools to investigate biocatalyst stability. Biocatal Biotransform 23(3/4):125-139
    • (2005) Biocatal Biotransform , vol.23 , Issue.3-4 , pp. 125-139
    • Bommarius, A.S.1    Broering, J.M.2
  • 6
    • 0035956268 scopus 로고    scopus 로고
    • Alcoholysis catalyzed by Candida antarctica lipase B in a gas/solid system obeys a ping pong bi bi mechanism with competitive inhibition by the alcohol substrate and water
    • Bousquet-Dubouch MP, Graber M, Sousa N et al. (2001) Alcoholysis catalyzed by Candida antarctica lipase B in a gas/solid system obeys a ping pong bi bi mechanism with competitive inhibition by the alcohol substrate and water. Biochim Biophys Acta 1550:90-99
    • (2001) Biochim Biophys Acta , vol.1550 , pp. 90-99
    • Bousquet-Dubouch, M.P.1    Graber, M.2    Sousa, N.3
  • 7
    • 0000292524 scopus 로고
    • A note on the kinetics of enzyme action
    • Briggs GE, Haldane JBS (1925) A note on the kinetics of enzyme action. Biochem J 19:338-339
    • (1925) Biochem J , vol.19 , pp. 338-339
    • Briggs, G.E.1    Haldane, J.B.S.2
  • 9
    • 0034237245 scopus 로고    scopus 로고
    • Effect of thermal and chemical denaturants on Thermoanaerobacter ethanolicus secondary-Alcohol dehydrogenase stability and activity
    • Burdette D, Tchernajencko V, Zeikus J (2000) Effect of thermal and chemical denaturants on Thermoanaerobacter ethanolicus secondary-Alcohol dehydrogenase stability and activity. Enzyme Microb Technol 27:11-18
    • (2000) Enzyme Microb Technol , vol.27 , pp. 11-18
    • Burdette, D.1    Tchernajencko, V.2    Zeikus, J.3
  • 11
    • 0023451469 scopus 로고
    • Substrate protection of immobilized glucose isomerase
    • Chen K, Wu J (1987) Substrate protection of immobilized glucose isomerase. Biotechnol Bioeng 30:817-824
    • (1987) Biotechnol Bioeng , vol.30 , pp. 817-824
    • Chen, K.1    Wu, J.2
  • 12
    • 50549159930 scopus 로고
    • The kinetic of enzyme-catalysed reactions with two or more substrates or products. Nomenclature and rate equations
    • Cleland WW (1963) The kinetic of enzyme-catalysed reactions with two or more substrates or products. Nomenclature and rate equations. Biochim Biophys Acta 67:104-137
    • (1963) Biochim Biophys Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 14
    • 0017258037 scopus 로고
    • Estimation of the dissociation constants of enzyme-substrate complexes from steady-state measurements: Interpretation of pH-independence of Km
    • Cornish-Bowden A (1976) Estimation of the dissociation constants of enzyme-substrate complexes from steady-state measurements: Interpretation of pH-independence of Km. Biochem J 153:455-461
    • (1976) Biochem J , vol.153 , pp. 455-461
    • Cornish-Bowden, A.1
  • 16
    • 0020751468 scopus 로고
    • Ionic strength: A neglected variable in enzyme technology
    • Dale E, White D (1982) Ionic strength: A neglected variable in enzyme technology. Enzyme Microb Technol 5(3):227-229
    • (1982) Enzyme Microb Technol , vol.5 , Issue.3 , pp. 227-229
    • Dale, E.1    White, D.2
  • 17
    • 0004262303 scopus 로고
    • 3rd edn. Academic Press New York
    • Dixon M, Webb EC (1979) Enzymes, 3rd edn. Academic Press, New York, 1116
    • (1979) Enzymes , pp. 1116
    • Dixon, M.1    Webb, E.C.2
  • 18
    • 0016167076 scopus 로고
    • The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters
    • Eisenthal R, Cornish-Bowden A (1974) The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. Biochem J 139(3):715-720
    • (1974) Biochem J , vol.139 , Issue.3 , pp. 715-720
    • Eisenthal, R.1    Cornish-Bowden, A.2
  • 19
    • 0030899458 scopus 로고    scopus 로고
    • Cross-linked stabilization of Escherichia coli penicillin G acylase against pH by dextran-dialdedhyde polymers
    • Ertan H, Kazan D, Erarslan (1997) Cross-linked stabilization of Escherichia coli penicillin G acylase against pH by dextran-dialdedhyde polymers. Biotechnol Tech 11:225-229
    • (1997) Biotechnol Tech , vol.11 , pp. 225-229
    • Ertan, H.1    Kazan D Erarslan2
  • 20
    • 0346725120 scopus 로고    scopus 로고
    • Activity and stability of immobilized penicillin acylase at low pH values
    • Ferreira JS, Straathof AJJ, Franco TT et al. (2004) Activity and stability of immobilized penicillin acylase at low pH values. J Mol Catal B Enzym 27:29-35
    • (2004) J Mol Catal B Enzym , vol.27 , pp. 29-35
    • Ferreira, J.S.1    Straathof, A.J.J.2    Franco, T.T.3
  • 21
    • 85047694896 scopus 로고    scopus 로고
    • Ph stability of penicillin acylase from Escherichia coli
    • Guranda DT, Volovik TS, & Švedas VK (2004) pH stability of penicillin acylase from Escherichia coli. Biochemistry (Moscow) 69(12):1700-1705
    • (2004) Biochemistry (Moscow , vol.69 , Issue.12 , pp. 1700-1705
    • Guranda, D.T.1    Volovik, T.S.2    Švedas, V.K.3
  • 22
    • 0001465376 scopus 로고
    • Studies on plant amylases: The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley
    • Hanes CS (1932) Studies on plant amylases: The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley. Biochem J 26:1406-1421
    • (1932) Biochem J , vol.26 , pp. 1406-1421
    • Hanes, C.S.1
  • 23
    • 0027970374 scopus 로고
    • Ionic strength dependence of the reaction between methanol dehydrogenase and cytochrome c-551i: Evidence of conformationally coupled electro transfer
    • Harris TK, Davidson VL, Chen L et al. (1994) Ionic strength dependence of the reaction between methanol dehydrogenase and cytochrome c-551i: Evidence of conformationally coupled electro transfer. Biochemistry 33:12600-12608
    • (1994) Biochemistry , vol.33 , pp. 12600-12608
    • Harris, T.K.1    Davidson, V.L.2    Chen, L.3
  • 24
    • 0026016270 scopus 로고
    • Ionic strength dependence on the kinetics of electron transfer from bovine mitochondrial cytochrome C to bovine cytochrome c oxidase
    • Hazzard JT, Rong SY, Tollin G (1991) Ionic strength dependence on the kinetics of electron transfer from bovine mitochondrial cytochrome C to bovine cytochrome c oxidase. Biochemistry 30:213-222
    • (1991) Biochemistry , vol.30 , pp. 213-222
    • Hazzard, J.T.1    Rong, S.Y.2    Tollin, G.3
  • 25
  • 26
    • 0022013872 scopus 로고
    • Categorization of enzyme deactivation using a series type mechanism
    • Henley J, Sadana A (1985) Categorization of enzyme deactivation using a series type mechanism. Enzyme Microb Technol 7:50-60
    • (1985) Enzyme Microb Technol , vol.7 , pp. 50-60
    • Henley, J.1    Sadana, A.2
  • 28
    • 0016816804 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme?
    • Hodgson EK, Fridovich I (1975) The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme? Biochemistry 14(24):5294-5299
    • (1975) Biochemistry , vol.14 , Issue.24 , pp. 5294-5299
    • Hodgson, E.K.1    Fridovich, I.2
  • 29
    • 0001395234 scopus 로고
    • Non-inverted versus inverted plots in enzyme kinetics
    • Hofstee BHJ (1959) Non-inverted versus inverted plots in enzyme kinetics. Nature 184:1296-1298
    • (1959) Nature , vol.184 , pp. 1296-1298
    • Hofstee, B.H.J.1
  • 30
    • 0027551647 scopus 로고
    • Analysis of substrate protection of an immobilized glucose isomerase reactor
    • Houng JY, Yu, HY, Chen KC (1993) Analysis of substrate protection of an immobilized glucose isomerase reactor. Biotechnol Bioeng 41:451-458
    • (1993) Biotechnol Bioeng , vol.41 , pp. 451-458
    • Houng, J.Y.1    Yu, H.Y.2    Chen, K.C.3
  • 31
    • 84890010739 scopus 로고
    • Inmovilización de glucoamilasa
    • Illanes A (1983) Inmovilización de glucoamilasa. Alimentos 8(3):22-27
    • (1983) Alimentos , vol.8 , Issue.3 , pp. 22-27
    • Illanes, A.1
  • 32
    • 0001424366 scopus 로고
    • Immobilization of lactase for the continuous hydrolysis of whey permeate
    • Illanes A, Ruiz A, ZúñigaME et al. (1990) Immobilization of lactase for the continuous hydrolysis of whey permeate. Bioproc Eng 5:257-262
    • (1990) Bioproc Eng , vol.5 , pp. 257-262
    • Illanes, A.1    Ruiz, A.2    Zúñiga, M.E.3
  • 33
    • 0002479119 scopus 로고
    • Enzyme reactor performance under thermal inactivation
    • Galindo E, Ramírez O (eds Kluwer Acad Publ, Dordrecht
    • Illanes A, Altamirano C, Cartagena O (1994) Enzyme reactor performance under thermal inactivation. In: Galindo E, Ramírez O (eds). Advances in bioprocess engineering. Kluwer Acad Publ, Dordrecht, pp 467-472
    • (1994) Advances In Bioprocess Engineering , pp. 467-472
    • Illanes, A.1    Altamirano, C.2    Cartagena, O.3
  • 34
    • 15844369202 scopus 로고    scopus 로고
    • Thermal inactivation of immobilized penicillin acylase in the presence of substrate and products
    • Illanes A, Altamirano C, Zuñiga M (1996) Thermal inactivation of immobilized penicillin acylase in the presence of substrate and products. Biotechnol Bioeng 50:609-616
    • (1996) Biotechnol Bioeng , vol.50 , pp. 609-616
    • Illanes, A.1    Altamirano, C.2    Zuñiga, M.3
  • 35
    • 0032127548 scopus 로고    scopus 로고
    • Packed-bed reactor performance with immobilized lactase under thermal inactivation
    • Illanes A, Altamirano C, Aillapán A et al. (1998) Packed-bed reactor performance with immobilized lactase under thermal inactivation. Enzyme Microb Technol 23:3-9
    • (1998) Enzyme Microb Technol , vol.23 , pp. 3-9
    • Illanes, A.1    Altamirano, C.2    Aillapán, A.3
  • 36
    • 0034255897 scopus 로고    scopus 로고
    • Temperature optimization for reactor operation with chitin-immobilized lactase under modulated inactivation
    • Illanes A, Wilson L, Tomasello G (2000) Temperature optimization for reactor operation with chitin-immobilized lactase under modulated inactivation. Enzyme Microb Technol 27:270-278
    • (2000) Enzyme Microb Technol , vol.27 , pp. 270-278
    • Illanes, A.1    Wilson, L.2    Tomasello, G.3
  • 37
    • 0032946805 scopus 로고    scopus 로고
    • Kinetics of lipase-catalysed esterification in organic media: Correct model and solvent effects on parameters
    • Janssen AEM, Sjursnes B, Vakurov AV et al. (1999) Kinetics of lipase-catalysed esterification in organic media: Correct model and solvent effects on parameters. Enzyme Microb Technol 24:463-470
    • (1999) Enzyme Microb Technol , vol.24 , pp. 463-470
    • Janssen, A.E.M.1    Sjursnes, B.2    Vakurov, A.V.3
  • 38
    • 23744433879 scopus 로고    scopus 로고
    • Kinetic of the thermal and pH inactivation of a thermostable β-galactosidase from Thermus sp. strain T2
    • Ladero M, Ferrero R, Vian A et al. (2005) Kinetic of the thermal and pH inactivation of a thermostable β-galactosidase from Thermus sp. strain T2. Enzyme Microb Technol 37:505-513
    • (2005) Enzyme Microb Technol , vol.37 , pp. 505-513
    • Ladero, M.1    Ferrero, R.2    Vian, A.3
  • 40
    • 0015307330 scopus 로고
    • Enzyme kinetics. Systematic generation of valid King-Altman patterns
    • Lam CF, Priest DG (1972) Enzyme kinetics. Systematic generation of valid King-Altman patterns. Biophys J 12:248:256
    • (1972) Biophys J , vol.12 , Issue.248 , pp. 256
    • Lam, C.F.1    Priest, D.G.2
  • 41
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H, Burk D (1934) The determination of enzyme dissociation constants. J Am Chem Soc 56:658-666
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 43
    • 0031031949 scopus 로고    scopus 로고
    • Effect of pH on kinetic parameters of NAD+ dependent formate dehydrogenase
    • Mesentsev AV, Lamzin VS, Tishkov VI et al. (1997) Effect of pH on kinetic parameters of NAD+ dependent formate dehydrogenase. Biochem J 321(2):475-480
    • (1997) Biochem J , vol.321 , Issue.2 , pp. 475-480
    • Mesentsev, A.V.1    Lamzin, V.S.2    Tishkov, V.I.3
  • 45
    • 84889973963 scopus 로고
    • The theory of the isoelectric effect
    • Michaelis L, Davidsohn, H (1911) The theory of the isoelectric effect. Biochem Z 30:143-150
    • (1911) Biochem Z , vol.30 , pp. 143-150
    • Michaelis, L.1    Davidsohn, H.2
  • 46
    • 0000870544 scopus 로고
    • Die kinetik der invertinwirkung
    • Michaelis L, Menten M (1913) Die kinetik der invertinwirkung. Biochem Z 49:333-369
    • (1913) Biochem Z , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.2
  • 47
    • 77957094108 scopus 로고
    • Stability of industrial enzymes
    • van den TweelW, Harder A, Buitelaar R (eds Elsevier, Amsterdam
    • Misset O (1993) Stability of industrial enzymes. In: Van den TweelW, Harder A, Buitelaar R (eds). Stability and stabilization of enzymes. Elsevier, Amsterdam, pp 111-131
    • (1993) Stability And Stabilization Of Enzymes , pp. 111-131
    • Misset, O.1
  • 48
    • 0021800102 scopus 로고
    • Microcomputer tools for steady-state enzyme kinetics
    • Myers D, Palmer G (1985) Microcomputer tools for steady-state enzyme kinetics. Comput Appl Biosci 1:105-110
    • (1985) Comput Appl Biosci , vol.1 , pp. 105-110
    • Myers, D.1    Palmer, G.2
  • 49
    • 0019317512 scopus 로고
    • Effective charge on acetylcholinesterase active site determined from the ionic strength dependence of association rate constants with cationic ligands
    • Nolte HJ, Rosenberry TL, Neumann E (1980) Effective charge on acetylcholinesterase active site determined from the ionic strength dependence of association rate constants with cationic ligands. Biochemistry 19:3705-3711
    • (1980) Biochemistry , vol.19 , pp. 3705-3711
    • Nolte, H.J.1    Rosenberry, T.L.2    Neumann, E.3
  • 50
    • 1642489328 scopus 로고    scopus 로고
    • Enzyme stabilization recent experimental progress
    • O'Fágáin C (2003) Enzyme stabilization recent experimental progress. Enzyme Microb Technol 33:137:149
    • (2003) Enzyme Microb Technol , vol.33 , Issue.137 , pp. 149
    • O'Fágáin, C.1
  • 51
    • 0015337408 scopus 로고
    • Thermal inactivation of immobilized enzymes in continuous reactors
    • O'Neill S (1972) Thermal inactivation of immobilized enzymes in continuous reactors. Biotechnol Bioeng 14:473-491
    • (1972) Biotechnol Bioeng , vol.14 , pp. 473-491
    • O'Neill, S.1
  • 52
    • 0031597088 scopus 로고    scopus 로고
    • Stabilization of β-glucosidase entrapped in alginate and polyacrylamide gels towards thermal and proteolytic deactivation
    • Ortega N, Busto M, Pérez-Mateos M (1998) Stabilization of β-glucosidase entrapped in alginate and polyacrylamide gels towards thermal and proteolytic deactivation. J Chem Technol Biotechnol 73:7-12
    • (1998) J Chem Technol Biotechnol , vol.73 , pp. 7-12
    • Ortega, N.1    Busto, M.2    Pérez-Mateos, M.3
  • 54
    • 0033580816 scopus 로고    scopus 로고
    • Variation in the steady state kinetic parameters of wild type and mutant T5 5′-3′-exonuclease with pH
    • Pickering TJ, Garforth S, Sayers JR et al. (1999) Variation in the steady state kinetic parameters of wild type and mutant T5 5′-3′- exonuclease with pH. J Biol Chem 274:17711-17717
    • (1999) J Biol Chem , vol.274 , pp. 17711-17717
    • Pickering, T.J.1    Garforth, S.2    Sayers, J.R.3
  • 55
    • 33745056511 scopus 로고
    • Eyring transition-state theory and kinetics in catalysis
    • Rooney JJ (1995) Eyring transition-state theory and kinetics in catalysis. J Mol Catal A Chemical 96(1):1-3
    • (1995) J Mol Catal A Chemical , vol.96 , Issue.1 , pp. 1-3
    • Rooney, J.J.1
  • 56
    • 0032911297 scopus 로고    scopus 로고
    • Kinetics of thermal inactivation of the extracellular proteinase from Pseudomonas fluorescens 22F: Influence of pH, calcium and protein
    • Schokker E, van Boekel M (1999) Kinetics of thermal inactivation of the extracellular proteinase from Pseudomonas fluorescens 22F: Influence of pH, calcium and protein. J Agric Food Chem 47:1681-1686
    • (1999) J Agric Food Chem , vol.47 , pp. 1681-1686
    • Schokker, E.1    Van Boekel, M.2
  • 57
    • 0023287616 scopus 로고
    • Immobilized cells. rfeti A review of recent literature
    • Scott CD (1987) Immobilized cells. A review of recent literature. Enzyme Microb Technol 9:6-73
    • (1987) Enzyme Microb Technol , vol.9 , pp. 6-73
    • Scott, C.D.1
  • 60
    • 0026816677 scopus 로고
    • Activity and stability of yeast alcohol dehydrogenase (YADH) entrapped in aerosol OT reverse micelles
    • Shraboni S, Jain TK, Maitra A (1992) Activity and stability of yeast alcohol dehydrogenase (YADH) entrapped in aerosol OT reverse micelles. Biotechnol Bioeng 39(4):474-478
    • (1992) Biotechnol Bioeng , vol.39 , Issue.4 , pp. 474-478
    • Shraboni, S.1    Jain, T.K.2    Maitra, A.3
  • 61
    • 0018089784 scopus 로고
    • Generalized rate equation for one-substrate enzymatic reactions
    • Siimer E (1978) Generalized rate equation for one-substrate enzymatic reactions. Biotechnol Bioeng 20(12):1853-1864
    • (1978) Biotechnol Bioeng , vol.20 , Issue.12 , pp. 1853-1864
    • Siimer, E.1
  • 62
    • 0029636671 scopus 로고
    • Do organic solvents affect the catalytic properties of lipase? Intrinsic kinetic parameters of lipases in ester hydrolysis and formation in various organic solvents
    • van Tol JBA, Stevens RMM, Veldhuizen WJ et al. (1995) Do organic solvents affect the catalytic properties of lipase? Intrinsic kinetic parameters of lipases in ester hydrolysis and formation in various organic solvents. Biotechnol Bioeng 47:71-81
    • (1995) Biotechnol Bioeng , vol.47 , pp. 71-81
    • Van Tol, J.B.A.1    Stevens, R.M.M.2    Veldhuizen, W.J.3
  • 63
    • 0025454631 scopus 로고
    • Catalysis may increase the stability of an enzyme: The example of horse liver alcohol dehydrogenase
    • Villaume I, Thoma, D, Legoy M (1990) Catalysis may increase the stability of an enzyme: The example of horse liver alcohol dehydrogenase. Enzyme Microb Technol 12:506-509
    • (1990) Enzyme Microb Technol , vol.12 , pp. 506-509
    • Villaume, I.1    Thoma, D.2    Legoy, M.3
  • 64
    • 0020373352 scopus 로고
    • Product activation of pancreatic lipase
    • Wieloch T, Borgstrom B, Piéroni G et al. (1982) Product activation of pancreatic lipase. J Biol Chem 19(10):11523-11528
    • (1982) J Biol Chem , vol.19 , Issue.10 , pp. 11523-11528
    • Wieloch, T.1    Borgstrom, B.2    Piéroni, G.3
  • 65
    • 0012863492 scopus 로고    scopus 로고
    • Kinetics of thermal inactivation of Penaeus penicillatus acid phosphatase
    • Yang P, Chen Q, Xie Z et al. (1999) Kinetics of thermal inactivation of Penaeus penicillatus acid phosphatase. Biochemistry (Moscow) 64:464-467
    • (1999) Biochemistry (Moscow , vol.64 , pp. 464-467
    • Yang, P.1    Chen, Q.2    Xie, Z.3


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