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  • parameter estimation  (1)
  • solid substrate suspension  (1)
  • 1
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 56 (1997), S. 433-440 
    ISSN: 0006-3592
    Schlagwort(e): simple dissolution-reaction model ; enzymatic conversion ; solid substrate suspension ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Although reactions in substrate suspension are employed in industry for several bioconversion processes, there appears to be no quantitative model available in the literature to rationalize the optimization of these processes. We present a simple model that incorporates the kinetics of substrate dissolution and a simultaneous enzymatic reaction. The model was tested in the α-chymotrypsin-catalyzed hydrolysis of an aqueous suspension of dimethyl benzylmethylmalonate to a homogeneous solution of enantiomerically pure monoester. This reaction occurs in the bulk phase, so catalysis by enzyme absorbed at the solid-liquid interface plays no role. The value of the parameters in the model (i.e., the mass transfer coefficient of substrate dissolution (kL), the substrate solubility, and the rate constant for the enzymatic reaction) were determined in separate experiments. Using these parameter values, the model gave a good quantitative prediction of the rate of the overall dissolution-reaction process. When the particle size distribution is known, kL may also be calculated instead. The model seems to be applicable also for other poorly soluble substrates, other enzymes, and other solvents. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 56: 433-440, 1997.
    Zusätzliches Material: 7 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 52 (1996), S. 433-437 
    ISSN: 0006-3592
    Schlagwort(e): parameter estimation ; enzyme kinetics ; identifiability ; Haldanes ; rate constants ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: For an enzymatic reaction the rate constants in the assumed mechanism (k1, k-1, etc.) sometimes can be calculated from the steady-state parameter values (Vmax, Km, etc.) and sometimes cannot. When identifiability problems occur, these are obscured by redundancy occurring among the steady-state parameters. This redundancy is only partly revealed by the known Haldane relations. We found the additional constraints between the parameters. These relations allow to predict in which situation rate constants are identifiable by steady-state kinetic methods. © 1996 John Wiley & Sons, Inc.
    Zusätzliches Material: 2 Tab.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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