Catalase Lab

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

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.

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.

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

An enzyme is a protein macromolecule which acts as a catalyst, an agent which speeds up reactions without being consumed by it. They are vital to life; cellular chemical reactions would not occur fast enough to support life, without the aid of enzymes. They do this by lowering the activation energy (EA), which is the energy that must be added to the reactants at the start of reactions, it has to be reached in order for the reaction to occur (Reece, Wasserman and Urry). There are hundreds of enzymes known, but not all cells contain the same ones, an example of this is catalase which will be the experimental enzyme in the lab.

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.

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.

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

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:

Effects Temperature and Substrate Concentration have on Enzyme Catalase Activity Abstract Enzymes are protein catalysts, which is a substance that speeds up the rate of a chemical reaction. The need of breaking down hydrogen peroxide into oxygen is growing because of the harmful toxins present. In the first experiment we hypothesized that as the substrate concentration increased, so did the reaction rate, therefore allowing more oxygen to be produced is less time. The first experiment mixed each substrate concentration, 0.8%, 0.4%, 0.2%, and 0.1% with a constant catalase buffer.

Enzyme are globular protein and are responsible for most of the chemical substance action of living organisms. They act as catalysts which is a substance that focal ratio up chemical reactions without being destroyed or altered during the cognitive process .Enzymes may be used over and over again. Both the temperature and the pH at which enzymes function are extremely important (Kent, M. 0) H2O2 is toxic to most living organisms. H2O2can be converted to oxygen and water, as follows: 2 H2O2 2 H2 O + O2 Although this reaction occurs spontaneously, the enzyme catalase increases the rate considerably. (Masterman, D., & Vernier Software. 1996A draw of being have the power to decompose hydrogen peroxide enzymatically. Enzymes are globular proteins and are responsible for most of the chemical substance substance action of living organisms. Catalase is find in most living organisms. A great deal can be learned about enzyme by studying the pace s of enzyme-catalyzed response which is the rate of a chemical reaction may be field in a bit of ways including: measuring the rate of appearance of a product (in this case, O2, which is given off as a flatulence ). In this experiment, you will bill the rate of enzyme activity under various conditions of enzyme concentration. substance that speed up chemical reactions without being destroyed or altered during the process. It is possible to measure the

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

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,

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.