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Volumn 26, Issue 1, 2010, Pages 73-78

Mechanistic model for prediction of formate dehydrogenase kinetics under industrially relevant conditions

Author keywords

Biocatalysis; Cofactor regeneration; Formate dehydrogenase; Process modeling

Indexed keywords

BATCH REACTIONS; BIOCATALYSIS; CANDIDA BOIDINII; COFACTOR REGENERATION; COFACTORS; COST EFFICIENCY; FORMATE DEHYDROGENASE; HIGH CONCENTRATION; INDUSTRIAL ENZYMES; INITIAL RATE; LITERATURE MODELS; MECHANISTIC MODELS; PREDICTION ERRORS; PROCESS CONDITION; PROCESS MODELING; PROGRESS CURVES; REACTION COURSE; REGENERATION REACTIONS; TIME HORIZONS;

EID: 76849093989     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.282     Document Type: Article
Times cited : (19)

References (36)
  • 4
    • 0032530505 scopus 로고    scopus 로고
    • Biocatalysis to amino acid-based chiral pharmaceuticals-examples and perspectives
    • Bommarius AS, Schwarm M, Drauz K. Biocatalysis to amino acid-based chiral pharmaceuticals-examples and perspectives. J Mol Catal B: Enzym. 1998;5:1-11.
    • (1998) J Mol Catal B: Enzym , vol.5 , pp. 1-11
    • Bommarius, A.S.1    Schwarm, M.2    Drauz, K.3
  • 5
    • 28844501226 scopus 로고    scopus 로고
    • Deactivation of formate dehydrogenase (FDH) in solution and at gas-liquid interfaces
    • Bommarius AS, Karau A. Deactivation of formate dehydrogenase (FDH) in solution and at gas-liquid interfaces. Biotechnol Prog. 2005;21:1663-1672.
    • (2005) Biotechnol Prog , vol.21 , pp. 1663-1672
    • Bommarius, A.S.1    Karau, A.2
  • 8
    • 0035931416 scopus 로고    scopus 로고
    • Preparative regioand chemoselective functionalization of hydrocarbons catalyzed by cell free preparations of 2-hydroxybiphenyl 3-monooxygen-ase
    • Schmid A, Vereyken I, Held M, Witholt B. Preparative regioand chemoselective functionalization of hydrocarbons catalyzed by cell free preparations of 2-hydroxybiphenyl 3-monooxygen-ase. J Mol Catal B: Enzym. 2001;11:455-462.
    • (2001) J Mol Catal B: Enzym , vol.11 , pp. 455-462
    • Schmid, A.1    Vereyken, I.2    Held, M.3    Witholt, B.4
  • 9
    • 11144247396 scopus 로고    scopus 로고
    • Catalytic mechanism and application of formate dehydrogenase
    • Tishkov VI, Popov VO. Catalytic mechanism and application of formate dehydrogenase. Biochemistry Mosc. 2004;69:1252-1267.
    • (2004) Biochemistry Mosc , vol.69 , pp. 1252-1267
    • Tishkov, V.I.1    Popov, V.O.2
  • 10
    • 0018304791 scopus 로고
    • Steady-state kinetics of formalde-hyde dehydrogenase and formate dehydrogenase from a methanol-utilizing yeast Candida boidinii
    • Kato N, Sahm H, Wagner F. Steady-state kinetics of formalde-hyde dehydrogenase and formate dehydrogenase from a methanol-utilizing yeast Candida boidinii. Biochim Biophys Acta. 1979;566:12-20.
    • (1979) Biochim Biophys Acta , vol.566 , pp. 12-20
    • Kato, N.1    Sahm, H.2    Wagner, F.3
  • 11
    • 0019330801 scopus 로고
    • Kinetic and chemical mechanisms of yeast formate dehydrogenase
    • Blanchard JS, Cleland WW. Kinetic and chemical mechanisms of yeast formate dehydrogenase. Biochemistry 1980;19:3543-3550.
    • (1980) Biochemistry , vol.19 , pp. 3543-3550
    • Blanchard, J.S.1    Cleland, W.W.2
  • 12
    • 0017252385 scopus 로고
    • Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii
    • Schutte H, Flossdorf J, Sahm H, Kula MR. Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii. Eur J Biochem. 1976;62:151-160.
    • (1976) Eur J Biochem , vol.62 , pp. 151-160
    • Schutte, H.1    Flossdorf, J.2    Sahm, H.3    Kula, M.R.4
  • 13
    • 50549159930 scopus 로고
    • Kinetics of enzyme-catalyzed reactions with 2 or more substrates or products. 1. Nomenclature and rate equations
    • Cleland WW. Kinetics of enzyme-catalyzed reactions with 2 or more substrates or products. 1. Nomenclature and rate equations. Biochim Biophys Acta. 1963;67:104-137.
    • (1963) Biochim Biophys Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 14
    • 0018864834 scopus 로고
    • Influence of substrate or product inhibition on the performance of enzyme reactors
    • Kula MR, Wichmann R, Oden U, Wandrey C. Influence of substrate or product inhibition on the performance of enzyme reactors. Biochimie. 1980;62:523-536.
    • (1980) Biochimie , vol.62 , pp. 523-536
    • Kula, M.R.1    Wichmann, R.2    Oden, U.3    Wandrey, C.4
  • 16
    • 36749041423 scopus 로고    scopus 로고
    • Biotransformation of D-methionine into L-methionine in the cascade of four enzymes
    • Findrik Z, Vasic-Racki D. Biotransformation of D-methionine into L-methionine in the cascade of four enzymes. Biotechnol Bioeng. 2007;98:956-967.
    • (2007) Biotechnol Bioeng , vol.98 , pp. 956-967
    • Findrik, Z.1    Vasic-Racki, D.2
  • 17
    • 0000798607 scopus 로고
    • Isolation of L-phenylalanine dehydrogenase from Rhodococcus sp. M4 and its application for the production of L-phenylalanine
    • Hummel W, Schutte H, Schmidt E, Wandrey C, Kula MR. Isolation of L-phenylalanine dehydrogenase from Rhodococcus sp. M4 and its application for the production of L-phenylalanine. Appl Microbiol Biotechnol. 1987;26:409-416.
    • (1987) Appl Microbiol Biotechnol , vol.26 , pp. 409-416
    • Hummel, W.1    Schutte, H.2    Schmidt, E.3    Wandrey, C.4    Kula, M.R.5
  • 18
    • 0026873227 scopus 로고
    • Kontinuierliche Reaktkionsfuhrung mit loslichen Enzymen
    • Kragl U, Vasic-Racki D, Wandrey C. Kontinuierliche Reaktkionsfuhrung mit loslichen Enzymen. Chem Ing Tech. 1992;6: 499-509.
    • (1992) Chem Ing Tech , vol.6 , pp. 499-509
    • Kragl, U.1    Vasic-Racki, D.2    Wandrey, C.3
  • 19
    • 0029891893 scopus 로고    scopus 로고
    • Continuous production of L-tert-leucine in series of two enzyme membrane reactors
    • Kragl U, Vasic-Racki D, Wandrey C. Continuous production of L-tert-leucine in series of two enzyme membrane reactors. Bioprocess Biosyst Eng. 1996;V14:291-297.
    • (1996) Bioprocess Biosyst Eng , vol.14 , pp. 291-297
    • Kragl, U.1    Vasic-Racki, D.2    Wandrey, C.3
  • 21
    • 0033527817 scopus 로고    scopus 로고
    • Enzymatic reduction of a less watersoluble ketone in reverse micelles with NADH regeneration
    • Orlich B, Schomaecker R. Enzymatic reduction of a less watersoluble ketone in reverse micelles with NADH regeneration. Biotechnol Bioeng. 1999;65:357-362.
    • (1999) Biotechnol Bioeng , vol.65 , pp. 357-362
    • Orlich, B.1    Schomaecker, R.2
  • 22
    • 0026625840 scopus 로고
    • Optimization of a process for the production of (R)-2-hydroxy-4-phenylbutyric acid -an intermediate for inhibitors of angiotensin converting enzyme
    • Schmidt E, Ghisalba O, Gygax D, Sedelmeier G. Optimization of a process for the production of (R)-2-hydroxy-4-phenylbutyric acid -an intermediate for inhibitors of angiotensin converting enzyme. J Biotechnol. 1992;24:315-327.
    • (1992) J Biotechnol , vol.24 , pp. 315-327
    • Schmidt, E.1    Ghisalba, O.2    Gygax, D.3    Sedelmeier, G.4
  • 23
    • 84941889613 scopus 로고
    • Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration
    • Wichmann R, Wandrey C, Buckmann AF, Kula M-R. Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration. Biotechnol Bioeng. 1981;23:2789-2802.
    • (1981) Biotechnol Bioeng , vol.23 , pp. 2789-2802
    • Wichmann, R.1    Wandrey, C.2    Buckmann, A.F.3    Kula, M.-R.4
  • 24
    • 2942597686 scopus 로고    scopus 로고
    • Incremental and simultaneous identification of reaction kinetics: Methods and comparison
    • Bardow A, Marquardt W. Incremental and simultaneous identification of reaction kinetics: methods and comparison. Chem Eng Sci. 2004;59:2673-2684.
    • (2004) Chem Eng Sci , vol.59 , pp. 2673-2684
    • Bardow, A.1    Marquardt, W.2
  • 25
    • 33745230163 scopus 로고    scopus 로고
    • Incremental identification of kinetic models for homogeneous reaction systems
    • Brendel M, Bonvin D, Marquardt W. Incremental identification of kinetic models for homogeneous reaction systems. Chem Eng Sci. 2006;61:5404-5420.
    • (2006) Chem Eng Sci , vol.61 , pp. 5404-5420
    • Brendel, M.1    Bonvin, D.2    Marquardt, W.3
  • 26
    • 34547954523 scopus 로고    scopus 로고
    • Application of the incremental identification method to the formate oxidation using formate dehydrogenase
    • Michalik C, Schmidt T, Zavrel M, Ansorge-Schumacher M, Spiess A, Marquardt W. Application of the incremental identification method to the formate oxidation using formate dehydrogenase. Chem Eng Sci. 2007;62:5592-5597.
    • (2007) Chem Eng Sci , vol.62 , pp. 5592-5597
    • Michalik, C.1    Schmidt, T.2    Zavrel, M.3    Ansorge-Schumacher, M.4    Spiess, A.5    Marquardt, W.6
  • 27
    • 33947472850 scopus 로고
    • A schematic method of deriving the rate laws for enzyme-catalyzed reactions
    • King EL, Altman C. A schematic method of deriving the rate laws for enzyme-catalyzed reactions. J Phys Chem. 1956;60: 1375-1378.
    • (1956) J Phys Chem , vol.60 , pp. 1375-1378
    • King, E.L.1    Altman, C.2
  • 28
    • 1842840173 scopus 로고    scopus 로고
    • Identification of diffusive transport by means of an incremental approach
    • Bardow A, Marquardt W. Identification of diffusive transport by means of an incremental approach. Comput Chem Eng. 2004; 28:585-595.
    • (2004) Comput Chem Eng , vol.28 , pp. 585-595
    • Bardow, A.1    Marquardt, W.2
  • 29
    • 0001641749 scopus 로고
    • Non-enzymatic interactions of reduced coenzyme I with inorganic phosphate and certain other anions
    • Alivisatos SG, Ungar F, Abraham G. Non-enzymatic interactions of reduced coenzyme I with inorganic phosphate and certain other anions. Nature 1964;203:973-975.
    • (1964) Nature , vol.203 , pp. 973-975
    • Alivisatos, S.G.1    Ungar, F.2    Abraham, G.3
  • 30
    • 0345817539 scopus 로고
    • Regeneration of nicotinamide cofactors for use in organic synthesis
    • Chenault HK, Whitesides GM. Regeneration of nicotinamide cofactors for use in organic synthesis. Appl Biochem Biotechnol. 1987;14:147-197.
    • (1987) Appl Biochem Biotechnol , vol.14 , pp. 147-197
    • Chenault, H.K.1    Whitesides, G.M.2
  • 31
    • 0003744057 scopus 로고
    • Cambridge University Press: Cambridge
    • Roberts D. Enzyme Kinetics. Cambridge University Press: Cambridge; 1977:177.
    • (1977) Enzyme Kinetics , pp. 177
    • Roberts, D.1
  • 32
    • 84955346459 scopus 로고    scopus 로고
    • Reaction engineering for enzyme-catalyzed biotransformations
    • In: Drauz K, Waldmann H, editors., Wiley-VCH: Weinheim
    • Biselli M, Kragl U, Wandrey C. Reaction engineering for enzyme-catalyzed biotransformations. In: Drauz K, Waldmann H, editors. Enzyme Catalysis in Organic Synthesis. Wiley-VCH: Weinheim; 2002, pp. 185-252.
    • (2002) Enzyme Catalysis In Organic Synthesis , pp. 185-252
    • Biselli, M.1    Kragl, U.2    Wandrey, C.3
  • 33
    • 0033769472 scopus 로고    scopus 로고
    • Characterization of the NAD{thorn} binding site of Candida boidinii formate dehydrogenase by affinity labelling and site-directed mutagenesis
    • Labrou NE, Rigden DJ, Clonis YD. Characterization of the NAD{thorn} binding site of Candida boidinii formate dehydrogenase by affinity labelling and site-directed mutagenesis. Eur J Biochem. 2000;267:6657-6664.
    • (2000) Eur J Biochem , vol.267 , pp. 6657-6664
    • Labrou, N.E.1    Rigden, D.J.2    Clonis, Y.D.3
  • 34
    • 0034011107 scopus 로고    scopus 로고
    • Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues
    • Slusarczyk H, Felber S, Kula MR, Pohl M. Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues. Eur J Biochem. 2000;267:1280-1289.
    • (2000) Eur J Biochem , vol.267 , pp. 1280-1289
    • Slusarczyk, H.1    Felber, S.2    Kula, M.R.3    Pohl, M.4
  • 35
    • 10144250281 scopus 로고    scopus 로고
    • Enzyme engineering aspects of biocatalysis: Cofactor regeneration as example
    • Kragl U, Kruse W, Hummel W, Wandrey C. Enzyme engineering aspects of biocatalysis: Cofactor regeneration as example. Biotechnol Bioeng. 1996;52:309-319.
    • (1996) Biotechnol Bioeng , vol.52 , pp. 309-319
    • Kragl, U.1    Kruse, W.2    Hummel, W.3    Wandrey, C.4
  • 36
    • 0015547509 scopus 로고
    • Mikrobielle Verwertung von Methanol
    • Sahm H, Wagner F. Mikrobielle Verwertung von Methanol. Arch MicrobioI. 1973;90:263-268.
    • (1973) Arch Microbioi , vol.90 , pp. 263-268
    • Sahm, H.1    Wagner, F.2


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