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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 34 (1989), S. 357-368 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The performance of an ultrafiltration hollow-fiber reactor, in which the enzymatic synthesis of glucose 6-phosphate from glucose and cofactor ATP and the enzymatic regeneration of ATP from ADP and acetyl phosphate are performed simultaneously, was analyzed theoretically. A simple analytical model in which the liquid flowing in the fiber tubes is assumed to be plug flow, and the radial concentration gradients in the tube and shell sides are both neglected, could simulate the reactor performance with satisfactory accuracy. The simulation elucidated the effects of the reactor configurations and various operational conditions on glucose conversion, ATP recycle number, and space-time yield. If the fiber tubes, through which the permeability of the relevant components such as substrates is high, were packed as much as possible in the reactor, good reactor performance could be expected. Furthermore, with a sufficiently high enzyme concentration, low ATP concentration in the feed solution, and appropriate space velocity, good space-time yield with high glucose conversion and with very high ATP recycle number is theoretically possible.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Enzymatic synthesis of glucose 6-phosphate from glucose and ATP catalyzed by glucokinase from B. stearothermophilus and enzymatic regeneration of ATP from ADP and acetyl phosphate catalyzed by acetatekinase from B. stearothermophilus were simultaneously performed in an Ultrafiltration hollow-fiber reactor of the multitubular heat-exchanger type. Experimental results of space-time yield, the conversion, and ATP recycle number were in good agreement with the theoretical predictions based on the simple analytical model developed in the preceding article. The best results for space-time yield and conversion were Ys = 1.97 mol/m3 h and X = 92.8%, respectively, under the same conditions, and the best result for the ATP recycle number was NR = 2130 under conditions different from those above. However, Ys = 1.72 mol/m3 h, X = 81.2%, and NR = 1620 were the results when the space-time yield, conversion, and recycle number were at the highest in combination under the same conditions. Results of long-term operation showed that the apparent remaining activity of the enzyme system was ca. 55% after continuous operation for 16 days, the decrease in the enzyme activity being faster than that expected from their half-life times determined individually in the homogeneous system.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 29 (1987), S. 924-933 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: For a reversible one-substrate reaction system that follows the Haldane reaction mechanism, a new and effective method has been proposed to extract true or intrinsic kinetic parameters of immobilized enzymes from diffusion limited rate data. The method utilizes the effectiveness factors correlated in terms of the general modulus defined by Aris and Bischoff, and a new modulus defined in the present study. It requires a trial-and-error calculation, but only a few data points. Furthermore, it provides a saving of materials such as substrates and enzymes, and takes less time for experiments compared to the initial rate methods. The usefulness of the method is demonstrated by determining the kinetic parameters for membrane bound fumarase which catalyzes the reaction of the conversion of fumarate to L-malate, for which the equilibrium constant is ca. 4.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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