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Corynebacterium glutamicum - JUWEL - Forschungszentrum Jülich

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2. Theory<br />

For batch fermentations, the equations can be simplified since all fluxes are 0 7 . For<br />

chemostat fermentations at steady state, all time derivatives are 0 which simplifies the<br />

balance to yield:<br />

− r = �<br />

f<br />

Ff (Cf − Css)<br />

V<br />

(2.6)<br />

which can readily be solved using the steady state concentration Css.<br />

For fed-batch fermentations, such general simplifications cannot be made. The concentrations<br />

can however be simulated over time when the initial concentrations C(0) and<br />

the fluxes are known and kinetic equations for the conversion rates as a function of the<br />

concentrations are given:<br />

2.3.2. Kinetics<br />

� t<br />

C(t) =C(0) +<br />

t=0<br />

˙Cdt (2.7)<br />

Now the challenge is to find kinetic descriptions for the conversion rates r as a function<br />

of the concentrations for all relevant substances: biomass, substrate(s) and product(s).<br />

One common type of kinetic equations is the Monod kinetics, which is based on the<br />

Michaelis-Menten type enzyme kinetics (Michaelis and Menten, 1913):<br />

r = vmaxCSCC<br />

Km + CS<br />

(2.8)<br />

where CS is the concentration of substrate, CC the catalyst concentration and Km<br />

the Michaelis-Menten constant, which is a binding constant, equal to the concentration<br />

needed to achieve an enzyme specific conversion rate 8 of half the maximal specific conversion<br />

rate vmax. For more detailed explanation of the theoretical background of this<br />

equation and similar enzyme kinetic models, see for instance Biselli (1992); Roels (1983).<br />

For biomass growth on one limiting substrate, the Monod kinetics (Monod, 1942) can<br />

be written analogously as:<br />

CSCX<br />

rx = µmax<br />

KS + CS<br />

rs = − rx<br />

Yxs<br />

(2.9)<br />

(2.10)<br />

7 except for the fluxes for for instance pH control and the flux of samples out of the reactor. The first<br />

of which is usually of little importance as long as sufficiently high concentrations of the correction<br />

fluids can be used. The last point is usually only of importance in research where many samples are<br />

taken and small biorectors are being used. However, since this does not change the concentrations<br />

but changes all amounts in an equal way, and since no substrates are added into the system, this can<br />

also be neglected.<br />

8 This is the conversion rate per unit enzyme, for instance in mmolsubstratemmol −1<br />

enzymes −1<br />

12

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