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Bioreactors Engineering

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Presentation on theme: "Bioreactors Engineering"— Presentation transcript:

1 Bioreactors Engineering
Enzymes Class work 1

2 Bioreactors Engineering
Enzymes

3 Bioreactors Engineering
Enzymes

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Enzymes Class work 2

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Enzymes Home work 1

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Enzymes End of Enzyme kinetics

7 Inhibited enzyme kinetics
Bioreactors Engineering Enzymes Inhibited enzyme kinetics Certain compounds may bind to enzymes and reduce their activity. These compounds are known to be enzyme inhibitors. Enzyme inhibitions may be irreversible or reversible. Irreversible inhibitors such as heavy metals (lead, cadmium, and mercury ) form a stable complex with enzyme and reduce enzyme activity. Such enzyme inhibition may be reversed only by using chelating agents such as EDTA (ethylene-diamine-tetra-acetic acid) and citrate. Reversible inhibitors may dissociate more easily from the enzyme after binding. The three major classes of reversible enzyme inhibitions are Competitive Noncompetitive, Uncompetitive inhibitions, Uncompetitive substrate inhibitions The substrate may act as an inhibitor in some cases.

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Enzymes Inhibited enzyme kinetics Competitive inhibitors Competitive inhibitors are usually substrate analogs and compete with substrate for the active site of the enzyme. The Competitive enzyme scheme can be described as; ES E + S K1 K-1 E + P KI K2 EI + I

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Enzymes Inhibited enzyme kinetics Competitive inhibitors

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Enzymes Inhibited enzyme kinetics Competitive inhibitors The net effect of competitive inhibition is an increased value of Km, app, and therefore, reduced reaction rate. competitive inhibition can be overcome by high concentrations of substrate. Fig. describes competitive enzyme inhibition in the form of a double-reciprocal plot.

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Enzymes Inhibited enzyme kinetics Noncompetitive inhibitors Noncompetitive inhibitors are not substrate analogs. Inhibitors bind on sites other than the active site and reduce enzyme affinity to the substrate. Noncompetitive enzyme inhibition can be described as follows;

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Enzymes Inhibited enzyme kinetics Noncompetitive inhibitors

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Enzymes Inhibited enzyme kinetics Noncompetitive inhibitors The net effect of noncompetitive inhibition is a reduction in High substrate concentrations would not overcome noncompetitive inhibition. Other reagents need to be added to block binding of the inhibitor to the enzyme. In some forms of noncompetitive inhibition is reduced and is increased. This occurs if the complex ESI can form product.

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Enzymes Inhibited enzyme kinetics Uncompetitive inhibitors Uncompetitive inhibitors bind to the ES complex only and have no affinity for the enzyme itself. The scheme for uncompetitive inhibition is

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Enzymes Inhibited enzyme kinetics Uncompetitive inhibitors

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Enzymes Inhibited enzyme kinetics Uncompetitive inhibitors The net effect of uncompetitive inhibition is a reduction in both Vm and Km values. Reduction in Vm has a more pronounced effect than the reduction in Km and the net result is a reduction in reaction rate. uncompetitive inhibition is described in Fig. in the form of a double-reciprocal plot.

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Enzymes Inhibited enzyme kinetics Uncompetitive substrate inhibitors High substrate concentrations may cause inhibition in some enzymatic reactions, known as substrate inhibition. Substrate inhibition is graphically described in Fig. The reaction scheme for uncompetitive substrate inhibition is; Fig. Comparison of substrate inhibited and uninhibited enzymatic reactions.

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Enzymes Inhibited enzyme kinetics Uncompetitive substrate inhibitors

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Enzymes

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Enzymes Inhibited enzyme kinetics Uncompetitive substrate inhibitors A double-reciprocal plot describing substrate inhibition is give in the Fig. below;

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Enzymes

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Enzymes

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Enzymes

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Enzymes

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Enzymes End of enzyme inhibition


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