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  • 1
    Electronic Resource
    Electronic Resource
    Diffusion and the limiting substrate in two-substrate immobilized enzyme systems (1982)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 24 (1982), S. 2705-2719 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effects of mass transport resistances on two-substrate immobilized enzyme systems are investigated theoretically. It is shown that the effects of mass transport resistances on the overall reaction rate are related mainly to the transport of the limiting substrate. In the absence of external mass transport resistances, the limiting substrate can be identified by knowing only the ratio of the bulk substrate concentrations, the permeability of the support to the two substrates, and the stoichiometry of the reaction. However, a combination of internal and external mass transport resistances may result in the other substrate becoming limiting. These effects are most significant when the mass transport resistances are high. Applications in the design of enzyme electrodes and chemical reactors are discussed.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260241208
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  • 2
    Electronic Resource
    Electronic Resource
    Determination of the intrinsic kinetic constants of immobilized glucose oxidase and catalase (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 29 (1987), S. 696-704 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Models of membrane systems containing immobilized glucose oxidase and catalase operating together or independently have been developed. A rotated disk electrode apparatus was employed with novel electrochemical operating conditions to experimentally determine mass transfer and intrinsic kinetic parameters of enzyme-containing membranes. The value of a mass transfer parameter that describes internal and external diffusion was first determined under conditions that do not permit the enzyme reactions. In a subsequent experiment with the reaction allowed, kinetic parameters corresponding to the intrinsic maximal velocity and Michaelis constants of the immobilized enzymes were estimated by regression analysis of data based on an appropriate two- or three- parameter model. It was found that immobilization reduced the maximal intrinsic velocity but had no detectable effect on the Michaelis constants. In all but one case- these methods for membrane characterization are nondestructive and can be used repeatedly on a given membrane. These techniques provide the means for quantitative comparisons of immobilization methods and make possible temporal studies of immobilized enzyme inactivation.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260290606
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  • 3
    Electronic Resource
    Electronic Resource
    Time-dependent inactivation of immobilized glucose oxidase and catalase (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 29 (1987), S. 705-713 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Homogeneous membranes containing immobilized glucose oxidase and catalase were stored in buffered solutions at 37°C to determine the mechanisms and rates of catalyst inactivation. The experiments were designed so that inactivation occurred homogeneously throughout the membrane, thereby simplifying the analysis. The mechanism of inactivation is consistent with the reaction of hydrogen peroxide and certain catalytic intermediates of both enzymes. Based on this information, numerical simulations were developed that incorporate spatially heterogeneous catalytic and inactivation processes.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260290607
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  • 4
    Electronic Resource
    Electronic Resource
    A novel rotated disc electrode and time lag method for characterizing mass transport in liquid-membrane systems (1980)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 26 (1980), S. 1013-1019 
    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 time lag method is described for use with a membrane-covered, rotated disc electrode that allows determination of the partitioning and diffusivity of small molecules in hydrophilic gel membranes and membrane permeability from a single measurement. This new technique takes into account the concentration boundary layer in the solution adjacent to the membrane and reaction at the electrode surface of solutes that are diffusion- or kinetic-limited. Examples are given of the use of this method for characterizing mass transfer in a commercial cellulosic membrane with oxygen, hydroquinone, ferrocyanide, and glucose as solutes.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690260617
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