Catalase Lab

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.

Students will be observing normal catalase reaction, the effect of temperature on enzyme activity, and the effect of pH on enzyme activity in this experiment. The enzymes will all around perform better when exposed in room temperature than when it is exposed to hot and cold temperatures. This is based on the fact that the higher the temperature, the better the enzymes will perform, but as the temperature reaches a certain high degree, the enzymes will start to denature, or lose their function.

If different amounts of enzyme solution are added to the hydrogen peroxide, then the highest amount of enzymes will have the greatest reaction rate because enzymes catalyze reactions, meaning more oxygen will be produced quicker.

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,

Since enzymes are proteins, they are subject to denaturation at high temperatures. Catalase is an enzyme present in the human liver and functions at an optimum of 37°C. The data from the 36.7° C recording on table 1 proves this fact to be true. Any increase after 37°C will result in the denaturation of catalase, resulting in it becoming ineffective in the hydrolysis of hydrogen peroxide (“What is the Role of Catalase,” 2017). However, even after reaching boiling point a reaction, albeit small, still occurred. The reason for this reaction can be explained by the second law of thermodynamics. This law states that “during any process, the universe tends towards disorder [entropy]” (Carter Edwards et al, 2011). Living systems, are the exception to that law because they utilize energy in order to decrease entropy. In addition, the kinetic molecular theory of matter states that as temperature increases so does kinetic energy, or energy in motion (“The Kinetic Molecular Theory”). Thus, by increasing the kinetic energy of a reaction through an increase in temperature, the activation energy of a reaction will be decreased, and consequently the reaction rate will increase. So although the catalase may have been denatured, or almost fully denatured, a reaction was still possible due to the kinetic energy provided by the drastic increase in temperature.

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

Substrate concentration also affects the rate of reaction as the greater the substrate concentration the faster the rate of reaction and all the active sites are filled. At this point the rate of reaction can only be increased if you add more enzymes in to make more active sites available.

We used apple, potato, and chicken liver to prove that not only beef liver contains catalase. The group conducted three experiments: one contained potato and H2O2, another had apple and H2O2, and the last had chicken liver and H2O2. We added 2mL of hydrogen peroxide (H2O2) to all three test tubes. The bubbling effect proved that all three had catalase in them. We realized that the more the substance bubbled the more catalase it contained, and that the less it bubbled, the less catalase there was. We also rated the reactions by the speed of the reaction in seconds, like we learned in part

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

If the temperature is too hot or too cold, then the reactivity and reaction rate of which the enzyme catalase breaks down hydrogen peroxide will decrease.

However extreme temperatures, for example, boiling water, will result in inconclusive data with no effect on the reaction rate. The purpose of this experiment is to measure the reaction rate of the catalase when interacting with different temperatures and substrate concentrations. This is significant because we can test and compare the timings of different factors that will affect the catalase reaction rate

The enzyme is found in high gear assiduity in a organelle in cellular telephone called the peroxisome. One of the functions of catalase is to prevent a toxic accumulation of hydrogen hydrogen peroxide (H2O2) in cells. It catalyses the spiritual rebirth of hydrogen peroxide to water and molecular oxygen. Hydrogen peroxide is a by ware of metabolic cognitive operation . It is usually produced in peroxisomes when they partially oxidize roly-poly acids. When catalase is absent, the reaction it catalyzes is spontaneous, but at very low rates that are not able to reduce the harmful effects of hydrogen peroxide

a. The enzyme of this experiment is the catalase from the potatoes. Catalase is an enzyme present in humans that breakdown peroxide (H2O2), a toxic substance to organisms but is a byproduct of biochemical reaction. Catalase is found in peroxisomes within cells, and typically breakdown the hydrogen peroxide (if any) produced within the cell before it is able to leave. This makes catalase an extremely vital enzyme as it basically prevents the toxin from doing any true harm.   b.

Within a cell, enzymes are used as a catalyst to increase the rate of chemical reaction. They do not consume themselves, rather they help in increasing the rate of reaction. Within the body, enzymes vary depending on their specific functions. For instance, hydrogen peroxide is a toxic chemical, but it breaks down into harmless oxygen and water. This reaction can be sped up using the enzyme catalyst produced by yeast. Hydrogen peroxide is produced as a byproduct in cellular reaction, because it is poisonous and must be broken down, therefore this reaction is important. The speeding up of the reaction is shown below:

Testing the Effects of Temperature on the Decomposition of Hydrogen Peroxide with the Enzyme Catalase