Enzymes Lab Report

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Recommended: Lab report of enzyme kinetics

The enzyme used in the experiments is called alkaline phosphatase. The enzyme was isolated from cow intestine, but can also be found in bone and embryo germ cells. Alkaline Phosphatase cleaves phosphate off any molecule in an alkaline buffer. In order to determine the function, we ran two experiments to study the enzyme. The first experiment we ran to determine the Vmax and Km. We first got our raw data and plotted an absorbance over time graph, then from that information we could graph a Michaelis-Menten graph to get our Vmax and Km. We also found out at what concentration our enzyme works best under. For the second experiment, we altered the pH conditions that our enzyme would be in. We changed the pH by adding NaOH or HCl. Then we took the …show more content…

In figure one you can see that the Michaelis-Menten fit has a positive increase. There’s a significant increase from 0-4, then it starts to level off as it reaches the Vmax. As the concentration of substrate increase the reaction velocity increases as well. In figure two you see a positive correlation between the time and the absorbance. When the pH was at 10.4 you saw a greater increase then when the pH was at 4.4. The goal of the experiments of Enzyme Kinetics 1 and Enzyme Kinetics 2 were to determine the enzyme activity of alkaline phosphatase. Week one we determined the Vmax and KM (Figure 1). Week 2 we determined if changing the PH level were to cause an effect of the efficiency of the enzyme (Figure …show more content…

In figure 4 you can see that the greatest slope is from the stock solution that is due to the fact that there are many alkaline phosphatase in the stock solution. However, dilution 5 has the lowest absorbance since it is the most diluted concentration there are not many enzymes present. Therefore the enzyme runs best when it is at a higher concentration. From the raw data, a Michaelis-Menten graph was constructed. The Michaelis-Menten graph gave us the Km and Vmax. The Km value was 1, the Km value represents the affinity. Since Km is a low number means a small number of substrate is needed to saturate and enzyme (Figure 1). The Vmax is 5.050, Vmax determines the rate of reaction. The enzyme activity was 50.5, which is a measure of the quality of active enzyme present. The specific activity was 2525, the specific activity I got was much larger than the one given by the company where the enzyme was bought from. That can be due to a mess up in carrying out the

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