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  • Biochemistry and Biotechnology  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Biochemical switching device: Monocyclic enzyme system (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 32 (1988), S. 527-537 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The switching characteristics of a monocyclic enzyme system, in which two enzymes share substrates or co-factors in a cyclic manner, such as, → X1 + B + E1 ⇄ A + E1 + X2 →, → X3 + A + E2 ⇄ B + E2 + X4 → (E1, E2 are enzymes, X1, X3 are substrates, X2, X4 are products, A, B are cofactors), were demonstrated using computer simulations. The detailed mathematical models of biochemically possible cyclic enzyme systems were built up and the effects of rate constants and the effects of initial concentrations of enzymes and cofactors on switching characteristics were discussed. The cyclic enzyme system could function as a switching circuit when the initial concentrations of enzymes or cofactors are over a certain threshold value. Based on the present results, we further discuss the dynamic characteristics of a biochemical reactor system (bioreactor) involving this cyclic enzyme system as a switching controller.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260320416
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  • 2
    Electronic Resource
    Electronic Resource
    Kinetic characteristics of biochemical cyclic reaction systems: Amplification of substrate cycle system (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 132-136 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The amplification of a substrate cycle system with reversible closed reaction of two substrates was represented by mathematical equations. The results are summarized as follows: the amplification was affected especially by the affinity of enzyme and substrate, by the rate constant in rate-limiting reaction step, and by the saturation degree of enzyme by substrate. These amplifications were not simply determined by the values of Km and Vmax, because each rate parameter in the system can affect the degree of amplification independently. The conclusion is that the “apparent” equilibrium constant of this system cannot be uniquely estimated from only data of Km and Vmax even if the reaction occurs in a closed system.
    Additional Material: 5 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270205
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  • 3
    Electronic Resource
    Electronic Resource
    Steady-state approximation of enzyme activation and inhibition (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 1453-1463 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This article deals with the effects of the initial concentration of effector (inhibitor or activator) on the steady-state approximation of enzyme kinetics. The results could be summarized as follows: (1) In competitive inhibition, the increase in the initial concentration of inhibitor led to the reduction of steady state time. (2) In noncompetitive and uncompetitive inhibitions, the steady state time was not changed with the increase in the initial concentration of inhibitor. (3) In nonessential activation, the increase in the initial concentration of activator led to the reduction of steadystate time. (4) It was specially noted that in nonessential activation, even if the reaction is in the steady-state, activation constant (KA) can not be determined exactly unless the initial concentration of activator is very small.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260250604
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