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Enzyme mediator control

Further discussion on the effects of the reaction media and Lewis acids on lacticily appears in Section 7.2. Attempts to control laciicily by template polymerization and by enzyme mediated polymerization are described in Section 7.3. Devising effective means for achieving stereochemical control over propagation in radical polymerization remains an important challenge in the field. [Pg.176]

Since the first report on the ferrocene mediated oxidation of glucose by GOx [69], extensive solution-phase studies have been undertaken in an attempt to elucidate the factors controlling the mediator-enzyme interaction. Although the use of solution-phase mediators is not compatible with a membraneless biocatalytic fuel cell, such studies can help elucidate the relationship between enzyme structure, mediator size, structure and mobility, and mediation thermodynamics and kinetics. For example, comprehensive studies on ferrocene and its derivatives [70] and polypy-ridyl complexes of ruthenium and osmium [71, 72] as mediators of GOx have been undertaken. Ferrocenes have come to the fore as mediators to GOx, surpassing many others, because of factors such as their mediation efficiency, stability in the reduced form, pH independent redox potentials, ease of synthesis, and substitutional versatility. Ferrocenes are also of sufficiently small size to diffuse easily to the active site of GOx. However, solution phase mediation can only be used if the future biocatalytic fuel cell... [Pg.420]

Equations 2.26 and 2.27 carmot be solved analytically except for a series of limiting cases considered by Bartlett and Pratt [147,192]. Since fine control of film thickness and organization can be achieved with LbL self-assembled enzyme polyelectrolyte multilayers, these different cases of the kinetic case-diagram for amperometric enzyme electrodes could be tested [147]. For the enzyme multilayer with entrapped mediator in the mediator-limited kinetics (enzyme-mediator reaction rate-determining step), two kinetic cases deserve consideration in this system in both cases I and II, there is no substrate dependence since the kinetics are mediator limited and the current is potential dependent, since the mediator concentration is potential dependent. Since diffusion is fast as compared to enzyme kinetics, mediator and substrate are both approximately at their bulk concentrations throughout the film in case I. The current is first order in both mediator and enzyme concentration and k, the enzyme reoxidation rate. It increases linearly with film thickness since there is no... [Pg.102]

The pyridinium salt NAD 19a and its reduced form NADH 20a are important co-factors for many enzymes, fhe reduced form is involved in enzyme mediated reductions where it is converted to NAD. In natural systems, NAD is converted back to NADH by another enzyme-controlled process. Attempts to effect the direct electrochemical conversion of NAD to NADH are not very successful. Reduction on a mercury cathode at -1.1 V see on the first one-electron reduction wave leads to the radical-zwitterion, which reacts further to give dimers. Three stereoisomers of the 4,4 -dimer account for 90 % of the mixture and three 4,6 -dimers form the remainder [78]. Reduction at -1.8 V on the second reduction wave produces only 50 % of enzymatically active 1,4-NADH. The NAD analogue 19b shows related behaviour and one-electron reduction affords two diastereoisomers... [Pg.249]

Now we consider situations in which transformation of the organic compound of interest does not cause growth of the microbial population. This may apply in many engineered laboratory and field situations (e.g., Semprini, 1997 Kim and Hao, 1999 Rittmann and McCarty, 2001). The rate of chemical removal in such cases may be controlled by the speed with which an enzyme catalyzes the chemical s structural change (e.g., steps 2, 3 and 4 in Fig. 17.1). This situation has been referred to as co-metabolism, when the relevant enzyme, intended to catalyze transformations of natural substances, also catalyzes the degradation of xenobiotic compounds due to its imperfect substrate specificity (Horvath, 1972 Alexander, 1981). Although the term, co-metabolism, may be used too broadly (Wackett, 1996), in this section we only consider instances in which enzyme-compound interactions limit the overall substrate s removal. Since enzyme-mediated kinetics were characterized long ago by Michaelis and Menten (Nelson and Cox, 2000), we will refer to such situations as Michaelis-Menten cases. [Pg.750]

Heller, J., and Trescony, P. Controlled drug release by polymer dissolution 11. Enzyme-mediated delivery device. J. Pharm. Sci. 68 919—921, 1979. [Pg.302]

There has been a resurgence of interest in proton-coupled redox reactions because of their importance in catalysis, molecular electronics and biological systems. For example, thin films of materials that undergo coupled electron and proton transfer reactions are attractive model systems for developing catalysts that function by hydrogen atom and hydride transfer mechanisms [4]. In the field of molecular electronics, protonation provides the possibility that electrons may be trapped in a particular redox site, thus giving rise to molecular switches [5]. In biological systems, the kinetics and thermodynamics of redox reactions are often controlled by enzyme-mediated acid-base reactions. [Pg.178]

In the kidneys, parathyroid hormone increases 1 -hydroxylation of calcidiol and reduces 24-hydroxylation. This is not the result of de novo enzyme synthesis, but an effect on the activity of the preformed enzymes, mediated by cAMP-dependent protein kinases. In turn, calcitriol has a direct role in the control of parathyroid hormone, acting to repress expression of the gene. In chronic renal failure, there is reduced synthesis of calcitriol, leading to the development of secondary hyperparathyroidism that results in excess mobilization of bone mineral, hypercalcemia, hypercalciuria, hyperphosphaturia, and the development of calcium phosphate renal stones. [Pg.88]

Long-term control is mediated by changes in the rates of synthesis and degradation of the enzymes participating in fatty acid synthesis. Animals that have fasted and are then fed high-carbohydrate, low-fat diets show marked increases in their amounts of acetyl CoA carboxylase and fatty acid synthase within a few days. This type of regulation is known as... [Pg.929]

Fig. 10.6. Change of the rate hmiting step in t5rrosinase carbon paste electrodes, (a) ind (b) show the flow rate dependence of steady-state currents for unmediated (a) emd mediated (b) enzyme electrodes. Applied potential — 0.05 V vs. Ag/AgCl for ( ) 1 p.M phenol ind ( ) 0.5 mM ferrocyanide as control of diffusion limited response. Error bars show the standard deviation of six electrodes. The cheinge from kinetic to dififtisional control in mediated electrodes results in higher sensitivity and improved operational stability as demonstrated in (c) where (1) represents the FIA response of mediated electrodes and (2) unmediated with consecutive 20 /rl injections of 10 p,M phenol in a thin-layer cell. Applied potential - 0.05 V vs. Ag/AgCl, mobile phase 0.25 M phosphate buffer pH 6.0 ind flow rate 0.7 ml min . ... Fig. 10.6. Change of the rate hmiting step in t5rrosinase carbon paste electrodes, (a) ind (b) show the flow rate dependence of steady-state currents for unmediated (a) emd mediated (b) enzyme electrodes. Applied potential — 0.05 V vs. Ag/AgCl for ( ) 1 p.M phenol ind ( ) 0.5 mM ferrocyanide as control of diffusion limited response. Error bars show the standard deviation of six electrodes. The cheinge from kinetic to dififtisional control in mediated electrodes results in higher sensitivity and improved operational stability as demonstrated in (c) where (1) represents the FIA response of mediated electrodes and (2) unmediated with consecutive 20 /rl injections of 10 p,M phenol in a thin-layer cell. Applied potential - 0.05 V vs. Ag/AgCl, mobile phase 0.25 M phosphate buffer pH 6.0 ind flow rate 0.7 ml min . ...
All biochemical reactions are enzyme-mediated. The rate of an enzyme reaction depends on the substrate concentration at the location of the enzyme and thereby on the diffusion rate of a substrate to the enzyme. It is therefore important to permanently obtain an intimate contact between a cell or enzyme and substrate molecules. Additionally, the product generated in the bioreactor has to be extracted because it may under certain conditions inhibit its own production. In some processes there may also be even a prepurification in the bioreactor itself. If living micro-organisms have to be applied, it is necessary to provide sufficient nutrition and respiration gases in case of aerobic fermentation. All other reaction parameters such as temperature, pH-value and reaction time have to be controlled precisely. In many cases (generally with modem processes) the maintenance of microbiological integrity (sterile process) is absolutely mandatory for a successful fermentation. [Pg.124]


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See also in sourсe #XX -- [ Pg.103 ]

See also in sourсe #XX -- [ Pg.103 ]




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