The Effect Of Temperature On Catalase Enzymes

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.

· I predict that the enzyme will work at its best at 37c because that

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

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.

This investigation will be carried out to investigate the rate of reaction of the enzyme catalase on the substrate hydrogen peroxide.

The Impact of Temperature and pH on the Enzyme Activity of Catechol Oxidase in Solanum Tuberosum Samples

Introduction: Starting out with some background information, I know that enzymes are biological catalysts. The enzyme that I used for this experiment was potato juice. Enzymes make reaction rates go faster. They lower activation energy, making chemical reactions. Temperature has an effect on canola cultivars. The higher temperature decreased stem diameter, but room temperature had thicker stems. So I believe the same will happen for the catechol oxidase; the solution will react faster at room temperature. Other enzymes can also have different effects such as the enzyme in cattle serum. The enzyme lost activity in room temperature. With that being said room temperature can also be detrimental with specific enzymes. Fungus also

These results show how temperature of extreme high, or low affects enzyme activity. The highest rate of enzyme activity occurred at 37 Cº. Anything that was hotter or cold than 37 Cº slowed the reaction rate. As I thought, 100 degrees would denature the enzyme, and that was the case. The data provided shows exactly what temperatures enzymes work best, and worst. The objective was achieved as we discovered the different reaction rates under different temperatures. The results are reliable, as we know enzymes do not work well when under extreme heat or denaturation occurs. What I learned in this experiment was that enzymes don’t work well under cold temperatures because they tend to move slower. My hypothesis did not quite match, because I thought they work best at lower temperatures.

Hypothesis: If the temperature increases, then rate of the chemical reaction will increase as well, and if the temperature decreases, then the rate of reaction will also decrease.

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.

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.

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.

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.