Catalase Lab Report

The scientific purpose of this experiment was to examine the rate of enzyme activity of a potato catalase when mixing 2.5 ml of potato catalyst with either 2.5 ml of H2O, 2.5 ml of 5% salt concentration, 2.5 ml of 15% salt concentration, or 2.5 ml of 30% salt concentration. It was hypothesized that the higher the concentration of salt each catalysts solution contained, the rate of enzyme activity would decrease when applied to hydrogen peroxide. This was tested by measuring (up to 240 seconds) in room temperature of 21 degrees Celsius how long it would take for each filter disk (dosed with the various salt and potato catalase solutions) to float off of the bottom of the beaker that contained hydrogen peroxide. The results of the experiment showed that enzyme activity decreased with higher salt concentrations, that being in tube four (which contained 2.5 ml of potato catalase and 2.5 ml of 30% of salt concentration) all four filter paper disks did not float within the 240 second range, having 240 seconds become the mean and 0 becoming the standard

The liver and the hydrogen peroxide or H2O2 reacted through hydrolysis. The hydrogen peroxide or H2O2 was separated by taking out the water that bonded it. The gas that was produced was O2 or oxygen. One can tell that O2 or oxygen was produced because it the only gas the supported burning. When the class did the demo, the splint stayed lit in the test tube, proving that oxygen was present. The liquid that was left behind was H2O better known as water. When hydrolysis took out the oxygen in the bond, the only thing that was left was H2O2.

The goal of this lab was to find the effect of different substrate concentrations of hydrogen peroxide on the rate of catalase enzyme activity. This experiment was specifically meant to find a correlation between an increasing substrate concentration of hydrogen peroxide on the rate of catalase enzyme activity. Four test tubes were used, one filled with 5 milliliters of water and three with 5 milliliters of different concentration of hydrogen peroxide ranging from 0.5%, 1%, and 1.5%. Four drops of yeast solution were dropped into each test tube using a pipette. Then, a lab quest probe was attached to each of the test tubes. The test tubes were tapped twice every second in order to agitate the solution. The rates of the catalase enzyme activities were recorded after 400 seconds of tapping. After the lab, all the materials were cleaned. This experiment was repeated the next day. After both trials were completed, the average from the two trials was taken. Then, the data from the experiment was graphed, with the different substrate concentrations of hydrogen peroxide recorded on the x-axis and the average rates of catalase enzyme activity in kilopascals per second recorded on the y-axis. The experiment results showed that there was a positive correlation

Problem/Info: Enzymes are large protein structures, also known as macromolecules and catalysts. They aid in the acceleration of chemical reactions by binding to another substance known as a substrate, converting it into different products that are more easily broken down called products. Only a small portion of the enzyme actually aids in catalyzing the substrate: the active site. When an enzyme is in specific conditions they tend to react quicker while in other, generally extreme, conditions the enzyme can be broken apart and rendered unusable, this is called denaturation. In the experiments conducted, an enzyme known as catalase, generally found in yeast, will be soaked onto a tiny paper circle and dropped into hydrogen peroxide H2O2. The catalase will break the hydrogen peroxide into oxygen and water. The oxygen inside of the paper will eventually be in a quantity that causes the paper to rise to the top of the hydrogen peroxide. The entire experiment is based off of observations of this piece of paper.

It catalyses the hydrogen peroxide to oxygen and water, such as this formula: 2H2O2→O2+2H2O However, the effects of catalase is influenced by the substrate concentration. The different levels of the concentration will lead to different results of oxygen produced off the Hydrogen peroxide, Increasing the substrate concentration will increase the amount of the oxygen produced. Investigation Question: How Does increasing the concentration of Hydrogen Peroxide affect the amount of oxygen formed?

The purpose for the Catalase Lab Experiment to have figured out if Hydrogen Peroxide could be broken down by catalyst found in and not in a living system.

Observe and record what happens when enzymes (chicken) are added to different amounts of acid (hydrogen peroxide) mixed with water. The activity level of these enzymes will differ and be dependent upon several factors, such as consistency, size and shape of the molecule. Specific factor will be the concentration enzyme and substrate. I will conduct a controlled experiment to determine the influence of pH on the enzyme catalase and the release of oxygen.

The hypothesis stated that if we decrease the amount of hydrogen peroxide then the amount of production of oxygen would decrease as well because the yeast, the catalyst that contains the catalase enzyme, will speed up the decomposition process of H2O2. As we increase the amount of H2O2, the moles of oxygen increase as well, and vice versa, as they are proportionate. In this experiment when 5mL of H2O2 was used it produced an average of 1.70 x10-3 moles of O2 and when 4mL of H2O2 was used it produced an average of 1.90 x10-4 moles of O2 displaying the increase in oxygen production as H2O2 increases. According to the New Mexico Institute of Mining and Technology, the compound of Hydrogen Peroxide will always in its usual state decompose into water and oxygen, but the Institute also adds that it would take a longer amount of time to do so. This is when the yeast fulfills its role as the catalyst with the active enzyme catalase to activate the reaction of the reactants and speed up the process of the reaction to break down the compound H2O2 into molecules of H2O and O2.

In this experiment, the enzyme that was investigated was catalase. It was extracted from celery tissue and introduced to different temperature and different pH and observed its activity. Catalase is one of the most effective enzyme known and it is found in all living organisms. Catalase is so efficient that it cannot be saturated by hydrogen peroxide at any concentration (Matés,

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

In this experiment, the effect of various pH conditions on catalase enzyme activity was observed. For the enzyme-substrate complex of this experiment, hydrogen peroxide, H2O2, is the substrate and the enzyme is catalase, which is secreted by yeast. 3mL of a pH buffer, available in pH 4, 7 and 10, was added to an equal amount of 3% hydrogen peroxide, H2O2. Then, to each of these three solutions, three drops of yeast that has been activated with warm water was added to catalyze this reaction. As the yeast secretes more and more catalase, the rate of reaction increases considerably and hydrogen peroxide is broken down into water and oxygen gas (H2O2⟶ H2O+O2(g)). As this reaction occurs, the test tubes began to warm up since this is an exothermic reaction and bubbles started to form due to the formation of oxygen gas. The program Logger Pro and a gas pressure sensor were used to measure the production of oxygen gas as hydrogen peroxide is destroyed by the enzyme catalase at various enzyme concentrations.

Hydrogen peroxide (H2O2) decomposes to water (H2O) and oxygen O2. The chemical reaction H2O2  H2O + O2 will be (Ferguson 2015). A conversion of O2 the final acceptor of the reduction oxidation reaction completed. The rate of chemical reaction is measured the O2 and substrate which is the H2O2. The effects of temperature is strongly affected on the rate of reaction.

The objective of the experiment is to measure and compare the enzyme activity (the enzyme Catalase which is extracted from chicken liver) and the factors that speed up the enzyme action such as concentration of the enzyme, temperature, and pH. This experiment was also used measure the production of oxygen gas using a fermentation vial as it reduces hydrogen peroxide. If the peroxide is destroyed within the experiment, there is a lesser amount available to have a reaction while the oxygen is produced at a lower rate. With that in mind, if there isn't any hydrogen peroxide left; oxygen is no longer created.

Combustion is a complex chemical process in which a substance reacts rapidly with oxygen accompanied by the production of heat. (Grc.nasa.gov, 2015). The original substance is called the fuel and the oxygen is called the oxidizer. Along with heat, CO2 (carbon dioxide) and H2O (water) are created as byproducts of the exothermic reaction. ( E-inst.com 2015).

Enzymes are organic catalysts and can speed up chemical reactions. Two molecules of hydrogen peroxide are broken down into two molecules of water and a molecule of oxygen gas. Both water and oxygen are harmless to cells and therefore, the presence of catalase allows cells to break down the toxic substance hydrogen peroxide before cells become poisoned. The mechanism is that the enzyme bind to the substrate at the active site.