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  • 1
    Digitale Medien
    Digitale Medien
    Reactivation of Horseradish peroxidase in organic solvent using extraction (2000)
    Springer
    Biotechnology letters 22 (2000), S. 485-489 
    Details
    ISSN: 1573-6776
    Schlagwort(e): enzyme ; extraction ; Horseradish peroxidase ; organic solvent ; reactivation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Abstract A novel extraction method was developed aiming at increasing the stability of enzymes in organic solvent media. Horseradish peroxidase (HRP), inactivated in a tetrahydrofuran (THF)/water (1:1, v/v), regained and maintained its activity when HRP was extracted by adding a THF/benzene mixture to the original solution. However, the HRP activity was drastically lowered in the enzyme-free blank solution that had been formed by employing the same extraction procedure. As a result, the reactivation after the extraction is believed to depend on enzyme history, and might be arisen from an irreversible structural change of the enzyme.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1023/A:1005660131552
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Mathematical Analysis of an Enzymatic Reaction in an Aqueous/Organic Two-Phase System: Tyrosinase-Catalysed Hydroxylation of Phenol (1997)
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 70 (1997), S. 163-170 
    Details
    ISSN: 0268-2575
    Schlagwort(e): two-phase reaction ; organic solvent ; tyrosinase ; phenol hydroxylation ; mass transfer model ; optimization ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: A mathematical model that incorporates both mass transfer effects and reaction kinetics was developed for an aqueous/organic two-phase reaction system. The hydroxylation of phenol by tyrosinase was examined as a model reaction. A mildly agitated reactor was employed to maintain a quiescent liquid-liquid interface and stable enzyme activity. Mass transfer rate was expressed as a function of bulk concentration of substrate in both phases, partition and mass transfer coefficients. The model fitted the experimental data well for various reaction conditions such as initial substrate concentration, phase volume ratio, agitation speed and organic media used. Simulations showed that the conversion of substrate was strongly dependent on the initial substrate and enzyme concentrations and phase volume ratio. A lower fraction of organic phase led to an improved product partition and a higher fraction of organic phase to a greater substrate partition. The proposed model could be used for the optimization of two-phase enzymatic reaction systems. © 1997 SCI
    Zusätzliches Material: 9 Ill.
    Materialart: Digitale Medien
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