How To Write A Catalase Lab Report

In this lab or experiment, the aim was to determine the following factors of enzymes: (1) the effects of enzymes concentration the catalytic rate or the rate of the reaction, (2) the effects of pH on a particular enzyme, an enzyme known and referred throughout this experiment as ALP (alkaline phosphate enzyme) and lastly (3) the effects of various temperatures on the reaction or catalytic rate. Throughout the experiment 8 separate cuvettes and tubes are mixed with various solutions (labeled as tables 1,3 & 4 in the apparatus/materials sections of the lab) and tested for the effects of the factors mentioned above (concentration, pH and temperature). The tubes labeled 1-4 are tested for pH with pH paper and by spectrophotometer, cuvettes 1a-4a was tested for concentration and cuvettes labeled 1b-4b was tested for temperature in four different atmospheric conditions (4ºC, 23ºC, 32ºC and 60ºC) to see how the enzyme solution was affected by the various conditions. After carrying out the procedures the results showed that the experiment followed the theory for the most part, which is that all the factors work best at its optimum level. So, the optimum pH that the enzymes reacted at was a pH of 7 (neutral), the optimum temperature that the reactions occurs with the enzymes is a temperature of 4ºC or

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.

In the experiment we used Turnip, Hydrogen Peroxide, Distilled Water, and Guaiacol as my substances. On the first activity, Effect of Enzyme concentration of Reaction Rate for low enzyme concentration, we tested three concentrations of the turnip extract, and hydrogen peroxide. For the Turnip Extract I used 0.5 ml, 1.0 ml, and 2.0 ml. For hydrogen peroxide we used 0.1 ml, 0.2 ml, and 0.4 ml. We used a control to see the standard, and used a control for each enzyme concentration used. The control contains turnip extract and the color reagent, Guaiacol. We prepared my substrate tubes separately from the enzyme tubes. My substrate tube

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.

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.

Background and Introduction: Enzymes are proteins that process substrates, which is the chemical molecule that enzymes work on to make products. Enzyme purpose is to increase the rate of activity and speed up chemical reaction in a form of biological catalysts. The enzymes specialize in lowering the activation energy to start the process. Enzymes are very specific in their process, each substrate is designed to fit with a specific substrate and the enzyme and substrate link at the active site. The binding of a substrate to the active site of an enzyme is a very specific interaction. Active sites are clefts or grooves on the surface of an enzyme, usually composed of amino acids from different parts of the polypeptide chain that are brought together in the tertiary structure of the folded protein. Substrates initially bind to the active site by noncovalent interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions. Once a substrate is bound to the active site of an enzyme, multiple mechanisms can accelerate its conversion to the product of the reaction. But sometimes, these enzymes fail or succeed to increase the rate of action because of various factors that limit the action. These factors can be known as temperature, acidity levels (pH), enzyme and/or substrate concentration, etc. In this experiment, it will be tested how much of an effect

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,

After the substrate solution was added, five drops of the enzyme were quickly placed in tubes 3, 4 and 5. There were no drops of enzyme added in tubes 1 and 2 and in tube 6 ten drops were added. Once the enzyme solution has been added the tubes were then left to incubate for ten minutes and after five drops of DNSA solution were added to tubes 1 to 6. The tubes were then placed in a hot block at 80-90oC for five minutes. They were then taken out after the five minute period and using a 5 ml pipette, 5 ml of distilled water were added to the 6 tubes and mixed by inversion. Once everything was complete the 6 tubes were then taken to the Milton Roy Company Spectronic 21 and the absorbance of each tube was tested.

Discussion: The purpose of this experiment was to observe what the normal enzyme1 (proteins that catalyze chemical reactions) activity of beef liver catalase was, and to measure the effects of extreme changes in temperature and pH on the beef liver catalase function. We also observed what the bromelain1 (proteins in pineapple) activity was in a fresh pineapple compared to canned pineapple. Enzymes are present in all living things.1 These specialized proteins speed up chemical reactions fast enough to sustain life.1 This lab was driven by the question; if there is an extreme change in temperature or pH on an enzyme catalase, or a bromelain enzyme, then that catalase or bromelain will be affected or denatured.

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 purpose of this experiment is to measure the rate of catalase enzyme activity under different

The purpose of this experiment is to understand that enzyme at different conditions will react different such as temperature . By comparing the catalase at 0°c and boiled catalase . A 5 mL Catalase covered in ice was prepared prior to the experiment has to reach certain level of temperature . Hydrogen Peroxide and Water with 1% detergent were used in this experiment to analyze cold and boiled catalase reaction . The observation to measure the height of bubbles in each 3 paired of labeled test tubes after transferring the catalase boiled and cold one at time for 30 seconds . As noticed , without the presents of the catalase hydrogen peroxide and water (w 1% detergent ) did not able to produce as much as bubbles . Nor the boiled catalase transfers

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.