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  • 1
    Electronic Resource
    Electronic Resource
    Immobilized enzymes: Pectin esterase covalently coupled to dorous glass particles (1975)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 17 (1975), S. 85-98 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Pectin esterase (E.C. 3.1.1.11) was covalently immobilized to porous glass particles by reaction of the native protein with pendant, benzoyl azide groups of the carrier. Enzyme loading on the carrier was 0.5 unit per ml as measured by pH stat, assay. Decreasing the size of the immobilized enzyme particles by grinding produced a 12-fold increase in activity suggesting severe internal mass transport restrictions on turnover kinetics, Gross fractionation of the citrus pectin substrate into high and low molecular weight categories and their subsequent use in kinetic characterization shows no effect of molecular weight upon the kinetic behavior of the native enzyme. In contrast the immobilized enzyme displayed a 5-fold increase in the apparent. Km for the high molecular weight fraction relative to that of the low molecular weight fraction. A striking difference exists in the low pH profile of immobilized pectin esterase relative to the native enzyme. Carrier matrix interactions with the polyelectrolyte substrate are invoked to explain this difference. The thermal stability of the immobilized enzyme is relatively low and displays a half-life of approximately 2 weeks at 25°C.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260170107
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  • 2
    Electronic Resource
    Electronic Resource
    Pore diffusion model for a two-substrate enzymatic reaction: Application to galactose oxidase immobilized on porous glass particles (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 18 (1976), S. 987-1000 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An analysis of the pore diffusion model involving a two-substrate enzymatic reaction is presented. The resulting equations have been applied to the case of galactose oxidase catalyzed oxidation of galactose when the enzyme is immobilized on porous glass particles. The physical constants of the system were obtained by theoretical predictions and the enzyme concentration in the porous medium was derived from the experimental results. The calculations were performed with the assumption that the kinetic parameters of the enzyme remain unchanged upon immobilization. The theoretically calculated effectiveness factors were compared with the experimental effectiveness factors determined from the batch kinetic experiments and were found to be in agreement. The results are presented as effectiveness factor plots graphed as functions of bulk galactose and oxygen concentrations. The model was extended in order to study the effect of external mass transfer coefficients and pore enzyme concentrations on the effectiveness factors.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260180711
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  • 3
    Electronic Resource
    Electronic Resource
    Galactose Oxidase: Applications of the covalently immobilized enzyme in a packed Bed configuration (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 18 (1976), S. 1679-1694 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Galactose oxidase (E.G. 1.1.3.9) was covalently immobilized to chemically modified porous silica particles by reaction of the native enzyme with pendant benzoyl azide groups on the carrier. The enzyme loading on the carrier was 100-150 units per milliliter. The immobilized enzyme was incorporated into a hardware assembly suitable for the determination of galactose or lactose concentrations in complex biological fluids. The prototype instrument as described is suitable for continuous, on-line monitoring or discrete sample analysis. Reaction conditions can be readily provided which maintain global first order kinetics within the reactor and strict linearity of the procedure over a wide range of sample concentrations. Auto-inactivation of the immobilized enzyme can be prevented by K3Fe(CN)6 and long-term reactor stability can be achieved by the periodic application of the reagent to the enzyme reactor in situ.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260181204
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