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  2. Substrate inhibition in bioreactors - Wikipedia

    en.wikipedia.org/wiki/Substrate_inhibition_in...

    Substrate inhibition in bioreactors occurs when the concentration of substrate (such as glucose, salts, or phenols [1]) exceeds the optimal parameters and reduces the growth rate of the cells within the bioreactor. This is often confused with substrate limitation, which describes environments in which cell growth is limited due to of low substrate.

  3. Reversible Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Reversible_Michaelis...

    Enzymes act on small molecules called substrates, which an enzyme converts into products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. The study of how fast an enzyme can transform a substrate into a product is called enzyme kinetics.

  4. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    in which e is the concentration of free enzyme (not the total concentration) and x is the concentration of enzyme-substrate complex EA. Conservation of enzyme requires that [28] = where is now the total enzyme concentration. After combining the two expressions some straightforward algebra leads to the following expression for the concentration ...

  5. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    They are classified according to the effect of the inhibitor on the V max (maximum reaction rate catalysed by the enzyme) and K m (the concentration of substrate resulting in half maximal enzyme activity) as the concentration of the enzyme's substrate is varied. [15] [16]

  6. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    The analysis of these reactions is much simpler if the concentration of substrate A is kept constant and substrate B varied. Under these conditions, the enzyme behaves just like a single-substrate enzyme and a plot of v by [S] gives apparent K M and V max constants for substrate B. If a set of these measurements is performed at different fixed ...

  7. EPSP synthase - Wikipedia

    en.wikipedia.org/wiki/EPSP_synthase

    When a substrate binds to the enzyme, the conformational change causes the domains to clamp around the substrate at the active site. EPSP synthase is classified into two groups based on sensitivity to glyphosate. Class I enzymes, found in plants and some bacteria, are inhibited by low micromolar concentrations of glyphosate.

  8. Catechol oxidase - Wikipedia

    en.wikipedia.org/wiki/Catechol_oxidase

    In plants, both enzymes can catalyze the oxidation of ortho-diphenols substrates into their corresponding ortho-quinones. The key difference between the two related enzymes is that tyrosinase can catalyze the hydroxylation of monophenols to diphenols (monophenolase activity) as well as the oxidation of the o-diphenol to the o-quinone ...

  9. Fed-batch culture - Wikipedia

    en.wikipedia.org/wiki/Fed-batch_culture

    Many enzymes, especially those involved in catabolic pathways, are subject to this repressive regulation. A powerful method of overcoming the catabolite repression in the enzyme biosynthesis is a fed-batch culture in which glucose concentration in the culture liquid is kept low, where growth is restricted, and the enzyme biosynthesis is ...