Catalase And Hydrogen Peroxide Lab Report

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.

Put the 100 g of potato in 1 petri dish and 100 g of liver in another petri dish. Then put equal amounts of hydrogen peroxide for an equal period of time in both dishes. Drain the dishes and titrate them with potassium permanganate simultaneously. The numbers can now be compared using the steps in the sample calculation above in the lab report. In order to compare perform a potassium permanganate titration on pure hydrogen peroxide.

In the experiment we used Turnip, Hydrogen Peroxide, Distilled Water, and Guaiacol as my substances. On the first activity, Effect of Enzyme concentration of Reaction Rate for low enzyme concentration, we tested three concentrations of the turnip extract, and hydrogen peroxide. For the Turnip Extract I used 0.5 ml, 1.0 ml, and 2.0 ml. For hydrogen peroxide we used 0.1 ml, 0.2 ml, and 0.4 ml. We used a control to see the standard, and used a control for each enzyme concentration used. The control contains turnip extract and the color reagent, Guaiacol. We prepared my substrate tubes separately from the enzyme tubes. My substrate tube

The topic of this lab is on biochemistry.This experiment was conducted to show how cells prevent the build of hydrogen peroxide in tissues. My group consisted of Lekha, Ruth, and Jason. There were used two different concentrations of hydrogen peroxide through this experiment , 1.5% and 3%. By testing two different types it is easier to understand how the H2O2 and catalase react with one another. To do this both the yeast, which was our catalase, and H2O2 were mixed together in a beaker. Each concentration was tested out twice for more accurate results . 1.5% concentrated H2O2 had an average reaction rate of 10.5 seconds while 3% concentrated H2O2 had an average reaction rate of 7.5 seconds. From this experiment we learned that by increasing the concentration of H2O2 and chemically combining it with a catalase it will speed up the reaction. Enzymes speed up chemical reactions . The independent variable in this experiment was the concentration of the H2O2. Some key vocabulary words are Catalase, enzyme, hydrogen peroxide ( H2O2), and concentration.

Students will place a potato cube into a test tube and add 3 ml of H202 into each tube. Then students will wait one minute and record the height in cm of the bubbles and rate how rapidly the solution bubbles on a scale of 0-5. (0=no reaction, 1=slow,……. 5= very fast.)

This investigation will be carried out to investigate the rate of reaction of the enzyme catalase on the substrate hydrogen peroxide.

There were three test tubes in which the experiment was held. A relatively equal sized portion of raw potato (this contained the enzyme [a biological catalyst] hydrogen peroxidase) was placed in each tube. Then, enough water to cover the potato was added. Proceeding this, each of the test tubes were assigned a temperature; cold, room temperature or warm (this was written on the tag so that they were not confused). The test tube destinated ‘cold’ was placed in a ice bath for five minutes. At the same time, the ‘hot’ test tube was placed in a hot water bath for five minutes. Meanwhile, the room temperature test tube sat at room temperature for five minutes. When the five minutes were over, the test tubes were returned to the rack (so that they were able to be observed). Then, the test tubes were allowed to sit at room temperature for five more minutes. Once that period of time was over, 2 ml of hydrogen peroxide (the substrate) was added to each tube.

Our team was given the temperature of 37 degrees celsius. For this experiment we will be looking for any bubbles and measuring air change in a submerged cylinder. Our hypothesis stated: “At 37 degrees celsius the enzyme would have affected the catalase

The first part of the experiment measured the effects temperature has on the enzyme activity. Our hypothesis for part one is that peroxidase activity is affected by temperature. One can predict that if the temperature of the environment around the enzyme increases, then the enzyme activity will increase. With that being said, there is an optimal temperature for peroxidase, so at some point the peroxidase will decrease in activity once it exceeds it’s optimal temperature. The second part of the experiment measured the effects of inhibition and how it influenced enzyme activity. A hypothesis for part two would be that peroxidase activity is affected by an addition of an inhibitor. If hydroxylamine is added to the reaction mixture, then the breakdown of hydrogen peroxide will decrease. Since hydroxylamine is an inhibitor, one can predict that the rate of peroxidase activity will decrease and the hydrogen peroxide concentration in the mixture will be much

The purpose of this experiment is to learn the effects of a certain enzyme (Peroxidase) concentration, to figure out the temperature and pH effects on Peroxidase activity and the effect of an inhibitor. The procedure includes using pH5, H202, Enzyme Extract, and Guaiacol and calibrating a spectrophotometer to determine the effect of enzyme concentration. As the experiment continues, the same reagents are used with the spectrophotometer to determine the temperature and pH effects on Peroxidase activity. Lastly, to determine the effect of an inhibitor on Peroxidase, an inhibitor is added to the extract. It was found that an increase in enzyme concentration also caused an increase in the reaction rate. The reaction rate of peroxidase increases at 40oC. Peroxidase performed the best under pH5 and declined as it became more basic. The inhibitor (Hydroxy-lamine) caused a decline in the reaction rate. The significance of this experiment is to find the optimal living conditions for Peroxidase. This enzyme is vital because it gets rid of hydrogen peroxide, which is toxic to living environments.

The chemical hydrogen peroxide(H₂O₂) is broken down by the enzyme catalase. Hydrogen peroxide is a byproduct formed in cellular reactions that, if not broken down, could inflict severe damage to the cell. Catalase is an enzyme that breaks down hydrogen peroxide in to water and oxygen. How efficient and strong the enzymes reaction to break down H₂O₂ determines largely on temperature and pH level. An enzyme only functions within a set pH and temperature range. Beyond that it becomes denatured, rendering it useless. The purpose of this lab is to determine at which temperature and pH level the enzyme catalase reacts best. Catalase in chicken and beef livers will be used to do the lab because enzymes still function after death as long as they are kept refrigerated at a low temperature.

This experiment is designed to analyze how the enzyme catalase activity is affected by the pH levels. The experiment has also been designed to outline all of the directions and the ways by which the observation can be made clearly and accurately. Yeast, will be used as the enzyme and hydrogen peroxide will be used as a substrate. This experiment will be used to determine the effects of the concentration of the hydrogen peroxide versus the rate of reaction of the enzyme catalase.

To find the effect of temperature on the activity of an enzyme, the experiment deals with the steps as follows. First, 3 mL if pH 7 phosphate buffer was used to fill three different test tubes that were labeled 10, 24, and 50. These three test tubes were set in three different temperature settings. The first test tube was placed in an ice-water bath for ten minutes until it reached a temperature of 2° C or less. The second tube’s temperature setting was at room temperature until a temperature of 21°C was reached. The third tube was placed in a beaker of warm-water until the contents of the beaker reached a temperature setting of 60° C. There were four more test tubes that were included in the procedure. Two of the test tubes contained potato juice were one was put in ice and the other was placed in warm-water. The other two test tubes contained catechol. One test tube was put in ice and the other in warm water. After

The experiment that the class worked on was about peroxidase. Peroxidase is part of the enzyme group that presents most living organisms (Ahmed, 2013). Peroxidase interferes with the removal of hydrogen peroxide (Ahmed, 2013). Hydrogen peroxide is a toxic product that have normal metabolism before it causes any cell damages (Ahmed, 2013). Peroxidase has two substrate and both of them must present a reaction (Ahmed, 2013). One of the two substrate is H2O2 and other one just depends on the organism or the cell type (Ahmed, 2013). The substrate that the class uses is turnip extract. In the class there were five experiments to do but the class were assigned into groups and each group were going to do two experiment. The names of the experiments are: Baseline, Temperature, and pH.

Hydrogen peroxide is a toxic byproduct of cellular functions. To maintain hydrogen peroxide levels the catalase enzyme deconstructs hydrogen peroxide and reconstructs the reactants into oxygen gas and water. The catalase enzyme is found inside cells of most plants and animals. Regulating the levels of hydrogen peroxide is crucial in homeostasis and analyzing it’s optimal conditions for performance is just as important. To understand the optimal environment for this enzyme, they are put into different environments based off protein activity (enzymes are proteins). Catalase samples will be put into different hydrogen peroxide environments based off pH and temperature. The more active the enzyme, the more oxygen and water it will produce. Enzyme activity can be seen through the release of oxygen in the hydrogen peroxide. Since oxygen cannot be accurately measured, the data will consist of the longevity of the reaction in different environments. If the pH is higher than 7, then the reaction rate will increase due to the ample amount of hydrogen ions in the hydrogen peroxide. However the pH level cannot be higher than 10 or else there will be too many hydrogen atoms in the peroxide for the enzyme to be able to deconstruct them. If the temperature is increased, then the reaction rate will increase due to the ample amount of energy and movement in the hydrogen peroxide and enzyme.