Km And Vmax And Enzyme Kinetics

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An enzymatic reaction also known as enzyme kinetics involves enzymes which are catalysts which speed up a reaction without being used up itself and do not appear as reaction products. Kinetics measures the rate of a chemical reaction to help determine the concentration or quantity of the enzyme of interest. Km and Vmax are used as constants in any enzyme reactions. (1) Vmax is known as the maximum velocity at which the reaction can be catalysed. It is used to measure the enzymes concentration and is found when all the enzymes active sites are saturated with the substrate. Km is the concentration of substrate which permits the enzyme from achieving half its Vmax. The lower the Km the greater the affinity the enzyme will have for the substrate. Km and Vmax are determined by saturating the enzyme with different amount of substrate, these results can be then plotted on a graph of rate of reaction vs concentration of substrate which will give you a curve. The slope determined from each curve is also the velocity. The Michaelis constant usually takes the form of an equation where reaction velocity is related to substrate concentration for a system, where a substrate S binds to an enzyme E to form an enzyme-substrate complex ES, which reacts to make a product P and restore the enzyme E. A bright yellow substance is released from the BAPNA, p-nitroaniline. This …show more content…

The primary function of the enzyme in this experiment was to enhance the rate of the reaction to get optimum results which were achieved. As was expected before starting the experiment, in every case, the amount of product formed increased with time until the reaction came to a stop and no change was seen in concentration of substrate or product. So overall the experiment was a success in my opinion with no major mistakes as all data could be calculated and

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