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Volumn 62, Issue 9, 2007, Pages 2375-2385

Non-isothermal lipase-catalyzed kinetic resolution in a packed bed reactor: Modeling, simulation and miniplant studies

Author keywords

Enzyme; Kinetic resolution; Mathematical modeling; Non isothermal; Packed bed; Simulation

Indexed keywords

COMPUTER SIMULATION; ENANTIOMERS; ENERGY BALANCE; ENZYMES; MATHEMATICAL MODELS; REACTION KINETICS;

EID: 33947630731     PISSN: 00092509     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ces.2007.01.006     Document Type: Article
Times cited : (16)

References (52)
  • 2
    • 33748750608 scopus 로고    scopus 로고
    • Einsatz und Potenzial der integrierten Miniplant-Technologie für die Enzymkatalyse
    • Berendsen W.R., and Samorski M. Einsatz und Potenzial der integrierten Miniplant-Technologie für die Enzymkatalyse. Chemie Ingenieur Technik 78 (2006) 1013-1021
    • (2006) Chemie Ingenieur Technik , vol.78 , pp. 1013-1021
    • Berendsen, W.R.1    Samorski, M.2
  • 3
    • 33845270128 scopus 로고    scopus 로고
    • A kinetic study of lipase-catalyzed reversible kinetic resolution involving verification at miniplant-scale
    • Berendsen W.R., Gendrot G., Freund A., and Reuss M. A kinetic study of lipase-catalyzed reversible kinetic resolution involving verification at miniplant-scale. Biotechnology and Bioengineering 95 5 (2006) 883-892
    • (2006) Biotechnology and Bioengineering , vol.95 , Issue.5 , pp. 883-892
    • Berendsen, W.R.1    Gendrot, G.2    Freund, A.3    Reuss, M.4
  • 4
    • 29844443252 scopus 로고    scopus 로고
    • Kinetic modeling of lipase catalyzed hydrolysis of (R / S)-1-methoxy-2-propyl-acetate as a model reaction for production of chiral secondary alcohols
    • Berendsen W.R., Gendrot G., Resnick S., and Reuss M. Kinetic modeling of lipase catalyzed hydrolysis of (R / S)-1-methoxy-2-propyl-acetate as a model reaction for production of chiral secondary alcohols. Journal of Biotechnology 121 (2006) 213-226
    • (2006) Journal of Biotechnology , vol.121 , pp. 213-226
    • Berendsen, W.R.1    Gendrot, G.2    Resnick, S.3    Reuss, M.4
  • 5
    • 33750011195 scopus 로고    scopus 로고
    • Investigations of reaction kinetics for immobilized enzymes-Identification of parameters in the presence of diffusion limitation
    • Berendsen W.R., Lapin A., and Reuss M. Investigations of reaction kinetics for immobilized enzymes-Identification of parameters in the presence of diffusion limitation. Biotechnology Progress 22 (2006) 1305-1312
    • (2006) Biotechnology Progress , vol.22 , pp. 1305-1312
    • Berendsen, W.R.1    Lapin, A.2    Reuss, M.3
  • 6
    • 0034233418 scopus 로고    scopus 로고
    • Enzymatic synthesis of alpha-butylglucoside linoleate in a packed bed reactor for future pilot scale-up
    • Bousquet M.P., Willemot R.M., Monsan P., and Boures E. Enzymatic synthesis of alpha-butylglucoside linoleate in a packed bed reactor for future pilot scale-up. Biotechnology Progress 16 (2000) 589-594
    • (2000) Biotechnology Progress , vol.16 , pp. 589-594
    • Bousquet, M.P.1    Willemot, R.M.2    Monsan, P.3    Boures, E.4
  • 7
    • 0037447614 scopus 로고    scopus 로고
    • Prediction of the fixed-bed reactor behaviour using dispersion and plug-flow models with different kinetics for immobilized enzyme
    • Carrara C.R., Mamarella E.J., and Rubiolo A.C. Prediction of the fixed-bed reactor behaviour using dispersion and plug-flow models with different kinetics for immobilized enzyme. Chemical Engineering Journal 92 (2003) 123-129
    • (2003) Chemical Engineering Journal , vol.92 , pp. 123-129
    • Carrara, C.R.1    Mamarella, E.J.2    Rubiolo, A.C.3
  • 8
    • 33845282987 scopus 로고
    • Quantitative analysis of biochemical kinetic resolution of enantiomers. 2. Enzyme-catalyzed esterifications in water-organic biphasic systems
    • Chen C.-S., Wu S.-H., Girdaukas G., and Sih G.J. Quantitative analysis of biochemical kinetic resolution of enantiomers. 2. Enzyme-catalyzed esterifications in water-organic biphasic systems. Journal of American Chemical Society 109 (1987) 2812-2817
    • (1987) Journal of American Chemical Society , vol.109 , pp. 2812-2817
    • Chen, C.-S.1    Wu, S.-H.2    Girdaukas, G.3    Sih, G.J.4
  • 9
    • 0010479905 scopus 로고
    • Modelling of a fixed bed and a fluidized bed immobilized enzyme reactor
    • Ching C.B., and Chu K.H. Modelling of a fixed bed and a fluidized bed immobilized enzyme reactor. Applied Microbiology and Biotechnology 29 (1988) 316-322
    • (1988) Applied Microbiology and Biotechnology , vol.29 , pp. 316-322
    • Ching, C.B.1    Chu, K.H.2
  • 11
    • 33947636431 scopus 로고    scopus 로고
    • Eigtved, P., 1992. Immobilization of lipase by adsorption on a particulate macroporous resin. US patent 5.156.963.
  • 12
    • 7944226615 scopus 로고    scopus 로고
    • Optimization of operating temperature for an continuous immobilized glucose isomerase reactor with pseudo linear kinetics
    • Faqir N.M. Optimization of operating temperature for an continuous immobilized glucose isomerase reactor with pseudo linear kinetics. Engineering in Life Science 4 (2004) 450-459
    • (2004) Engineering in Life Science , vol.4 , pp. 450-459
    • Faqir, N.M.1
  • 13
    • 0037137910 scopus 로고    scopus 로고
    • Optimal temperature policy for immobilized enzyme packed bed reactor performing reversible Michaelis-Menten kinetics using the disjoint policy
    • Faqir N.M., and Attarakih M.M. Optimal temperature policy for immobilized enzyme packed bed reactor performing reversible Michaelis-Menten kinetics using the disjoint policy. Biotechnology and Bioengineering 77 (2002) 163-173
    • (2002) Biotechnology and Bioengineering , vol.77 , pp. 163-173
    • Faqir, N.M.1    Attarakih, M.M.2
  • 15
    • 0024673651 scopus 로고
    • An approach in mathematical modeling of an upflow packed-bed reactor for enzymatic hydrolysis of wheat straw
    • González G., Caminal G., de Mas C., and Lopez-Santin J. An approach in mathematical modeling of an upflow packed-bed reactor for enzymatic hydrolysis of wheat straw. Biotechnology and Bioengineering 34 (1989) 242-251
    • (1989) Biotechnology and Bioengineering , vol.34 , pp. 242-251
    • González, G.1    Caminal, G.2    de Mas, C.3    Lopez-Santin, J.4
  • 18
    • 33947684663 scopus 로고    scopus 로고
    • Process intensification through the combined use of process simulation and miniplant technology
    • Heimann F. Process intensification through the combined use of process simulation and miniplant technology. Computer Aided Chemical Engineering 14 (2003) 155-160
    • (2003) Computer Aided Chemical Engineering , vol.14 , pp. 155-160
    • Heimann, F.1
  • 19
    • 24444444497 scopus 로고
    • Wandgekühlte chemische Festbettreaktoren und deren Modellierung mit Ein- und Zweiphasenmodellen
    • Hein S., and Vortmeyer D. Wandgekühlte chemische Festbettreaktoren und deren Modellierung mit Ein- und Zweiphasenmodellen. Zeitschrift für Naturforschung 50a (1995) 568-576
    • (1995) Zeitschrift für Naturforschung , vol.50 a , pp. 568-576
    • Hein, S.1    Vortmeyer, D.2
  • 20
    • 33845555534 scopus 로고
    • Heats of formation of the ionic and neutral enols of acetaldehyde and acetone
    • Holmes J.L., and Lossing F.P. Heats of formation of the ionic and neutral enols of acetaldehyde and acetone. Journal of American Chemical Society 104 (1982) 2648-2652
    • (1982) Journal of American Chemical Society , vol.104 , pp. 2648-2652
    • Holmes, J.L.1    Lossing, F.P.2
  • 21
    • 0024621304 scopus 로고
    • General theory of determining intraparticle active immobilized enzyme distribution and rate parameters
    • Hossain Md.M., and Do D.D. General theory of determining intraparticle active immobilized enzyme distribution and rate parameters. Biotechnology and Bioengineering 33 (1989) 963-975
    • (1989) Biotechnology and Bioengineering , vol.33 , pp. 963-975
    • Hossain, Md.M.1    Do, D.D.2
  • 22
    • 0022751802 scopus 로고
    • Immobilization of enzymes in porous solids under restricted diffusion conditions
    • Hossain Md.M., Do D.D., and Bailey J.E. Immobilization of enzymes in porous solids under restricted diffusion conditions. A.I.Ch.E. Journal 32 (1986) 1088-1098
    • (1986) A.I.Ch.E. Journal , vol.32 , pp. 1088-1098
    • Hossain, Md.M.1    Do, D.D.2    Bailey, J.E.3
  • 23
    • 10244224050 scopus 로고    scopus 로고
    • Stereoselective bioconversions in continuously operated fixed bed reactors: modeling and process optimization
    • Indlekofer M., Brotz F., Bauer A., and Reuss M. Stereoselective bioconversions in continuously operated fixed bed reactors: modeling and process optimization. Biotechnology and Bioengineering 52 4 (1996) 459-471
    • (1996) Biotechnology and Bioengineering , vol.52 , Issue.4 , pp. 459-471
    • Indlekofer, M.1    Brotz, F.2    Bauer, A.3    Reuss, M.4
  • 24
    • 0000272271 scopus 로고
    • Kinetic analysis and simulation studies for lipase-catalysed resolution of racemic 2-methyl-1-pentanol
    • Indlekofer M., Reuss M., Barth S., and Effenberger F. Kinetic analysis and simulation studies for lipase-catalysed resolution of racemic 2-methyl-1-pentanol. Biocatalysis 7 (1993) 249-266
    • (1993) Biocatalysis , vol.7 , pp. 249-266
    • Indlekofer, M.1    Reuss, M.2    Barth, S.3    Effenberger, F.4
  • 25
    • 0026932087 scopus 로고
    • Determination of process parameters and modelling of lipase-catalyzed transesterification in a fixed bed reactor
    • Jung H.J., and Bauer W. Determination of process parameters and modelling of lipase-catalyzed transesterification in a fixed bed reactor. Chemical Engineering Science 15 (1992) 341-348
    • (1992) Chemical Engineering Science , vol.15 , pp. 341-348
    • Jung, H.J.1    Bauer, W.2
  • 26
    • 84978734472 scopus 로고    scopus 로고
    • Kazlauskas, R.J., Bornscheuer, U.T., 1998. Biotransformations with Lipases. In: Rehm, H.J., Reed, G., Pühler, A., Stadler, P.J.W., Kelly, D.R. (Eds.), Biotechnology, Biotransformations I, second ed., vol. 8a, VCH, Weinheim, pp. 37-191.
  • 27
    • 84988091849 scopus 로고
    • Optimization of operating temperature for continuous glucose isomerase reactor system
    • Kim C., Kim H.S., and Ryu D.D.Y. Optimization of operating temperature for continuous glucose isomerase reactor system. Biotechnology and Bioengineering 24 (1982) 1889-1896
    • (1982) Biotechnology and Bioengineering , vol.24 , pp. 1889-1896
    • Kim, C.1    Kim, H.S.2    Ryu, D.D.Y.3
  • 28
    • 84985687360 scopus 로고
    • Backmixing and mass-transfer in the design of immobilized enzyme reactors
    • Kobayashi T., and Moo-Young M. Backmixing and mass-transfer in the design of immobilized enzyme reactors. Biotechnology and Bioengineering 13 (1971) 893-910
    • (1971) Biotechnology and Bioengineering , vol.13 , pp. 893-910
    • Kobayashi, T.1    Moo-Young, M.2
  • 29
    • 33947639834 scopus 로고    scopus 로고
    • Koning, G.W., 2002. Heat and mass transport in tubular packed bed reactors at reacting and non-reacting conditions. Ph.D. Thesis, University of Twente, Twente University Press, ISBN 903651813x.
  • 30
    • 3543021486 scopus 로고    scopus 로고
    • Dynamic behavior of microbial populations in stirred bioreactors simulated with Euler-Lagrange methods-traveling along the lifelines of single cells
    • Lapin A., Müller D., and Reuss M. Dynamic behavior of microbial populations in stirred bioreactors simulated with Euler-Lagrange methods-traveling along the lifelines of single cells. Industrial and Engineering Chemistry Research 43 (2004) 4647-4656
    • (2004) Industrial and Engineering Chemistry Research , vol.43 , pp. 4647-4656
    • Lapin, A.1    Müller, D.2    Reuss, M.3
  • 31
    • 33646816768 scopus 로고    scopus 로고
    • Modeling the dynamics of E. coli populations in the three-dimensional turbulent field of a stirred-tank bioreactor-A structured-segregated approach
    • Lapin A., Schmid J., and Reuss M. Modeling the dynamics of E. coli populations in the three-dimensional turbulent field of a stirred-tank bioreactor-A structured-segregated approach. Chemical Engineering Science 61 (2006) 4783-4797
    • (2006) Chemical Engineering Science , vol.61 , pp. 4783-4797
    • Lapin, A.1    Schmid, J.2    Reuss, M.3
  • 32
    • 0041110840 scopus 로고    scopus 로고
    • Thermokinetic models of enzyme-catalyzed reactions in batch and plug-flow reactors
    • Liang Y., Wu Y., Dinghuo L., Wang C., Liu Y., Songsheng Q., and Zou G. Thermokinetic models of enzyme-catalyzed reactions in batch and plug-flow reactors. Thermochimica Acta 307 (1997) 149-153
    • (1997) Thermochimica Acta , vol.307 , pp. 149-153
    • Liang, Y.1    Wu, Y.2    Dinghuo, L.3    Wang, C.4    Liu, Y.5    Songsheng, Q.6    Zou, G.7
  • 33
    • 0015452464 scopus 로고
    • Nonisothermal immobilized enzyme reaction in a packed bed reactor
    • Lin S.H. Nonisothermal immobilized enzyme reaction in a packed bed reactor. Biophysik 8 (1972) 302-309
    • (1972) Biophysik , vol.8 , pp. 302-309
    • Lin, S.H.1
  • 34
    • 0025923930 scopus 로고
    • Optimal feed temperature for an immobilized enzyme packed-bed reactor
    • Lin S.H. Optimal feed temperature for an immobilized enzyme packed-bed reactor. Journal of Chemical Technology and Biotechnology 50 (1991) 17-26
    • (1991) Journal of Chemical Technology and Biotechnology , vol.50 , pp. 17-26
    • Lin, S.H.1
  • 35
    • 0028452839 scopus 로고
    • Evaluation of the performance of immobilized enzyme reactors with Michaelis-Menten kinetics
    • Lortie R. Evaluation of the performance of immobilized enzyme reactors with Michaelis-Menten kinetics. Journal of Chemical Technology and Biotechnology 60 (1994) 189-193
    • (1994) Journal of Chemical Technology and Biotechnology , vol.60 , pp. 189-193
    • Lortie, R.1
  • 36
    • 0022766595 scopus 로고
    • Heterogeneous one-dimensional model for fixed bed enzyme reactors
    • Lortie R., and Thomas D. Heterogeneous one-dimensional model for fixed bed enzyme reactors. Biotechnology and Bioengineering 28 (1986) 1256-1260
    • (1986) Biotechnology and Bioengineering , vol.28 , pp. 1256-1260
    • Lortie, R.1    Thomas, D.2
  • 37
    • 0016560111 scopus 로고
    • Enzyme immobilized in a packed-bed reactor: kinetic parameters and mass transfer effects
    • Marrazzo W.N., Merson R.L., and McCoy B.J. Enzyme immobilized in a packed-bed reactor: kinetic parameters and mass transfer effects. Biotechnology and Bioengineering 17 (1975) 1515-1528
    • (1975) Biotechnology and Bioengineering , vol.17 , pp. 1515-1528
    • Marrazzo, W.N.1    Merson, R.L.2    McCoy, B.J.3
  • 38
    • 84985653024 scopus 로고
    • A heat transfer study on packed bed reactors of immobilized glucoamylase
    • Marsh D.R., and Tsao G.T. A heat transfer study on packed bed reactors of immobilized glucoamylase. Biotechnology and Bioengineering 18 (1976) 349-362
    • (1976) Biotechnology and Bioengineering , vol.18 , pp. 349-362
    • Marsh, D.R.1    Tsao, G.T.2
  • 39
    • 0017209816 scopus 로고
    • A theoretical and computational study of the heat effects on packed-bed reactors of immobilized enzymes
    • Marsh D.R., and Tsao G.T. A theoretical and computational study of the heat effects on packed-bed reactors of immobilized enzymes. Journal of Solid-Phase Biochemistry 1 (1976) 67-79
    • (1976) Journal of Solid-Phase Biochemistry , vol.1 , pp. 67-79
    • Marsh, D.R.1    Tsao, G.T.2
  • 40
    • 0037687640 scopus 로고    scopus 로고
    • Imaging the distribution and secondary structure of immobilized enzymes using infrared microspectroscopy
    • Mei Y., Miller L., Gao W., and Gross R.A. Imaging the distribution and secondary structure of immobilized enzymes using infrared microspectroscopy. Biomacromolecules 4 (2003) 70-74
    • (2003) Biomacromolecules , vol.4 , pp. 70-74
    • Mei, Y.1    Miller, L.2    Gao, W.3    Gross, R.A.4
  • 41
    • 0024962543 scopus 로고
    • Urea hydrolysis by immobilized urease in a fixed bed reactor: analysis and kinetic parameter estimation
    • Moynihan H.J., Lee C.K., Clark W., and Wang N.H.L. Urea hydrolysis by immobilized urease in a fixed bed reactor: analysis and kinetic parameter estimation. Biotechnology and Bioengineering 34 (1989) 951-963
    • (1989) Biotechnology and Bioengineering , vol.34 , pp. 951-963
    • Moynihan, H.J.1    Lee, C.K.2    Clark, W.3    Wang, N.H.L.4
  • 43
    • 0020115913 scopus 로고
    • Film diffusional influences on the kinetic parameters in packed-bed immobilized enzyme reactors
    • Patwardhan V.S., and Karanth N.G. Film diffusional influences on the kinetic parameters in packed-bed immobilized enzyme reactors. Biotechnology and Bioengineering 24 (1982) 763-780
    • (1982) Biotechnology and Bioengineering , vol.24 , pp. 763-780
    • Patwardhan, V.S.1    Karanth, N.G.2
  • 44
    • 33947627948 scopus 로고    scopus 로고
    • Resnick, S.M., Donate, F.A., Frank, T.C., Foley, P., 2003. Enzymatic resolution of propylene glycol alkyl (or aryl) ethers and ether acetates. World patent, WO 03/083126 A2.
  • 45
    • 33947612875 scopus 로고    scopus 로고
    • Rotticci, D., 2000. Understanding and engineering the enantioselectivity of Candida antarctica lipase B towards sec-Alcohols. Ph.D. Thesis, Stockholm, ISSN 110-7974.
  • 46
    • 0026832998 scopus 로고
    • Determination of total and active immobilized enzyme distribution in porous solid supports
    • Scharer R., Hossain Md.M., and Do D.D. Determination of total and active immobilized enzyme distribution in porous solid supports. Biotechnology and Bioengineering 39 (1992) 679-687
    • (1992) Biotechnology and Bioengineering , vol.39 , pp. 679-687
    • Scharer, R.1    Hossain, Md.M.2    Do, D.D.3
  • 47
    • 33947638784 scopus 로고    scopus 로고
    • Stadler, H.-G., 2005. Entwicklung eines kontinuierlichen Verfahrens zur enzymkatalysierten Synthese eines strukturierten Triglycerides. Ph.D. Thesis, University of Stuttgart.
  • 48
    • 0002118048 scopus 로고
    • Keto-enol equilibrium constants
    • Rappaport Z. (Ed), Wiley, New York
    • Toullec J. Keto-enol equilibrium constants. In: Rappaport Z. (Ed). The Chemistry of Enols (1990), Wiley, New York 323-398
    • (1990) The Chemistry of Enols , pp. 323-398
    • Toullec, J.1
  • 50
    • 33947619326 scopus 로고    scopus 로고
    • Tsotsas, E., 2002. Wärmeleitung und Dispersion in durchströmten Schüttungen. In: VDI-Wärmeatlas, ninth ed., Chapter. Mh1-14. Springer, Berlin.
  • 51
    • 0034237660 scopus 로고    scopus 로고
    • At what temperature can enzymes maintain their catalytic activity?
    • Turner N.A., and Vulfson E.N. At what temperature can enzymes maintain their catalytic activity?. Enzyme Microbial Technology 27 (2000) 108-113
    • (2000) Enzyme Microbial Technology , vol.27 , pp. 108-113
    • Turner, N.A.1    Vulfson, E.N.2
  • 52
    • 0035811851 scopus 로고    scopus 로고
    • Mass-transfer limitations for immobilized enzyme-catalyzed kinetic resolution of racemate in a fixed bed reactor
    • Xiu G.-H., Jiang L., and Li P. Mass-transfer limitations for immobilized enzyme-catalyzed kinetic resolution of racemate in a fixed bed reactor. Biotechnology and Bioengineering 74 1 (2001) 31-39
    • (2001) Biotechnology and Bioengineering , vol.74 , Issue.1 , pp. 31-39
    • Xiu, G.-H.1    Jiang, L.2    Li, P.3


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