Purpose/Problem: There are four parts to the Enzyme Catalyst lab - Activity A, B, C, and D. In activity A, the characteristics of enzyme actions will be observed. The main purposes are to determine the rate of an enzyme catalyzed reaction, to study the characteristics of an enzyme mediated reaction, and to observe the effect of heat on enzyme activity. The purpose of activity B is to use the Titration Protocol to determine the initial amount of H2O2 present in a solution. The amount will be the baseline for activities C and D. The purpose of activity C is to determine the rate at which H2O2 spontaneously decomposes when exposed to room temperatures and ambient light for 24 hours. The purpose of activity D is to determine the rate at which catalase decomposes H2O2. After adding H2SO4 for different time lashes, etc., the resulting data will be graphed at which the catalase decomposed by catalase.…
Enzymes are biological catalysts or assistants that consist of various types of proteins that work to drive the chemical reaction required for a specific action or nutrient. They can either launch a reaction or speed it up. Catalase is a common enzyme found in nearly all living organisms exposed to oxygen. It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). The catalase used in this experiment will come from five different sources: Spinacia oleracea (Spinach), Brassica oleracea (Broccoli), Solanum tuberosum (Russet Potato), Malus domestica (Apple), and Allium cepa (Onion). The five different catalases from the sources will all be used to catalyze Hydrogen peroxide (H2O2). When hydrogen…
The enzyme in this experiment was catechol oxidase, extracted from a potato. In the experiment, when substrate concentration was held constant, and the different enzyme serial dilutions were being tested, the reaction rate was expected reaction rate was expected to increase until all enzymes are saturated, then the reaction rate would level off. First, dilute the enzyme and substrate. After,…
We found a study about the effects of glycosylation and pH conditions in the dynamics of human arylsuffatase A. They concluded that lowering pH and increasing glycosylation reduced the flexibility of the enzyme. Also, at acidic pH levels the glycosylated enzyme had a higher conformational stability. This study was similar to ours in that it investigated how pH conditions affect enzyme functionality. They found optimal pH conditions for the enzyme like we did, but they took into account another variable that is that influenced functionality…
The Effect of Different Concentrations of the Enzyme Catechol Oxidase on the Rate of Benzoquinone Production When Mixed with Pure Catechol…
1977). The average rate of catalase activity as seen in the chart above is 4.97 seconds while the orange is at zero seconds. During the experiment, none of the orange filtered discs rose in the given amount of time. From the data, one can see that the orange has no effect on catalase activity. Therefore the null hypothesis, the orange will not affect the catalase activity is accepted.…
Results show: as the buffer pH deviates from a neutral pH of 7.0, the reaction is slowed and/or inhibited; cooling or heating the reaction slows and/or inhibits the rate and/or completeness of the reaction. The bioavailability of enzymes is hindered by deviating the temperature and/or the pH of the buffer solution; hence, the color change of the product is less drastic and intense, drastic being dark brown, somewhat reactive being pink, and non-reactive being colorless/clear; thus, chemical activity was hindered due to lack of the enzyme¡¦s ability to act at its full potential as a catalyst. Reactions seemingly best occur when all conditions are ¡§neutral¡¨ (i.e. buffer pH =7.0 and temperature around room temperature +-28¢XC), and enzyme is completely pure and non-diluted (referred to as ¡§Stock…
As the data is then changed into the rate of reaction based on time, we can tell that the rate of disappearance is slowly decreasing. To get a even clearer idea on what our data looked like, I put the rate of disappearance of H2O2 into a time plot which illustrates rate over time. We can now see the image that the graph is exponentially decreasing at a rapid rate as the time of the mixing increases. The average rate of reaction for our results is .031 mL/s. The data we see is an result of decreasing concentration of substrate. When the catalase is first introduced for 10seconds, the rate of reaction was highest because that was when substrate and enzyme concentration stayed the highest. As the experiment is prolonged, substrate concentration will only decrease as it is limited but the enzymes will continue to catalyze the lower concentration which leads to a lower rate. The amount of H2O2 consumed in the time course determination test never exceeded the baseline because it is expected that the baseline reacts to…
The purpose of this lab was to test if ethanol affects the reaction involving hydrogen peroxide and catalase. Tests were performed by putting chicken liver, ethanol solution (diluted ethanol solution for other trials) and hydrogen peroxide in a test tube with a side arm, and having a rubber tube lead the oxygen gas into a gas collection tube. Results from the tests showed a negative correlation, this means that the more diluted the solution of 95% ethanol was, the less oxygen gas collected. Controlling a number of factors which include human error, temperature change, pH levels, substrate concentrations and ensuring a controlled experimental environment will work to increase the accuracy of the experiment.…
Introduction: The Enzyme Lab is to conduct investigations to determine the most favorable conditions for the most efficient enzyme activity. Variables to be used testing include temperature, pH values and surface area. Enzymes are proteins that speed up the rate of chemical reactions, which would otherwise progress more slowly.(Background Information; pg. 1) pH is a measurement of the acidity or alkalinity (base) of a solution. When the liver got mixed with H2O2 , the first time the chemical reaction was fast, the second time the reaction was slow and the last try was very fast. Temperature is the degree or intensity of heat present in a substance or object. When the temperature of the liver changed from freezing to very hot to room…
In order to investigate the effects of temperature on the activity of enzyme-catalyzed reactions, we made fifteen tubes that contained reaction buffer, hydrogen peroxide, turnip extract, and the dye. These reagents were placed in large bottles and were labeled with a sharpie. We gathered fifteen small test tubes for testing and three large test tubes to fill it with stock solutions needed to carry out the experiment. The large test tubes were filled with buffer, dye, and hydrogen peroxide. Each test tube made contrasted in the amounts of solutions used. The odd numbered tubes contained 1.0 ml of turnip extract and 4.0 ml of reaction buffer. The even numbered tubes contained 1.0 ml dye and 2.0 ml of hydrogen peroxide.…
In this laboratory exercise we studied enzyme catalase, which accelerates the breakdown of hydrogen peroxide into water and oxygen. The purpose was to isolate catalase and measure the rate of activity under different conditions. The laboratory was also conducted in association with a second laboratory that measured the effects of an inhibitor on the enzymes. Changes in temperature and pH along with Substrate Concentration and Enzyme Concentration were the conditions tested in the experiment.…
As the environment and temperature is changed from 0 °c to 20°c to 95°c, the absorbance of catechol and catecholase reaction will increase over time. The rate of reaction increases as the temperature increases.…
For Activity A, we first tested enzyme activity. First, we used an H2O2 syringe to transfer 10 mL of H2O2 into an unlabeled 60-mL cup. Then, we used a transfer pipet to add one mL of catalase solution into the unlabeled 60-mL cup that we put H2O2 in. After that, we observed the solution for one minute. Then we tested the effect of boiling on enzyme activity. First we used a transfer pipet to transfer 4 mL of catalase into a test tube. After that, we placed the test tube filled with catalase in a boiling water bath for five minutes. While we were waiting, we rinsed the unlabeled cup we used earlier when we tested enzyme activity. Then we used a H2O2 syringe to transfer 10 mL of H2O2 into the rinsed unlabeled cup. After five minutes, we transferred 1 mL of the boiling catalase into the unlabeled cup with H2O2 in it with an unused transfer pipet and observed the results. After testing the effect of boiling on enzyme activity, we tested for catalase in living tissue. First, we rinsed the unlabeled 60 mL cup we used earlier. Then, we used a scalpel to cut a small piece of liver. After that, we macerated the piece of liver with a glass rod. When the liver was macerated enough, we put it in a cup with 10 mL of H2O2, which was transferred into the cup with a H2O2 syringe. Lastly, we observed the cup.…
Based on this experiment and the data collected one is able to conclude that the optimal environment in which this specific catalase is able to function is around 40°C…