This experiment was started by having one regular sized tub, filled up with water. Next a 100mL graduated cylinder was filled up to the top with the water that was inside the tub. The top of the cylinder was held shut with one hand while carefully at the same time the graduated cylinder was inverted, facing upside down in the water tub. This was done, so that the water that was captured didn’t leak out into the tub. One group member held the inverted cylinder inside the tub the whole time so that it wouldn’t tip over. 10 mL’s of Hydrogen peroxide was kept separate in a small graduated cylinder before it was mixed with catalase. The 10 mL’s of hydrogen peroxide (H2O2), was poured into an Erlenmeyer flask. Then, one end of a black tube was placed inside the inverted graduated cylinder from the bottom that …show more content…
There was a cold water bath with ice to measure cold temperatures and a hot water bath to measure hot temperatures. The cold water bath was measured with a thermometer so that the temperature would be at 0 degrees Celsius for the first trial. Then, the Erlenmeyer flask containing the 10 mL’s of hydrogen peroxide was placed into the cold water bath that was measured 0 degrees Celsius. (This was repeated for each temperature for both the hot and cold water baths). After waiting a couple minutes for the flask to reach the desired temperature (which was 0 for this trial), a syringe was used to take 1mL of catalase and it was put into the flask that contained the 10 mL’s of hydrogen peroxide. 1mL of catalase (labeled liver extract) was injected into the Erlenmeyer flask with 10 mL’s of H2O2. The syringe was kept inside. Right after the 1 mL of catalase was injected into the 10mls of H2O2, the flask was swirled continuously. Then, it was observed if the reaction produced any O2 gas and was recorded in the data table. Each minute, the amount of O2 produced was
The preparation for the experiment started by gathering the solutions of enzyme Peroxidase, substrate hydrogen peroxide, the indicator guaiacol and distilled water. Two small spectrometer tubes and three large test tubes with numbered labels. In addition, one test tube rack, one pipet pump and a box of kimwipes were also gathered. Before the experiment, the spectrometer must be set up to use by flipping the power switch to on. Following, the machine was warmed up for 10 minutes and the filter lever was moved to the left. In addition, I set the wavelength to 500 nm with the wavelength control knob. Before the experiment, I had to create the blank solution by pipetting 0.1 ml of guaiacol, 1.0 ml of turnip extract and 8.9 ml water into tube #1. Following the creation of the blank, a control 2% solution was created.
This is an experiment to examine how the concentration of the substrate hydrogen peroxide affects the rate of reaction of the enzyme catalase.
The experiment was both a controlled experiment and interpretation of data because we used the data to interpret the enzyme activity and had controlled variables for comparisons. The materials used to conduct this experiment included: acids (vinegar and hydrochloric acid), base (sodium hydroxide), catalase solution (potato puree), flasks, beakers, granulated cylinder, temperature measuring device, ruler and test tubes. After getting the materials, we started on changing the pH levels by adding vinegar, hydrochloric acid or sodium hydroxide to the catalase before the adjusting the temperatures. When we began to add the drops, we started with 3 test tubes with different amount of drops in the solution: 3 drops, 4 drops, and 5 drops. We added 3, 4, and 5 drops to the solution because we needed a range of
The data from the experiment supports the hypothesis that catalase functions the most efficiently at a neutral pH of 7. Table 1 shows that catalase helped consume 3 mL of hydrogen peroxide in the solution with a pH of 7, more than any other solution. As the pH
We used apple, potato, and chicken liver to prove that not only beef liver contains catalase. The group conducted three experiments: one contained potato and H2O2, another had apple and H2O2, and the last had chicken liver and H2O2. We added 2mL of hydrogen peroxide (H2O2) to all three test tubes. The bubbling effect proved that all three had catalase in them. We realized that the more the substance bubbled the more catalase it contained, and that the less it bubbled, the less catalase there was. We also rated the reactions by the speed of the reaction in seconds, like we learned in part
For the experiment, the enzyme Catalase was used at varied temperatures to measure oxygen produced by the breakdown of H2O2. Most enzymes are specialized molecules of protein that have a specific structure to them. They are catalysts in metabolic activity. Being that they are made from proteins, the shape comes from the folding or condensing of the long strands of amino acids. These polypeptides fold from primary, to a secondary, then tertiary structure.
Catalase Experiment In many cases, the body needs a way to break down proteins, enzymes, and even poisons. In this case our main goal within this experiment was to break down hydrogen peroxide. When you add an enzyme called, catalase, and it will break hydrogen peroxide down into water and oxygen gas. As the lab went on we were trying to test the activity between catalase and hydrogen peroxide (the action of the enzyme in the environment).
Results: The results of the experiment were there that the catalase affected the rate of hydrogen peroxide breakdown. Without the presence of the enzyme no reaction would have occurred. Our control for this experiment was the amount of buffer added each time (4.0 ml) and the amount of water added during each run with a different pH level. The purpose of the controlled substances was to determine whether or not the catalase really influenced the rate of oxygen production.
Objective: This lab was performed to help students understand what enzymes do, what they are, and how they are effected by temperature, pH, and concentration. This lab write up only contains information based on the temperature portion of the lab. Introduction: In lab 5; enzyme activity, yeast solution was used as an enzyme to test the rate that oxygen was produced.
We did this by placing 20 mL of 0.3% hydrogen peroxide into a small test tube. Once this had been completed, 1mL of diluted catalase was placed into the small test tube. Quickly, we placed a large test tube over it and inverted the tubes, then measured the amount of oxygen immediately. This experiment included the mean, standard deviation and three t-tests set at
This study attempts to find how H2O2, H2SO4¬, and KMnO¬¬4 react together to tell how catalase will catalyze H2O2 over time. The way that H2O2 breaks down is illustrated by 2 H2O2 2 H2O + O2 (Campbell, 2008). In the absence of catalase, this happens extremely slowly. In the presence of catalase, the reaction speeds up and can be stopped by using H2SO4¬ to measure the amount of hydrogen peroxide used over time. To measure the quantity used up over a specific time interval, potassium permanganate (KMnO¬¬4) is added to the solution to essentially “eat up” the leftover hydrogen peroxide from the reactions with the
A 0-5 rating scale was used to compare the reaction of catalase and hydrogen peroxide in different conditions. A 0 is no reaction, 1 is very little or slow reaction, and 5 is a very fast reaction.
Introduction: Throughout the coarse of the lab experiment the decomposition of hydrogen peroxide (H2O2) was done using catalase (an enzyme usually found in living organisms like yeast). The yeast acted as the substance that speeds up the decomposition of the reactants in H2O2 without changing its mass (not undergoing permanent change). Hydrogen peroxide is a complex compound that is commonly found in reaction that involve living organisms/cells, the function of the catalyst, otherwise known as yeast in this is experiment, with it catalase enzyme is to break down the compound H2O2 into smaller molecules of H2O (water) and O2 (oxygen). The enzyme catalase is built and shaped to allow the break down and decomposition of H2O2 to occur. Yeast
The enzyme that will be used in this experiment is catalase which can be found in animal or plant cells. The substrate that will be catalyzed by catalase is hydrogen peroxide (H2O2), toxic product in most living organisms. The catalase enzyme will catalyze the hydrolysis reaction of hydrogen peroxide into oxygen and water
I knew that the catalase was working, because it was evident that it was speeding up the chemical reaction of the hydrogen peroxide. The decomposition reaction of hydrogen peroxide into products water and oxygen occured very quickly as soon as the enzyme for hydrogen peroxide (catalase) was added into the graduated cylinder with the hydrogen peroxide. As a result, an increasing amount of foam was being produced; a mixture of the products water and oxygen. Catalase speeds up chemical reactions by lowering the activation energy required to initiate the chemical reaction. Therefore, after adding catalase to the substrate that needed to be broken down into it’s products, the reaction’s activation energy was lowered, and it did not need as much