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Volumn 80, Issue , 2012, Pages 435-450

Model-based characterization of operational stability of multimeric enzymes with complex deactivation behavior: An in-silico investigation

Author keywords

Biocatalysis; Biocatalyst operational stability; Catalyst deactivation; Model based experimental analysis; Parameter identification; T ramping

Indexed keywords

BIOCATALYSIS; BIOTRANSFORMATION PROCESS; CHARACTERIZATION METHODS; CONTINUOUS REACTOR OPERATION; CONTINUOUS REACTORS; DEACTIVATION MECHANISM; DEGRADATION PATHWAYS; DESIGN TASKS; DIMERIC ENZYME; DIMERIC MODELS; ERROR DATA; EXPERIMENTAL PROCEDURE; IN-SILICO; INPUT DATAS; LACK-OF-FIT; MECHANISTIC MODELS; MODEL-BASED EXPERIMENTAL ANALYSIS; MODELING STUDIES; MULTIMERIC ENZYMES; OPERATIONAL STABILITY; PARAMETERIZATIONS; PROCESS CONDITION; PROCESS PREDICTION; PROGRESS CURVES; SUBUNIT DISSOCIATION; T-RAMPING; VIRTUAL PROCESS;

EID: 84864058997     PISSN: 00092509     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ces.2012.05.030     Document Type: Article
Times cited : (10)

References (61)
  • 1
    • 0023709866 scopus 로고
    • Analysis of processes causing thermal inactivation of enzymes
    • Ahern T.J., Klibanov A.M. Analysis of processes causing thermal inactivation of enzymes. Methods Biochem. Anal. 1988, 33:91-127.
    • (1988) Methods Biochem. Anal. , vol.33 , pp. 91-127
    • Ahern, T.J.1    Klibanov, A.M.2
  • 2
    • 0035843136 scopus 로고    scopus 로고
    • Combinatorial and computational challenges for biocatalyst design
    • Arnold F.H. Combinatorial and computational challenges for biocatalyst design. Nature 2001, 409:253-257.
    • (2001) Nature , vol.409 , pp. 253-257
    • Arnold, F.H.1
  • 3
    • 35649020855 scopus 로고    scopus 로고
    • Development of an amino acid racemase from Pseudomonas putida DSM 3263 and model-based characterization for application in medium-constrained continuous processes
    • Bechtold M., Makart S., Reiss R., Alder P., Panke S. Development of an amino acid racemase from Pseudomonas putida DSM 3263 and model-based characterization for application in medium-constrained continuous processes. Biotechnol. Bioeng. 2007, 98:812-824.
    • (2007) Biotechnol. Bioeng. , vol.98 , pp. 812-824
    • Bechtold, M.1    Makart, S.2    Reiss, R.3    Alder, P.4    Panke, S.5
  • 4
    • 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., Reuss M. Investigations of reaction kinetics for immobilized enzymes-Identification of parameters in the presence of diffusion limitation. Biotechnol. Prog. 2006, 22:1305-1312.
    • (2006) Biotechnol. Prog. , vol.22 , pp. 1305-1312
    • Berendsen, W.R.1    Lapin, A.2    Reuss, M.3
  • 5
    • 33947630731 scopus 로고    scopus 로고
    • Non-isothermal lipase-catalyzed kinetic resolution in a packed bed reactor: modeling, simulation and miniplant studies
    • Berendsen W.R., Lapin A., Reuss M. Non-isothermal lipase-catalyzed kinetic resolution in a packed bed reactor: modeling, simulation and miniplant studies. Chem. Eng. Sci. 2007, 62:2375-2385.
    • (2007) Chem. Eng. Sci. , vol.62 , pp. 2375-2385
    • Berendsen, W.R.1    Lapin, A.2    Reuss, M.3
  • 6
    • 4143143467 scopus 로고    scopus 로고
    • Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface
    • Bjork A., Dalhus B., Mantzilas D., Sirevag R., Eijsink V.G.H. Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface. J. Mol. Biol. 2004, 341:1215-1226.
    • (2004) J. Mol. Biol. , vol.341 , pp. 1215-1226
    • Bjork, A.1    Dalhus, B.2    Mantzilas, D.3    Sirevag, R.4    Eijsink, V.G.H.5
  • 7
    • 28244497820 scopus 로고    scopus 로고
    • Established and novel tools to investigate biocatalyst stability
    • Bommarius A., Broering J. Established and novel tools to investigate biocatalyst stability. Biocatal. Biotransform. 2005, 23:125-139.
    • (2005) Biocatal. Biotransform. , vol.23 , pp. 125-139
    • Bommarius, A.1    Broering, J.2
  • 8
    • 0035210891 scopus 로고    scopus 로고
    • New method for rapid determination of biocatalyst process stability
    • Boy M., Bohm D., Voss H. New method for rapid determination of biocatalyst process stability. Biocatal. Biotransform. 2001, 19:413-425.
    • (2001) Biocatal. Biotransform. , vol.19 , pp. 413-425
    • Boy, M.1    Bohm, D.2    Voss, H.3
  • 9
    • 0032118139 scopus 로고    scopus 로고
    • A method for fast determination of biocatalyst process stability
    • Boy M., Dominik A., Voss H. A method for fast determination of biocatalyst process stability. Chem. Eng. Technol. 1998, 21:570-575.
    • (1998) Chem. Eng. Technol. , vol.21 , pp. 570-575
    • Boy, M.1    Dominik, A.2    Voss, H.3
  • 10
    • 0032828583 scopus 로고    scopus 로고
    • Fast determination of biocatalyst process stability
    • Boy M., Dominik A., Voss H. Fast determination of biocatalyst process stability. Process Biochem. 1999, 34:535-547.
    • (1999) Process Biochem. , vol.34 , pp. 535-547
    • Boy, M.1    Dominik, A.2    Voss, H.3
  • 11
    • 79954593169 scopus 로고    scopus 로고
    • Biocatalytic process optimization based on mechanistic modeling of cholic acid oxidation with cofactor regeneration
    • Braun M., Link H., Liu L., Schmid R.D., Weuster-Botz D. Biocatalytic process optimization based on mechanistic modeling of cholic acid oxidation with cofactor regeneration. Biotechnol. Bioeng. 2011, 108:1307-1317.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 1307-1317
    • Braun, M.1    Link, H.2    Liu, L.3    Schmid, R.D.4    Weuster-Botz, D.5
  • 12
    • 33745751462 scopus 로고    scopus 로고
    • Analysis of two-liquid-phase multistep biooxidation based on a process model: indications for biological energy shortage
    • Buhler B., Straathof A.J.J., Witholt B., Schmid A. Analysis of two-liquid-phase multistep biooxidation based on a process model: indications for biological energy shortage. Org. Proc. Res. Dev. 2006, 10:628-643.
    • (2006) Org. Proc. Res. Dev. , vol.10 , pp. 628-643
    • Buhler, B.1    Straathof, A.J.J.2    Witholt, B.3    Schmid, A.4
  • 13
    • 34248174364 scopus 로고    scopus 로고
    • Modelling and optimisation of a transketolase-mediated carbon-carbon bond formation reaction
    • Chen B.H., Baganz F., Woodley J.M. Modelling and optimisation of a transketolase-mediated carbon-carbon bond formation reaction. Chem. Eng. Sci. 2007, 62:3178-3184.
    • (2007) Chem. Eng. Sci. , vol.62 , pp. 3178-3184
    • Chen, B.H.1    Baganz, F.2    Woodley, J.M.3
  • 16
    • 0035312394 scopus 로고    scopus 로고
    • The temperature optima of enzymes: a new perspective on an old phenomenon
    • Daniel R.M., Danson M.J., Eisenthal R. The temperature optima of enzymes: a new perspective on an old phenomenon. Trends Biochem. Sci. 2001, 26:223-225.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 223-225
    • Daniel, R.M.1    Danson, M.J.2    Eisenthal, R.3
  • 19
    • 33745664260 scopus 로고    scopus 로고
    • The thermal behaviour of enzyme activity: implications for biotechnology
    • Eisenthal R., Peterson M.E., Daniel R.M., Danson M.J. The thermal behaviour of enzyme activity: implications for biotechnology. Trends Biotechnol. 2006, 24:289-292.
    • (2006) Trends Biotechnol. , vol.24 , pp. 289-292
    • Eisenthal, R.1    Peterson, M.E.2    Daniel, R.M.3    Danson, M.J.4
  • 20
    • 70349782241 scopus 로고    scopus 로고
    • Stabilization of multimeric enzymes: strategies to prevent subunit dissociation
    • Fernandez-Lafuente R. Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb. Technol. 2009, 45:405-418.
    • (2009) Enzyme Microb. Technol. , vol.45 , pp. 405-418
    • Fernandez-Lafuente, R.1
  • 21
    • 0037199132 scopus 로고    scopus 로고
    • Full model for reversible kinetics of lipase-catalyzed sugar-ester synthesis in 2-methyl 2-butanol
    • Flores M.V., Halling P.J. Full model for reversible kinetics of lipase-catalyzed sugar-ester synthesis in 2-methyl 2-butanol. Biotechnol. Bioeng. 2002, 78:794-800.
    • (2002) Biotechnol. Bioeng. , vol.78 , pp. 794-800
    • Flores, M.V.1    Halling, P.J.2
  • 22
    • 77957357262 scopus 로고    scopus 로고
    • A model-based systems approach to pharmaceutical product-process design and analysis
    • Gernaey K.V., Gani R. A model-based systems approach to pharmaceutical product-process design and analysis. Chem. Eng. Sci. 2010, 65:5757-5769.
    • (2010) Chem. Eng. Sci. , vol.65 , pp. 5757-5769
    • Gernaey, K.V.1    Gani, R.2
  • 23
    • 77953913430 scopus 로고    scopus 로고
    • Application of mechanistic models to fermentation and biocatalysis for next-generation processes
    • Gernaey K.V., Lantz A.E., Tufvesson P., Woodley J.M., Sin G. Application of mechanistic models to fermentation and biocatalysis for next-generation processes. Trends Biotechnol 2010, 28:346-354.
    • (2010) Trends Biotechnol , vol.28 , pp. 346-354
    • Gernaey, K.V.1    Lantz, A.E.2    Tufvesson, P.3    Woodley, J.M.4    Sin, G.5
  • 24
    • 20144365371 scopus 로고    scopus 로고
    • Accelerated biocatalyst stability testing for process optimization
    • Gibbs P.R., Uehara C.S., Neunert U., Bommarius A.S. Accelerated biocatalyst stability testing for process optimization. Biotechnol. Prog. 2005, 21:762-774.
    • (2005) Biotechnol. Prog. , vol.21 , pp. 762-774
    • Gibbs, P.R.1    Uehara, C.S.2    Neunert, U.3    Bommarius, A.S.4
  • 27
    • 0037250884 scopus 로고    scopus 로고
    • Enzyme reactor design under thermal inactivation
    • Illanes A., Wilson L. Enzyme reactor design under thermal inactivation. Crit. Rev. Biotechnol. 2003, 23:61-93.
    • (2003) Crit. Rev. Biotechnol. , vol.23 , pp. 61-93
    • Illanes, A.1    Wilson, L.2
  • 29
    • 77954862055 scopus 로고    scopus 로고
    • Bioprocesses: modeling needs for process evaluation and sustainability assessment
    • Jimenez-Gonzalez C., Woodley J.M. Bioprocesses: modeling needs for process evaluation and sustainability assessment. Comp. Chem. Eng. 2010, 34:1009-1017.
    • (2010) Comp. Chem. Eng. , vol.34 , pp. 1009-1017
    • Jimenez-Gonzalez, C.1    Woodley, J.M.2
  • 30
    • 0020999167 scopus 로고
    • Stabilization of enzymes against thermal inactivation
    • Klibanov A.M. Stabilization of enzymes against thermal inactivation. Adv. Appl. Microbiol. 1983, 29:1-28.
    • (1983) Adv. Appl. Microbiol. , vol.29 , pp. 1-28
    • Klibanov, A.M.1
  • 31
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry R., Eyring H. Conformation changes of proteins. J. Phys. Chem. 1954, 58:110-120.
    • (1954) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 33
    • 22744438969 scopus 로고    scopus 로고
    • Model-based experimental analysis of kinetic phenomena in multi-phase reactive systems
    • Marquardt W. Model-based experimental analysis of kinetic phenomena in multi-phase reactive systems. Chem. Eng. Res. Des. 2005, 83:561-573.
    • (2005) Chem. Eng. Res. Des. , vol.83 , pp. 561-573
    • Marquardt, W.1
  • 34
    • 0033778161 scopus 로고    scopus 로고
    • Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange
    • Mayne L., Englander S.W. Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange. Prot. Sci. 2000, 9:1873-1877.
    • (2000) Prot. Sci. , vol.9 , pp. 1873-1877
    • Mayne, L.1    Englander, S.W.2
  • 36
    • 33847757782 scopus 로고    scopus 로고
    • The dependence of enzyme activity on temperature: determination and validation of parameters
    • Peterson M.E., Daniel R.M., Danson M.J., Eisenthal R. The dependence of enzyme activity on temperature: determination and validation of parameters. Biochem. J. 2007, 402:331-337.
    • (2007) Biochem. J. , vol.402 , pp. 331-337
    • Peterson, M.E.1    Daniel, R.M.2    Danson, M.J.3    Eisenthal, R.4
  • 37
    • 2442677663 scopus 로고    scopus 로고
    • A new intrinsic thermal parameter for enzymes reveals true temperature optima
    • Peterson M.E., Eisenthal R., Danson M.J., Spence A., Daniel R.M. A new intrinsic thermal parameter for enzymes reveals true temperature optima. J. Biol. Chem. 2004, 279:20717-20722.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20717-20722
    • Peterson, M.E.1    Eisenthal, R.2    Danson, M.J.3    Spence, A.4    Daniel, R.M.5
  • 41
    • 0035910597 scopus 로고    scopus 로고
    • Combinatorial and evolution-based methods in the creation of enantioselective catalysts
    • Reetz M.T. Combinatorial and evolution-based methods in the creation of enantioselective catalysts. Angew. Chem. Int. Ed. 2001, 40:284-310.
    • (2001) Angew. Chem. Int. Ed. , vol.40 , pp. 284-310
    • Reetz, M.T.1
  • 42
    • 76549099302 scopus 로고    scopus 로고
    • Utilizing simple biochemical measurements to predict lifetime output of biocatalysts in continuous isothermal processes
    • Rogers T.A., Bommarius A.S. Utilizing simple biochemical measurements to predict lifetime output of biocatalysts in continuous isothermal processes. Chem. Eng. Sci. 2010, 65:2118-2124.
    • (2010) Chem. Eng. Sci. , vol.65 , pp. 2118-2124
    • Rogers, T.A.1    Bommarius, A.S.2
  • 43
    • 76549131680 scopus 로고    scopus 로고
    • Deactivation of TEM-1 beta-lactamase investigated by isothermal batch and non-isothermal continuous enzyme membrane reactor methods
    • Rogers T.A., Daniel R.M., Bommarius A.S. Deactivation of TEM-1 beta-lactamase investigated by isothermal batch and non-isothermal continuous enzyme membrane reactor methods. Chemcatchem 2009, 1:131-137.
    • (2009) Chemcatchem , vol.1 , pp. 131-137
    • Rogers, T.A.1    Daniel, R.M.2    Bommarius, A.S.3
  • 44
    • 77951977004 scopus 로고    scopus 로고
    • Protein kinetic stability
    • Sanchez-Ruiz J.M. Protein kinetic stability. Biophys. Chem. 2010, 148:1-15.
    • (2010) Biophys. Chem. , vol.148 , pp. 1-15
    • Sanchez-Ruiz, J.M.1
  • 48
    • 0036401862 scopus 로고    scopus 로고
    • The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space
    • Shortle D. The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space. Unfolded Proteins 2002, 62:1-23.
    • (2002) Unfolded Proteins , vol.62 , pp. 1-23
    • Shortle, D.1
  • 49
    • 62649091844 scopus 로고    scopus 로고
    • Defining the stability of multimeric proteins
    • Shriver J.W., Edmondson S.P. Defining the stability of multimeric proteins. Methods Mol. Biol. 2009, 490:57-82.
    • (2009) Methods Mol. Biol. , vol.490 , pp. 57-82
    • Shriver, J.W.1    Edmondson, S.P.2
  • 50
    • 73249131640 scopus 로고    scopus 로고
    • Application of modeling and simulation tools for the evaluation of biocatalytic processes: a future perspective
    • Sin G., Woodley J.M., Gernaey K.V. Application of modeling and simulation tools for the evaluation of biocatalytic processes: a future perspective. Biotechnol. Prog. 2009, 25:1529-1538.
    • (2009) Biotechnol. Prog. , vol.25 , pp. 1529-1538
    • Sin, G.1    Woodley, J.M.2    Gernaey, K.V.3
  • 51
    • 0038565896 scopus 로고    scopus 로고
    • The detection of kinetic intermediates during the unfolding of lipoxygenase-1 by urea or guanidine hydrochloride
    • Srinivasulu S., Rao A.G.A. The detection of kinetic intermediates during the unfolding of lipoxygenase-1 by urea or guanidine hydrochloride. Biochim. Biophys. Acta-Protein Struct. Mol. Enzym. 1996, 1294:115-120.
    • (1996) Biochim. Biophys. Acta-Protein Struct. Mol. Enzym. , vol.1294 , pp. 115-120
    • Srinivasulu, S.1    Rao, A.G.A.2
  • 52
    • 0035931452 scopus 로고    scopus 로고
    • Development of a computer program for analysis of enzyme kinetics by progress curve fitting
    • Straathof A.J.J. Development of a computer program for analysis of enzyme kinetics by progress curve fitting. J. Mol. Catal. B-Enzymatic 2001, 11:991-998.
    • (2001) J. Mol. Catal. B-Enzymatic , vol.11 , pp. 991-998
    • Straathof, A.J.J.1
  • 55
    • 0001893174 scopus 로고
    • Protein denaturation
    • Academic Press, New York, C.B.J. Anfinsen, J.T. Edsall, F.M. Richards (Eds.)
    • Tanford C. Protein denaturation. Advances in Protein Chemistry 1970, 2-95. Academic Press, New York. C.B.J. Anfinsen, J.T. Edsall, F.M. Richards (Eds.).
    • (1970) Advances in Protein Chemistry , pp. 2-95
    • Tanford, C.1
  • 56
    • 80052616943 scopus 로고    scopus 로고
    • Modelling as a tool of enzyme reaction engineering for enzyme reactor development
    • Vasic-Racki D., Findrik Z., Presecki A.V. Modelling as a tool of enzyme reaction engineering for enzyme reactor development. Appl. Microbiol. Biotechnol. 2011, 91:845-856.
    • (2011) Appl. Microbiol. Biotechnol. , vol.91 , pp. 845-856
    • Vasic-Racki, D.1    Findrik, Z.2    Presecki, A.V.3
  • 57
    • 36048971938 scopus 로고    scopus 로고
    • Innovative technology to meet the demands of the white biotechnology revolution of chemical production
    • Villadsen J. Innovative technology to meet the demands of the white biotechnology revolution of chemical production. Chem. Eng. Sci. 2007, 62:6957-6968.
    • (2007) Chem. Eng. Sci. , vol.62 , pp. 6957-6968
    • Villadsen, J.1
  • 58
    • 0342683812 scopus 로고    scopus 로고
    • Analysis of mechanism and kinetics of thermal inactivation of enzymes: evaluation of multitemperature data applied to inactivation of yeast invertase
    • Vrabel P., Polakovic M., Stefuca V., Bales V. Analysis of mechanism and kinetics of thermal inactivation of enzymes: evaluation of multitemperature data applied to inactivation of yeast invertase. Enzyme Microb. Technol. 1997, 20:348-354.
    • (1997) Enzyme Microb. Technol. , vol.20 , pp. 348-354
    • Vrabel, P.1    Polakovic, M.2    Stefuca, V.3    Bales, V.4
  • 60
    • 0026765152 scopus 로고
    • Enzyme stability in downstream processing.1. enzyme inactivation, stability and stabilization
    • Weijers S.R., Van't Riet K. Enzyme stability in downstream processing.1. enzyme inactivation, stability and stabilization. Biotechnol. Adv. 1992, 10:237-249.
    • (1992) Biotechnol. Adv. , vol.10 , pp. 237-249
    • Weijers, S.R.1    Van't Riet, K.2
  • 61
    • 34548017156 scopus 로고    scopus 로고
    • Modelling the reaction course of N-acetylneuraminic acid synthesis from N-acetyl-d-glucosamine-new strategies for the optimisation of neuraminic acid synthesis
    • Zimmermann V., Hennemann H.G., Daumann T., Kragl U. Modelling the reaction course of N-acetylneuraminic acid synthesis from N-acetyl-d-glucosamine-new strategies for the optimisation of neuraminic acid synthesis. Appl. Microbiol. Biotechnol. 2007, 76:597-605.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 597-605
    • Zimmermann, V.1    Hennemann, H.G.2    Daumann, T.3    Kragl, U.4


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