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Hydrogen Peroxide Catalase Reaction Lab

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Conclusion In conclusion, the reason why this lab was conducted to examine the effects of Hydrogen Peroxide coming into contact with a catalase solution, in this experiment it was Calf Liver. As a result of the contact, oxygen gas was formed. Therefore, the collected data suggested the rate of reaction of the catalyse increases as the volume of Hydrogen Peroxide increases. This can be seen through the linear trend line that moves up in a positive direction, which shows that the relationship between the rate of reaction and the volume of hydrogen peroxide is positive. However, the increase in the rate of change is non-constant. When comparing this lab to that of another the results are similar. For example, in both the labs, the decomposition …show more content…

This is significant because the reaction can be altered based on the volume of catalase the Hydrogen Peroxide is exposed to. So with more catalase on the tab, the Oxygen displaced would be increased. However, with less catalase covering the tab, the amount of oxygen displaced will be lowered. An improvement that can be made in order to prevent the uneven amount of liver solution covering the tab, is to measure a specific amount of liver solution for the tab to be dipped into. This would improve the results because the amount of oxygen that will be displaced will be consistent throughout the lab. Thus, by doing …show more content…

This limitation is significant because the pressure of released gas, oxygen, is the dependant variable that is depending on the amount of substrate that the catalase liver solution is exposed to. However, the water droplets would not have been enough to cause the results to be change too much. Using a paper towel to dry the inside of the test tube or a test tube rack to allow the test tube to dry naturally. This improvement will prevent water molecules from mixing into the Hydrogen Peroxide solution and therefore will not act as a physical interference with the substrate and the catalase enzyme. (Allot, et al,

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Nevertheless, the effects caused by the breakage of bonds will eventually lead to a decrease in the rate of reaction. As seen in the data, the reaction rate increased from 0.088 to 0.101 throughout the interval of -5℃ to 20℃ then decreased to 0.037 throughout the interval 20℃ to 56℃. This can be explained by the fact that 20℃ is the optimal temperature, therefore the active site of the enzyme is complementary to the substrate, causing the rate of reaction to be

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1410 Words | 6 Pages

Catalase Activity on Substrate Based On Gas Pressure Production Rate Name of the Class Author’s Name Date Enzymes are organic compounds which act as catalysts and speed up biological reactions in biological organisms. They are not destroyed or changed during the reaction but rather they are used over and over again to catalyze many more reactions. Their activity may be affected and altered by factors such as temperature, substrate concentration, enzyme concentration and Ph.

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The addition of the extra catechol was supposed to have sped up the reaction with the enzyme and force the inhibitor out of the enzymes active site. If there was more time allowed to observe any possible color changes the results would have been more conclusive and our results more accurate. In other

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The three things that can cause the enzyme to denature is a large change in pH level, High Temperature, and substrate concentration. According to our knowledge, we know that a large change in pH will cause instability in the protein structure thus resulting in denaturation of the enzyme. From the data, we can see that pH 3 (total:6.3) and 10 (total:6.2) were the slowest because pH 3 is probably the highest acid and pH 10 is the highest base. The highest acid or base pH represents a large change which would cause the enzyme to denature. The fastest pH was 6 (total:34.5), and it seems that there wasn’t a large change which resulted in a stable structure.

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492 Words | 2 Pages

The Catalase test was used to determine whether or not the unknown contains Catalase enzymes that would react when hydrogen peroxide was added. If the unknown contained Catalase enzymes then the unknown would bubble/fizz when the hydrogen peroxide was added, and would be recorded as a positive reaction. If the unknown did not contain Catalase enzymes there would be no reaction, and would be recorded as a negative reaction. The procedures for this test included: obtaining a microscope slide with your unknown sample on it and placing 1-2 drops of hydrogen peroxide on it. The results of the Catalase test would be determined that same

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ABSTRACT To catalyze a reaction, an enzyme will grab on (bind) to one or more reactant molecules. In this experiment we examined how increasing the volume of the extract added to the reaction would affect the rate of the reaction. The enzyme used was horseradish peroxidase which helps catalyze hydrogen peroxide. Using different pH levels, the absorbance rate of the reaction was measured to see at which condition the enzyme worked best. The rates of absorption were calculated using a spectrophotometer in 20 second intervals up to 120 seconds.

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901 Words | 4 Pages

After record your data and determine the absolute rate of the enzyme-catalyzed reaction. Based on the data and observations the hypothesis was accepted. It was accepted because when pH were changed to a variety of levels the transmittance began to get higher reaction rates. The increased absorbance means greater amount of product and a higher reaction rate will be produced.

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The cleanliness of the apparatus used is was a possible source of error. Even after trying to find the cleanest pipets and glassware, there were a distinct hint of purple and blue that covered parts of the apparatuses. Even after cleaning with ethanol, the residue could not be fully removed from the materials, thus possibly affecting the concentration of solutions that passed through the stained apparatuses. Having a more effective cleaning method would resolve this source of error. Since the reaction between the dye and NaOH was instantaneous, it was impossible to mix the solution together and measure the absorbance of the solution from the moment of reaction.

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899 Words | 4 Pages

H20 + 2 O2 This experiment will use 1% catalase solution and 3% hydrogen peroxide solution, both diluted into water so the reaction slows down. Temperature will be controlled in this experiment to change the reaction speed of the enzyme and the substrate, this is what the experiment is looking at. The effect of the temperature will be determined by how much gas is released in two minutes, which will change the pressure inside the test tube and will be measured by a gas

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180 Words | 1 Pages

From this experiment, the data gathered support the hypothesis. For the first trial, in the cold hydrogen peroxide the reaction lasted six minutes and twenty-one seconds, in the warm hydrogen peroxide the reaction lasted two minutes and fourteen seconds, and in the room temperature hydrogen peroxide the reaction lasted for two minutes and thirty-one seconds. During the second trial, in the cold hydrogen peroxide the reaction lasted five minutes and fifty-seven seconds, in the warm hydrogen peroxide the reaction lasted one minute and fifty-five seconds, and in the room temperature hydrogen peroxide the reaction lasted for two minutes and sixteen seconds. The warm hydrogen peroxide reactions were about four minutes faster than the cold hydrogen

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By doing

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Catalase (CAT) activity 255 With slight modifications, catalase activity was assayed according to the method of Aebi 256 (41) by monitoring the disappearance of H2O2 at 240 nm. The 3 ml reaction

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20 20 5 10 10 1.00 15.81 0.06 Graph Discussion: From the table and graph above it was observed that decrease in the concentration of hydrogen peroxide increased the time for the blue black colouration to appear, which gave rise to decrease in the rate of the reaction. The volume of distilled water added as shown in the table was to reduce the concentration of the hydrogen peroxide. The same trend was observed in the dilution of potassium Iodide.

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Therefore, through such

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If this test is positive, the hydrogen peroxide which is dropped onto the colonies in the streak plate will begin to bubble. If bubbles are produced that means the organism is an aerobe. Because H2O2 is such a potent agent, if an organism lives in the presence of O2, they need to be able to break down the H2O2 to survive. The bacteria tested positive for catalase, as the hydrogen peroxide was dropped onto the streak plate, it immediately began to produce bubbles.

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