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Catalase Inhibition Lab
Transcript of Catalase Inhibition Lab
Will the presence of copper sulfate inhibit catalase's reaction rate?
By: Sravya, Ria, Humberto, and Julia
Sources of Error
Varying amounts of input
The amount of substance that was intended to have been used may have deviated slightly due to inevitable human error and other limitations.
If 50 mM of CuSO4 (copper sulfate) is added to a mixture of catalase, H2O2 (hydrogen peroxide), and H20 (water), then the enzyme catalase will no longer function due to the breakage of the disulphide bonds by the copper sulfate.
Catalase Inhibition Lab
This was dependent on the location in the classroom we performed our experiment, which was close by the windows. This could have resulted in a slightly colder environment for the experiment, which could affect our results.
Non-distilled water residue
Between trials, we washed the nalgene bottles used in non-distilled water. Some drops may have remained inside the bottle even after it was dried.
Varying force used swirling
The method and forces applied while swirling the solution may have had slight differences between each trial.
Our experiment consisted of a solution containing potato pulp catalase, hydrogen peroxide, and distilled water.
Copper sulfate was used as the inhibitor. This was added to our solution.
Slight differences in time
Some error may have arose due to slight errors in time-keeping.
Our 10 mM stock
The undiluted CuSO4
This run depicts the data we collected during the second baseline run. As expected, the data shows an increase in the percentage of oxygen as the catalase breaks down the hydrogen peroxide. The oxygen increased at a rate of 0.00096759% (parts per hundred) per second.
Prior to the experiment, we predicted that:
This run depicts the data we collected during the 20 mM copper sulfate concentration run. As expected, the data shows a decrease in the percentage of oxygen as the copper sulfate inhibits the breaking down of the hydrogen peroxide by the catalase. The oxygen decreased at a rate of -0.00021753% (parts per hundred) per second.
The run depicts the data we collected during the 30 mM copper sulfate concentration run. The data shows a decrease in the percentage of oxygen similar to the 20 mM of copper sulfate. The oxygen decreased at a rate of -0.00033642% (parts per hundred) per second.
Data for All Trials
The catalase was not functioning properly and was replaced with a new sample of catalse
The run depicts the data we collected during the 50 mM copper sulfate concentration run. The graph for this run is odd in that the correlation starts negative, but ends with a postive slope. Many confounding variables can be at play.
Our results show that the presence of copper sulfate does inhibit the reaction rate of the catalase and the hydrogen peroxide. The data showed that a moderate concentration of CuSO4, such as a 20 mM or a 30 mM concentration had the most effect with the seemingly fewest number of confounding factors. Our data proved our hypothesis wrong, as we initially believed that the run with the greatest concentration of copper sulfate (50 mM) would inhibit the catalase the most, as it would be able to break more of the disulphide bonds in the catalase.
This experiment demonstrates one of the ways in which an enzyme can be prevented from functioning, either through inhibition or denaturing. Enzymes play an important role in chemical reactions by acting as a catalyst, often being necessary for the survival of an organism. In animals and protists, the enzyme catalase breaks down the naturally occurring hydrogen peroxide, which can be toxic if it accumulates. If the enzyme were to be inhibited by an agent such as copper sulfate or denatured by other factors, such as temperature and pH, then it would not be able to convert the H2O2 into water and oxygen. If that were to happen, there could be fatal consequences for the organism, such as severe damage to cells and tissues. Such possibilities further exemplify the importance of enzymes in biological organisms.