Enzyme Catalase Lab Report

Students will label 3 test tubes hot, cold, and room temperature and place potato cub (3X3X3 cm)

The purpose of this experiment was to simply measure oxygen production rates released from decomposed hydrogen peroxide under different conditions (concentration of enzymes, temperature, and PH level).

1. We measured 2 mL of diluted hydrogen peroxide (the substrate), 1 mL of guaiacol (the product indicator), and 1 mL of neutral buffer (pH 7) with a syringe and disposed it into tubes 1, 2 , 4, 9, 11, and 12.

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.

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

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 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.

Purpose To investigate how changes in the acidic pH level of an HCl solution will affect the rate at which the catalase enzyme will break down hydrogen peroxide into its products, oxygen and water. Hypothesis If the pH of the solution is related to the reaction rate of catalase, then changing the acidity of the environment will affect the decomposition rate of hydrogen peroxide because catalase has an optimal pH level at which it functions best. Since catalase is found throughout the human body (and highly concentrated in the liver), it is expected that the optimal pH of catalase will be similar to the pH of a human liver, which is maintained around 7 (neutral) (Science Buddies, 2012).

The objective of this experiment was to determine how different pH values and temperature affect the enzyme activity of peroxidase. Hydrogen peroxide is a byproduct of metabolic feedback in majority of the living organisms. However,hydrogen peroxide is harming to molecules in the cells. Subsequently,nearly every organism produce the enzyme peroxidase,which breaks down hydrogen peroxide as it is formed. Peroxidase can be obtained from from potatoes.

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

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.

Based on the prompt above, “You will design a lab to see if the enzyme Catalase (Peroxidase) can be denatured” we devised a hypothesis that states if you expose the Catalase to a pH that is not within its optimal working range, such as a pH of 2 and a pH of 12, the Catalase will denature because the catalase will only work in its optimal range that which is a pH of 7 (“PH Levels of Catalase.” 2017). The hypothesis that we have come up with proved to be incorrect 66% of the time as 2 out of the 3 trials above showed a reaction when we mixed the hydrogen peroxide with the Catalase. Although our results and observation states that 66% of the time Catalase and hydrogen peroxide has a reaction even when exposed to the different levels of pH, there

Testing the Effects of Temperature on the Decomposition of Hydrogen Peroxide with 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.