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  • Wiley-Blackwell  (2)
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  • 1
    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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    Paper (German National Licenses)
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  • 2
    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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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