Catalase Concentration On Hydrogen Peroxide

In this above reaction, oxygen is released and is used for other cellular purposes, but when it occurs in a test tube, similar to this experiment, the oxygen gas bubbles producing a layer of foam on the surface of the peroxide. The amount of foam and the speed it is produced are forms of measuring the catalase activity. In the next experiments, one would determine the degree of catalase action by calculating the thickness of the foam layer. It is hypothesized that when reacting with: potato, apple, steak, or liver, the plants and animal tissues will react differently.

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.

Enzyme catalysis is dependant upon factors such as concentration of enzyme and substrate, temperature and pH. These factors determine the rate of reaction, and an increase in temperature or pH above the optimum will

pH - Enzymes also have an optimum pH level. The pH of a solution affects the enzyme's secondary and tertiary structures. These bonds make the shape of an enzyme's active site. So, if these bonds are broken, the shape of the active site changes and is distorted. If there is no active site, there is no reaction resulting in no products. If the enzyme is put in a pH that is very different from the optimum pH, it can cause the enzyme to denature.

This experiment was used to determine the effect of varying concentration of hydrogen peroxide on the rate of enzyme activity. This was a decomposition reaction of hydrogen peroxide into water and oxygen gas. The hypothesis of this reaction is that, the rate of reaction will decrease with the decrease of hydrogen peroxide concentration.

The purpose of this experiment was to simply measure oxygen production rates released from decomposed hydrogen peroxide under different conditions (concentration of enzymes, temperature, and PH level).

Enzymes are defined as catalysts that speed up chemical reactions but remain the same themselves. The shape of an enzyme enables it to receive one type of molecule and that specific molecule will fit into the enzyme’s shape. Where a substance fits into an enzyme is called the active site and the substance that fits into the active site is called a substrate. Several factors affect enzymes and the rate of their reactions. Temperature, pH, enzyme concentration, substrate concentration, and the presence of any inhibitors or activators can all affect enzymes. Temperature can affect enzymes because if the temperature gets too high, it can cause the enzyme to denature. pH can affect an enzyme by changing the shape of the enzyme or the charge properties of the substrate so that either the substrate cannot bind to the active site or it cannot undergo catalysis. Every enzyme has an ideal pH that it will strive in. Increasing substrate concentration increases the rate of reaction because more substrate molecules will be interacting and colliding with enzyme molecules, so more product will be formed. Inhibitors can affect enzymes and the rate of their reactions by either slowing down or stopping catalysis. The three types of inhibitors include competitive, non-competitive, and substrate inhibition.

The aim of my investigation is to see how pH affects the activity of potato tissue catalase, during the decomposition of hydrogen peroxide to produce water and oxygen.

Changes in pH also alter an enzyme’s shape. Different enzymes work best at different pH values. The optimum pH for an enzyme depends on where it normally works. For example, intestinal enzymes have an optimum pH of about 7.5 whereas enzymes in the stomach have an optimum pH of about 2.

We used a computer and a gas pressure sensor to measure the production of oxygen gas as hydrogen peroxide was destroyed by the enzyme catalase at various enzyme concentrations, pH values, and substrate concentrations. We then put 3 mL of water and 3 mL of 3% H2O2 (hydrogen peroxide) to our four test tubes as well as different amounts of catalase drops to each test tube. For the second trial, we added 3 mL of 3% H2O2 and pH Buffer as well as 2 drops of enzyme solution. Lastly, for our last trial we added different amounts of 3% H2O2 and water. We concluded that as pH increases, the rate of enzyme activity decreases and this can be seen in the graphs since when the pH was 10, the rate of enzyme activity was the lowest at 0.3513.

For the experiment, the enzyme Catalase was used at varied temperatures to measure oxygen produced by the breakdown of H2O2. Most enzymes are specialized molecules of protein that have a specific structure to them. They are catalysts in metabolic activity. Being that they are made from proteins, the shape comes from the folding or condensing of the long strands of amino acids. These polypeptides fold from primary, to a secondary, then tertiary structure.

The purpose of this experiment was to analyze the effects of substrate concentration and temperature on activity of catalase. The activity was measured by observing the amount of time it took for 10 mL of oxygen to evolve as an outcome of the catalyzed breakdown of hydrogen peroxide. Increased temperature and substrate concentration will both effect the activity of a catalase enzyme. We used 4 different temperatures of an enzyme, as well as a variety of scientific materials. The results of this experiment confirmed the hypothesis that was tested.

The effect different temperatures have on the rate that enzymes work was tested by this lab. The concentration of the enzyme catalase in different tissues was also tested. It was tested by pouring 5 ml of hydrogen peroxide over liver in different conditions and over a piece of meat and potato.

reaction rate increases. If the temperature of an enzyme gets to high the reaction rate will slow

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.