Analyzing The Biochemical Reactions Caused By A Catalyst And An Enzyme That Break Down Hydrogen Peroxide

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.

The rate of reaction between Catalase and the hydrogen peroxide (H2O2) can vary depending on many factors including the enzyme concentration in a solution. In this investigation, the rate of reaction will be measured by the change in temperature of the liquefied spinach (catalase) over a period of 30 seconds, once the hydrogen peroxide (H2O2) has been added into the solution.

Hydrate the yeast packets in a beaker with 400 mL of distilled water at a 10% concentration. In a 50 mL

In the first part of the enzyme lab, we mixed a substrate and an indicator with an enzyme. There was also a neutral buffer in each of the chemical mixtures. The neutral buffer regulated the pH to around 7. We got a color palette and once we mixed each together, we observed and saw a change in the color of the substance. The darker and more brown the substance got, the more oxygen produced by the reaction. Our results showed that amount of oxygen produced increased about 10% a minute until it sort of equilibrated at 4 minutes and didn’t change to the fifth minute mark. If we were to change anything we did in the experiment, we would make our comparisons to the chart more precise. Overall we thought it

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.

In this week’s lab experiment, the rate of decomposition of hydrogen peroxide forming oxygen gas will be observed and studied. Since the rate of a chemical reaction is dependent on two things; the concentrations of the reactants and the temperature at which the process is performed, the rate can be measured at which a reactant disappears or at which a product appears. When measuring the rate, the rate law will be applied. The objective of this lab is to demonstrate how the rate changes with varying initial concentrations of hydrogen peroxide by measuring the rate at which oxygen is evolved.

Peroxidase is an enzyme found in potatoes that catalyzes the breakdown of hydrogen peroxide, H2O2, into O2 gas and water. We examined the different pH environments that can affect the enzyme activity during the breakdown of H2O2. In order to do this, we added different levels of pH, low, medium, and high, into different test tubes with the enzyme and H2O2, and we then inverted the tube. The amount of O2 gas produced was then measured and recorded. The result was that the higher pH produced more gas, followed by medium pH, then low pH. The enzymes were more active in the pH of about 10. It increased

In order to be an enzyme, it must be made out of protein. Since MnO2 is not a protein, it cannot be an enzyme, but it is still a catalyst for this reaction. All MnO2 did in this reaction was serve as a catalyst, but that does not mean it has the biological components to be an enzyme.

The purpose of this investigation is to discover the effect of pH on the activity of catalase, an enzyme which plays the integral role of converting hydrogen peroxide into water and oxygen, and discover which pH level it will work at the most efficient rate (the optimum). The original hypothesis states that that the optimum would be at a pH is 7, due to the liver, where catalase usually resides, being neutral. The experiment consists of introducing the catalase to hydrogen peroxide, after exposure to certain solutions; hydrogen peroxide, water and hydrochloric acids, all containing the adjusted pH, and measuring the height of froth formed, an observable representation of the activity of the enzyme. The final data indicated that

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

Part A was just a beginning. The experiment showed us what a normal catalase reaction really is. We had one basic procedure; observe what happens when you add hydrogen peroxide to beef liver. At first we were just amazed by the bubbling product, we did not realize that a chemical reaction was going on. We had to redo the experiment so we could note that heat was being released as well as a combination of harmless gasses. We timed the reaction and learned to estimate the reaction rates by the time. We descovered that the bubbles were actually two main gasses, 2H2O and O2. They were being released due to the break down of a harmful gas H2O2. Another experiment we did was testing if catalase was reusable. We discovered that it was, in fact, reusable. The basics of a normal catalase reaction is what we learned about part A. Everything kept growing more and more into depth with our experiments as we went on during our lab.

The research and observations of this lab primarily focused on the enzyme activity of the enzyme Peroxidase. Peroxidase is a large protein and is composed of more than three hundred amino acids. The enzyme was selected as it is easy to experiment with and effectively showcases the effects of varying independent variables, such as pH and temperature. Peroxidase catalyzes the decomposition reaction of the chemical Hydrogen Peroxide ( H2 O2 ) into water and an electron donating molecule, which stands for R in the written chemical equation. ( The equation is displayed below:

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.

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.