Catalase Lab Report

This experiment looked at how substrate concentration can affect enzyme activity. In this case the substrate was hydrogen peroxide and the enzyme was catalase. Pieces of meat providing the catalase were added to increasing concentrations of hydrogen peroxide in order to measure the effect of hydrogen peroxide concentrations on the enzyme’s activity. The variable measured was oxygen produced, as water would be too difficult to measure with basic equipment.

The human body is an incredible system that is capable of working a multitude of diverse functions. Without the help of the many different protein molecules, the human body would not be able to function properly. One major group of proteins called enzymes are mandatory for essential life. These proteins are constantly at work assembling molecules, metabolizing energy, and fighting off infections. An enzyme is a macromolecule that acts as a catalyst that speeds up a chemical reaction without being consumed by the reaction. Without these proteins, these reactions would take place too slowly to keep us alive. Essential parts in your body like vitamins and minerals cannot do any work without

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

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

In order to see the effects of pH and temperature on the enzymatic reaction of catechol oxidase when separated from potato tissue. We used a spectrophotometer to measure how much blue light energy is absorbed by benzoquinone. Benzoquinone is a product of catechol when it has been oxidized by different temperatures and pHs. We hypothesized that the benzoquinone absorbance rate would be faster when the pH added to the cuvettes were greater than the pH of the potato tissue. The pH of the potato tissue was pH 6. Our results show that pH 7 had the faster absorbance rate, slightly slower at pH 4, and slowest at pH

The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,

The differences for the rates of reaction between the liver and potato are accounted for because liver contains more catalase enzymes than potatoes. This is because the liver is responsible for ridding toxins out of the body and as a result needs more catalase enzymes to do so; explaining the bigger reaction it had with the hydrogen peroxide.

Objective: Measure the rate of decomposition of hydrogen peroxide with and without the addition of an enzyme catalase at different time intervals.

There were few changes made in the follow up inquiry experiment, which changed the peroxidase enzyme extract from turnip, to potato. Discussion: This lab experiment related back to chapter eight, with metabolic processes with enzymes. That chapter discussed metabolism, the structure and shapes of enzymes, and their many functions. The main one being speeding up chemical reactions, which is what happened in this lab.

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.

Discussion: The purpose of this experiment was to observe what the normal enzyme1 (proteins that catalyze chemical reactions) activity of beef liver catalase was, and to measure the effects of extreme changes in temperature and pH on the beef liver catalase function. We also observed what the bromelain1 (proteins in pineapple) activity was in a fresh pineapple compared to canned pineapple. Enzymes are present in all living things.1 These specialized proteins speed up chemical reactions fast enough to sustain life.1 This lab was driven by the question; if there is an extreme change in temperature or pH on an enzyme catalase, or a bromelain enzyme, then that catalase or bromelain will be affected or denatured.

The purpose of this lab was to identify a skin-associated microbe from two skin regions of the body (moist/oily and dry). Based on the results from Figure 1, the moist/oily region (ear) was the only region to exhibit growth on the PEA plate. In addition, in Figure 2, the morphology of the moist/oily microbe appeared to be cocci from the Gram Stain. Since the morphology was cocci, the Catalase test was performed. In Table 1, the results from the Catalase test were negative.

After conducting the experiment in Part A, the results were the same as the hypothesis that as the number of disks increases the enzyme activity also, proportionally increase simultaneously shown clearly in figure achieved. When three disks were utilized, increasing the enzyme concentration enabling the molecules to collide with more hydrogen peroxide substrate molecules decomposing at a faster rate enabling more product to be formed. It can be seen that the Vmax approximately occurs at 230 kpa, indicating that

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.

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.