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  • 1985-1989  (14)
  • 1
    Electronic Resource
    Electronic Resource
    Fundamental studies of glucose oxidase immobilization on controlled pore glass (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 842-851 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilization experiments have been performed with glucose oxidase as enzyme and controlled-pore glass of different pore sizes as support for chemical coupling. The experimental results have been analyzed for comparison with the theoretical model predictions. Analysis of the initial stage of the process gives the fundamental characteristic of the immobilization reaction. These investigations allow us to study the influence of the degree of diffusional restriction on the evolution of the immobilization process and spatial distribution of immobilized enzyme. Nonuniformly distributed concentrations have been achieved within the porous matrix, and suggestions have been made in designing such profiles by choosing appropriate experimental parameters.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270614
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Modeling of enzyme immobilization in porous membranes (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 1126-1135 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This article deals with the mathematical modeling of the process of enzyme immobilization in porous membranes. During the initial period, an analytical solution is available to extract the rate constant for immobilization. Beyond this period, the model equations are solved numerically to yield the transient response of the enzyme concentration in the immobilizing solution and also the evolution of the enzyme loading profile inside the membrane. It is found that the immobilization practically ceases even through the attachment sites are still available within the membrane.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270807
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    A novel method of determination of the internal enzyme distribution within porous solid supports and the deactivation rate constant (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 486-493 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This article presents a method for determining the rate constant for deactivation and the internal distribution of immobilized enzyme. This method makes use of the parallel deactivation process in a diffusion-controlled regime, in which the internal activity profile behaves like a penetration front. This front basically traces through the initial active enzymatic profile, and one can determine the internal profile and the rate constant for deactivation from the experimentally observable bulk concentration versus time. This method is applied to the experimental data of the system of hydrogen-peroxide-immobilized catalase on controlled pore glass and Si-Al particles.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260280404
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    General theory of determining intraparticle active immobilized enzyme distribution and rate parameters (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 963-975 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A general theory is presented in this article for determining the intrinsic rate constants for the main reaction and deactivation reaction, the effective diffusivity of the substrate, and the active enzyme distribution within porous solid supports from deactivation study of a continuous stirred-basket reactor (CSBR). For the parallel deactivation five reaction kinetics are considered: (a) Michaelis-Menten, (b) substrate inhibition, (c) product inhibition (competitive), (d) product inhibition (anticompetitive), and (e) zero-order kinetics. The experimental results of the system of hydrogen-peroxide-immobilized catalase on controlled-pore glass particles are analyzed to demonstrate the application of the theory developed for parallel deactivation of active immobilized enzyme (IME). For series deactivation only first-order kinetics is treated, and a numerical procedure is proposed to deter mine the rate parameters and the internal active enzyme distribution. The experimental data of the system of glucose-immobilized glucose oxidase on silica-alumina and controlled-pore glass particles are used to verify the theory.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260330805
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Determination of km and De from a one-shot experiment of enzyme immobilization (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 883-886 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270619
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    A new method to determine active enzyme distribution, effective diffusivity, rate constant for main reaction and rate constant for deactivation (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 29 (1987), S. 545-551 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A new method is presented to determine (1) the rate constant for the main reaction, (2) the rate constant for deactivation, (3) the effective diffusivity, and (4) the active enzyme distribution within a porous solid support by utilizing data of bulk substrate concentration versus time in a continuous stirred basket reactor. The method relies on an assumption of parallel deactivation mechanism with strong pore diffusional resistance with respect to substrate species. The data of hydrogen peroxide-immobilized catalase published in the literature are used to demonstrate the theory. A parameter determination procedure is also presented.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260290502
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Determination of intrinsic parameters for immobilization reactions of catalase and amyloglucosidase in porous glass supports (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 31 (1988), S. 730-736 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Experiments have been carried out for immobilizing enzyme-catalase and amyloglucosidase in controlled-pore glass particles of two different pore sizes. The experimental results have been analyzed, initial-stage analysis for the rate parameters of immobilization reactions and long-time analysis for determining the evolution of the immobilization process. These investigations suggest that the overall process of immobilization is controlled by the restricted diffusion of enzymes into the pores of the support. As a result, immobilized enzyme (IME) can penetrate only up to a certain distance into the support. The penetration depth of IME for the support-enzyme system mentioned have been evaluated from the experimental bulk enzyme concentration data in a batch recirculation reactor.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260310716
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    Paper (German National Licenses)
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  • 8
    Electronic Resource
    Electronic Resource
    Immobilization of enzymes in porous solids under restricted diffusion conditions (1986)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 32 (1986), S. 1088-1098 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A restricted diffusion model is developed to study the immobilization of enzyme in porous solid supports. Simulation studies have been carried out for various combinations of process variables and parameters of the immobilization system. The model has also been used to develop a method for estimating the intrinsic rate constant of immobilization when enzyme diffusion into the support is restricted. Results of experiments in which glucose oxidase was immobilized in porous glass supports are consistent with model simulations.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690320705
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    Paper (German National Licenses)
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  • 9
    Electronic Resource
    Electronic Resource
    Discrete cell model of fixed-bed adsorbers with rectangular adsorption isotherms (1985)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 31 (1985), S. 1329-1337 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Adsorption of organics inot activated carbon particles within a fixed-bed adsorber is modeled using the concept of mixing cells. The adsorption isotherm of these organics is taken to be rectangular because of the commonly observed strong affinity of organics into activated carbons. The model equations are solved by a singular perturbation method, and this results in a graphical procedure similar to that of McCabe and Thiele used in distillation column design. Such a graphical procedure provides a quick means to determine the adsorbate profiles along the adsorber for a given time and also the breakthrough curve, which reflects the performance of the adsorber.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690310812
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    Paper (German National Licenses)
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  • 10
    Electronic Resource
    Electronic Resource
    A new simplified model for adsorption in a single particle (1987)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 33 (1987), S. 1397-1400 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690330819
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    Paper (German National Licenses)
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