How The Catalase Enzyme

The hypothesis is that catalase activity will increase exponentially with higher concentrations of hydrogen peroxide until all catalase active sites are filled, in which case the

If another enzyme like lactase is used, no reaction would take place because the substrate, hydrogen peroxide, wouldn’t fit into the active site.

What would it mean if a known catalase positive bacteria did not produce bubbles after the addition of H2O2? It would mean that a different strain of bacteria was used that doesn’t react to hydrogen peroxide.

The first experiment begun by filling a 600-ml beaker, almost to the top, with water. Next, a 10-ml graduated cylinder was filled to the top with water. Once water was added to the beaker and graduated cylinder, a thumb was placed over the top of the graduated cylinder. This would ensure that no water was let out and no bubbles were let into the graduated cylinder. Next, it was turned upside down and fully submerged into the beaker. Then, a U-shaped glass tube was attained. The short end of the glass tube was placed into the beaker with the tip inside of the graduated cylinder. Next, a 50-ml Erlenmeyer flask was received. After, 10-ml of substrate concentration and 10-ml of catalase/buffer solution were placed into the flask. A rubber stopper was then placed on the opening of the flask. After adding these, the flask was held at the neck and spun softly

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

The data from the experiment supports the hypothesis that catalase functions the most efficiently at a neutral pH of 7. Table 1 shows that catalase helped consume 3 mL of hydrogen peroxide in the solution with a pH of 7, more than any other solution. As the pH

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

For the final test, two drops of hydrogen peroxide (H2O2) were placed on the isolated colony of the BHIA medium, observed immediate formation of bubbles, as O2 was produced indicating a positive test for catalase.

One test tube was placed in an ice bath at 1°C, one in the incubator at 37°C (room temp), one in boiling water at 95/98°C. After 15 minutes the test tubes were removed one at a time and hydrogen peroxide was added to each and then mixed. 20 seconds after mixing the height of the bubble column was measured and recorded in a table. For the next test the concentration of the enzyme to catalase ratio was changed, leaving the amount of hydrogen peroxide as constant. For this, three test tubes (all marked at every 1 and 5th cm) were used.

We could use the H2O4 because acids will interfere with hydrogen bonds and other IMFs in the enzyme which would denature it, permanently making the enzyme unable to work. The catalase was the enzyme that acted on the product, which was hydrogen peroxide (H2O2). And of course, the hydrogen peroxide, or H2O2, was the substrate and the catalase was the enzyme.Our results seemed to be consistent because once we added the necessary amount that was needed to determine the amount of H2O2 in the solution, the color of the solution afterwards would always be a light, clear brown, as opposed to having various colors and shades each time. This means that we added the correct, proportional amount of potassium permanganate each time. In comparison to the class data, less of our H2O2 was decomposed. For example, for the trial for 30 seconds, 0.6 mL of our H2O2 was decomposed while the average for the class data was 2.22

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.

Catalase are an enzyme that catalyses the reduction of hydrogen peroxide into H2O and O2. Catalase are a common enzyme that can be found in almost all living organisms such as potatoes. It is specifically found in the cells that are exposed to oxygen and can be in a plant or animal cell. [1]

A catalase is a molecule that speeds “up the rate of a reaction without themselves being used up or permanently altered” (Audesirk & Byers 2008). They do this by lowering the activation energy required for the reaction to begin. This allows a higher proportion of molecules to move fast enough to react when the molecules collide. Enzymes are biological catalysts. They are proteins that promote specific chemical reactions. In this lab experiment, the chemical equation is: 2H2O2 2H20 + O2. Catalase, an enzyme that destroys hydrogen peroxide (H2O2), is used here to facilitate the chemical reaction from the substrate (2H2O2) to the product (2H20 + O2). This demonstrates how catalase operates in our body to destroy harmful toxins. However, the reaction

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.

“Is there a relationship between catalase concentration and the rate of enzyme activity?” The cells in your body use enzymes every day, they turn harmful chemicals into innocuous substances in your body. Enzymes are proteins produced by cells in your body that speed up reactions, that would otherwise a longer amount of time; however, the enzyme is not altered during this process. Each of the hundreds of enzymes in your body have a specific job or purpose, they are each responsible for a particular reaction in each of the cells in your body. In the following lab, we will study and look into one of the enzymes that is found in the living tissues of the body. This enzyme is called a catalase, and it speeds up a reaction that breaks down hydrogen peroxide, a deathly chemical, into two innocuous substances, water and oxygen. The chemical equation for this reaction is: 2H2O2  2H2O + O2. Without the enzyme catalase, this reaction occurs significantly slower. In this lab, we will be testing the impact of the enzyme catalase on hydrogen peroxide given different amounts of time, adding more time to the experiment with each trial.