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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Analytical chemistry 67 (1995), S. 1669-1678 
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 42 (1996), S. 829-836 
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Many living organisms store iron in solid form, Fe(III), as a crystal in the inner cavity of the ferritin molecule. When iron is needed for biosynthesis, a reducing agent reduces Fe(III) into the soluble form Fe2+ released by ferritin. Crystallization and release processes are reversible, and their rates evolve in an identical way as a function of the number n of iron atoms in the molecule. The rate increases with n, showing a maximum value when n is approximately 1,300, and then stabilizes for the highest values of n, which can reach 4,500. On the other hand, plotting the amount of released iron as a function of time gives curves with a sigmoid shape. The proposed model was based on the theoretical description of different steps involved in crystal growth inside the protein shell: several independent crystals grow freely at the inner protein wall, and then a distribution function takes into account possible overlapping of different crystallite clusters, whose further growth is limited by diminution of the available space inside the cavity. The kinetics derived was then used to calculate the release curve as a function of time. Solving the system of differential mass-balance equations was simplified by describing the ferritin population as a large discrete distribution of species. The model fully fitted and explained the variation in the crystallization rate with n, and the sigmoid shape of the release curve as a function of time obtained experimentally in a thin-layer electrochemical cell.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 41 (1995), S. 1944-1954 
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Thin-layer electrochemical reactors are analytical reactors where mass transfers are generally assumed not to affect the overall reaction rate. The validity of this hypothesis was tested for systems involving a second-order or an enzymatic homogeneous reaction that consumed the product generated by the electrochemical heterogeneous reaction. The experiments were performed with the oxidation of hexacyanoferrate II into hexacyanoferrate III, coupled with the consumption of hexacyanoferrate III by the reduced form of nicotinamide adenine dinucleotide, catalyzed or not by a diaphorase. The tools commonly used for gas - liquid interfaces were adapted to the description of mass transfer in a closed thin film. The theoretical model agreed well with the experimental data and served as the basis for testing the thin-layer hypothesis. The validity of the hypothesis was plotted as a function of the Hatta and Damköhler numbers. The influence of concentration and diffusion parameters are discussed with focus on the validity criterion.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 42 (1996), S. 2967-2976 
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Electrochemical biosensors were used to develop a numerical model of transient mass transfer coupled with enzymatic reactions in thin multilayer microstructures. A finite volume method integrates the partial derivative mass-balance equations making the model very versatile. With a multilayer physical description, general nonlinear enzymatic kinetics and efficient space discretization, the model could be applied to various devices under a broad range of physicochemical conditions. Theoretical results were validated according to experimental data obtained with three different biosensors involving homogeneous or heterogeneous enzymatic catalyses. Model predictions are further discussed for a bienzymatic immobilized enzyme system. The biosensor transient behavior depended strongly on the location of the enzymes in the device and on the mass-transport features. A transient maximum on the current-time curves was predicted accurately by the model. This could be used to improve the biosensor performance. The model can also be a useful framework for designing new electrochemical microreactors.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 68 (1997), S. 389-396 
    ISSN: 0268-2575
    Keywords: biochemical synthesis ; electrochemical reactor ; oxidoreductase immobilisation ; electropolymerised modified electrode ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: In many fields such as fine chemistry and pharmacy, biotechnology is increasingly being used to produce natural-like molecules of great interest. The main method remains fermentation which results in complex mixtures in which there is only a very small amount of the required compound. Numerous downstream separation steps are necessary, which are expensive and generate large amounts of polluting wastes such as solvents, resins or salts. Using free enzymes extracted from microorganisms would avoid most of these separations and wastes. Oxidoreductases catalyse a lot of electron transfer reactions involved in many economically interesting syntheses, but electron extraction or feed is still a critical stage in developing free enzyme processes with them. The use of an electrochemical reactor to ensure electrical extraction or feed would provide a good step towards cleaner processes because the highest selectivity would be ensured without any by-products being generated. The first purpose of this paper is to show the broad application field of oxidoreductases in which electrochemistry could be introduced with some benefit. A concise analysis of the first electroenzymatic reactor design shows that in order to develop such economically efficient reactors, the enzymes must be confined in the strict vicinity of the electrode surface. Consequently, the experimental part is devoted to the development of an electrode/enzyme interface specificially adapted to synthesis processes. Electropolymerisation of pyrrole on a platinum electrode was used to entrap successively glucose oxidase for gluconic acid production, and hydrogenase for NADH regeneration. Emphasis was placed on increasing the mass transfer rates in the film and the amount of enzyme retained. © 1997 SCI.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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