An Explanation Of The Activity Of A Catalase

Its role as an enzyme is to quickly break down hydrogen peroxide (H2O2) into water and oxygen, preventing cellular damages. H2O2 is produced as a harmful by-product in all organisms that use molecular oxygen, so catalase is especially abundant in liver cells of humans and other organisms, because the liver is an organ that detoxifies many harmful substances including peroxides (Lab Manual). The catalase and hydrogen peroxide reaction process is as seen as below:

Catalase is an important enzyme that protects cells from oxidative damage, which hydrogen peroxide can cause. It is an incredibly efficient enzyme where one catalase molecule can convert millions of hydrogen peroxide molecules each second.

An Investigation on the rate of reaction of the enzyme Catalase on the substrate Hydrogen peroxide.

If another enzyme like lactase is used, no reaction would take place because the substrate, hydrogen peroxide, wouldn’t fit into the active site.

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

An Enzyme is a protein that in essence speeds up biological reactions. So that would mean that a Catalase is an enzyme reaction that decomposes hydrogen peroxide to water and oxygen. It is primarily found in the liver and it is important in protecting the cell from damaging oxidative reactions.

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.

Its function is the speed up the decomposition of Hydrogen peroxide within cells. This is an important function within living animals because it becomes a poisonous substance. Catalase breaks apart hydrogen peroxide into water and oxygen through enzyme-substrate complexes. (Tully) The shape of catalase is complex with various alpha-helices and beta-sheets.

Five different temperatures of enzyme (spinach extract) (5°C, 20°C, 35°C, 45°C and 65°C) were added to individual measuring cylinders -each filled with 7ml of Hydrogen Peroxide (H202). The height of foam (oxygen + water) produced by the reaction was recorded for each temperature of the catalase after 30 seconds, to find at which degrees the enzyme activity had the fastest reaction rate. The data collected from this experiment suggested that the enzyme extract had the greatest efficiency at 20 °C, and the temperatures greater displayed a decline in rate of reaction.

Enzymes are proteins that catalyze (speed up) biological reactions in an organism by lowering the activation energy of a reaction. They do this by either straining the bonds in a molecule so that is easier to break up or by placing separate molecules/elements close to each other so that bonds are formed. Enzyme activity is influenced by an array of different factors such as enzyme concentration, substrate concentration, temperature, pH and inhibitor concentration. All of these affect the rate of reactions of enzymes and some such as temperature, inhibitors and pH can under circumstances cause enzymes to become permanently affected. Catalase is an enzyme found in almost all organisms on earth exposed to Oxygen.

The oxidation reaction completed in this experiment included the enzyme catalase breaking down hydrogen peroxide. The primary function of Catalase is to break down hydrogen peroxide into water and oxygen gas. Methods/Materials

Introduction: Enzymes are proteins that are used to catalyze a chemical reaction by reducing the activation energy necessary for the reaction to take place. Enzymes are highly specific to a particular substrate and function best at optimal pH ranges and temperatures (Bursal, 2013). Peroxidase is an enzyme which can be found in many plants and animals, such as horseradish and humans. The main function of peroxidase is to breakdown hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2) (Groves and Boaz, 2014). A catalytic process is used by peroxidase to breakdown H2O2 which can be harmful to an organism (Zazza et al., 2009). The purpose of this experiment was to test the functionality and efficiency of peroxidase at various pH values to determine the optimal pH of the enzyme. The hypothesis was that peroxidase would perform optimally at a slightly basic pH and

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.

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.