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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 1651-1665 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Apparent kinetics and pH-activity relationships have been determined for glucoamylase and glucose oxidase immobilized on activated carbon using a diimide method. Reaction rate expressions of Michaelis-Menten form adequately approximate the observed kinetics for both enzyme preparations over the ranges of substrate concentrations considered. Influences of external mass transfer as well as substrate and product adsorption on interpretation of the experimental data have been examined. Immobilization of a glucose oxidase-gluconolactonase enzyme mixture has been found to increase substantially the ratio of gluconolactonase to glucose oxidase activities compared to the corresponding activity ratio for these enzymes in solution.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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