Catalase Activity Lab

The results of the three-part experiment provide a deeper knowledge about the factors that influence the rate of the reaction of the enzyme activity and how the factors influence the structure or function of the enzyme.

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.

Abstract: Enzymes, catalytic proteins that at as catalysis which makes the process of chemical reactions more easily. There are two main factors that actually affects enzymes and their functions which are temperature and pH. Throughout this experiment, the study how pH and peroxidase affects each other and the enzyme was made. The recordings of how the enzymes responded when it was exposed to four different pH levels to come up with an optimum pH which was predicted in the hypothesis and the IRV at the end.

Enzymes are very efficient catalysts for biochemical reactions. They speed up reactions by providing an alternative reaction pathway of lower activation energy. Like all catalysts, enzymes take part in the reaction - that is how they provide an alternative reaction pathway. But they do not undergo permanent changes and so remain unchanged at the end of the reaction. They can only alter the rate of reaction, not the position of the equilibrium. Enzymes are usually highly selective, catalyzing specific reactions only. This specificity is due to the shapes of the enzyme molecules.

In the following experiments we will measure precise amounts of potato extract as well as Phenylthiourea, combined with or without deionized water and in some instances change the temperature and observe and record the reaction. We will also investigate the different levels of prepared pH on varying samples of the potato extract and the Phenylthiourea and record the results. We will answer question such as what is the best temperature for optimum temperature reaction as well as the best pH level for the same reaction.

peroxide (H2O2). The enzyme breaks H2O2 into water and oxygen. The production of the oxygen

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.

Enzymes are high molecular weight molecules and are proteins in nature. Enzymes work as catalysts in biochemical reactions in living organisms. Enzyme Catecholase is found on in plants, animals as well as fungi and is responsible for the darkening of different fruits. In most cases enzymatic activities are influenced by a number of factors, among them is temperature, PH, enzyme concentration as well as substrate concentration (Silverthorn, 2004). In this experiment enzyme catecholase was used to investigate the effects of PH and enzyme concentration on it rate of reaction. A pH buffer was used to control the PH, potato juice was used as the substrate and water was used as a solvent.

The Effects of Varied Temperatures, pH Values, Enzyme Concentrations, and Substrate Concentrations on the Enzymatic Activity of Catecholase

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,

Observing how the enzyme catalase found in chicken and beef livers breaks down hydrogen peroxide at varying pH levels and temperatures.

The purpose of this lab was to determine to what degree environmental factors affect cellular processes and the rate of activity for the enzyme catalase. Since catalase speeds up the production of oxygen gas, the rate of enzyme activity can be measured as the height of the column of oxygen gas bubbles or the perceived intensity of the reaction (on a scale of 0-5) produced in a test tube. To record the role that environment plays in the reaction of an enzyme, the enzyme was exposed to various changes in temperature, pH, and concentration by placing a small piece of liver in test tubes of different conditions (one cold, one room temperature, one at core body temp, another boiling and the final in the dark.)

Enzyme are proteins that act as biological catalysts to facilitate the biochemical reactions in all living organisms (Pickering, 2000). A catalyst is a substance that increases the rate of chemical reactions without itself undergoing a permanent change (Engelkirk et al., 2011). In most cases, chemical reactions require a certain amount of energy to take place or else, they would happen at a rate too low to sustain life. Therefore, enzyme lowers the activation energy to reach the transition state for chemical reactions to happen faster and maintain the live of organism (Lenaz et al., 1972).

The purpose of this study is to test how changing the temperature of the liver, which was the catalase source, would affect the rate of reaction with H2O2. If temperature increases then there would be less O2 released because proteins denature when temperatures are too high, losing their shape and ability to carry out their intended function.