Catalysis by micelles

Enzymes and micelles resemble each other with respect to both structure (e.g., globular proteins and spherical aggregates) and catalytic activity. Probably the most common form of enzyme catalysis follows the mechanism known in biochemistry as Michaelis-Menton kinetics. In this the rate of the reaction increases with increasing substrate concentration, eventually leveling off. According to this mechanism, enzyme E and substrate A first react reversibly to form a complex EA, which then dissociates to form product P and regenerate the enzyme  

The various k s are the rate constants for the specific reactions shown. Standard kinetic analysis of this mechanism predicts that the rate of product formation is given by 

003 M NaOH are plotted versus the concentration of various alkyl trimethyl ammonium bromides. Several things should be noted about these data  

The catalytic role of the surfactant begins more or less sharply at the CMC. The C10 and C 2 surfactants also show catalytic activity above their respective CMCs at higher concentrations. 

The enhancement of rate qualitatively follows Michaelis-Menton kinetics, with both the initial slope and the final plateau increasing with increasing length of the alkyl tails of the surfactant. 

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Catalysis, by micelles, membranes and other aqueous aggregates as models of enzyme action, 17,... 

Catalysis by Micelles, Membranes and other Aqueous Aggregates as Models of Enzyme Action... 

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