Catalase is an enzyme found in many organisms, including plants and animals, that plays a crucial role in the breakdown of hydrogen peroxide, a toxic compound produced as a byproduct of cellular metabolism. In this lab report, we will explore the factors that affect the activity of catalase and how this enzyme carries out its important function.
The first step in this lab report is to describe the experimental setup. A common method for studying catalase activity is to measure the rate of oxygen production as the enzyme breaks down hydrogen peroxide. To do this, we can set up a reaction vessel containing a known concentration of hydrogen peroxide and a small amount of catalase enzyme. The reaction can be started by adding a small amount of potato or liver tissue, both of which contain high levels of catalase. The reaction can be monitored by measuring the volume of oxygen produced over time using a gas pressure sensor or by collecting the gas in a graduated cylinder.
Next, we will describe the results of the experiment. As the catalase enzyme breaks down hydrogen peroxide, it produces water and oxygen gas. The rate of oxygen production can be measured and plotted on a graph to determine the activity of the enzyme. The results of the experiment will likely show that the rate of oxygen production increases as the concentration of hydrogen peroxide increases, indicating that the enzyme is more active at higher substrate concentrations.
After describing the experimental setup and results, we can then discuss the factors that affect the activity of catalase. One important factor is the concentration of the substrate, hydrogen peroxide. As mentioned above, the rate of oxygen production typically increases as the concentration of hydrogen peroxide increases. Other factors that can affect catalase activity include pH, temperature, and the presence of other chemicals or enzymes.
Finally, we can conclude the lab report by summarizing the main findings and discussing the significance of catalase in biological systems. The results of the experiment demonstrate that catalase is an important enzyme that plays a vital role in the breakdown of hydrogen peroxide, a potentially harmful compound produced during cellular metabolism. Understanding the factors that affect the activity of catalase can help us to better understand the mechanisms of cellular metabolism and may have practical applications in the medical field, such as in the development of new drugs or treatments.
In conclusion, the catalase enzyme activity lab report provides a detailed analysis of the factors that affect the activity of this important enzyme and how it carries out its vital function in biological systems. Understanding the mechanisms of catalase can help us to better understand the complex processes of cellular metabolism and may have practical applications in the medical field.
Catalase Enzyme Lab Report
Catalysts bring the reactives closer to the appropriate orientation and weaken the bonds, increasing the reaction rate. Next, the graduated cylinder, used for measuring the amount of water and extract, was rinsed and 32 ml of distilled water added and stirred with a stirring rod. Hydrogen peroxide is a regular product in many cellular reactions, but the substance can be toxic, and therefore needs to be broken down to conserve the cells. One class of enzymes are known as peroxidase. Enzymes are proteins that catalyze biochemical reactions that work by reducing the activation energy for each reaction, causing an increase to the rate of the reaction. Enzymes can be found all over the body, and help aid in digestion, muscle or nerve function, as well as respiration as the function depends on the environment the enzyme is found in. Therefore I wanted to examine the breakdown properties of a digestive enzyme while under the influence of a strong inhibitor.
Overall, it is important to consider all aspects of each variable being used and how changes and differences in them can create substantial variations of results. Without enzymes acting as catalysts for biochemical reactions, life would not be able to be sustained for too long. Bacillus lincheniformis and Aspergillus oryzae are both organisms that live that in medium temperature environments. I selected Copper Sulphate as enzyme inhibitor against the concentration of 2% of Amylase solution. They do this by attaching to the substrate to form an intermediate; the substrate binds to the active site of the enzyme. The theme of this lab is the identification of unknown.
As shown in the images from the results, there was some minor foam formation from the oxygen, but in comparison to the first glass, the enzyme reaction was nowhere near as strong as the first glass. Enzyme could only function in specific shape, and the shape of enzyme is depending on the environment, therefore it is hard for an enzyme to function well in an extreme environment. This is likely because the hot temperature denatured the protein, making it impossible for the substrate to bind to the enzyme 2. The organelle responsible for the destruction of hydrogen peroxide is peroxide using the enzyme catalase. When a substrate binds to an active site on an enzyme, a reaction occurs 1. Catalase, an enzyme produced by most living organisms, catalyzes the decomposition of H2O2 in our bodies in order to maintain homeostasis. There are too Laboratory Report on Enzyme Activity 1407 Words 6 Pages LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.
Enzymes have an active site where it bonds with substrates at the and reacts with the substrates to produce and release a product. In order to do this, 5 mL of gelatin solution is added to the test tube. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells. Enzymes and proteins are important in organisms because they are involved in most chemical reactions that take place inside of an organism. Hot temperatures can denature a protein, making the substrate unable to bind to the enzyme, while cooler temperatures slow enzyme activity 2. Following that, 2 mL of 3% hydrogen peroxide was added to the test tube and was incubated again for 5 minutes.
Through this experiment, it was found that higher concentrations of acetic acid will effectively denature the enzyme catalase, preventing it from binding with the hydrogen peroxide substrate, and ultimately making it unable to decompose the toxic substance. To also learn about how to report uncertainty in your measurements. A catalyst increases the rate of reaction by reducing the activation energy required Reece 2005. An enzyme, a biological catalyst, works to speed up chemical reactions. Meaning that it eliminates H2O2 in order to prevent damage to the cells and tissues Department of Biology University of Tampa 74. These results match findings in other professional studies. They are selective in what they bind to and specific to their substrates.
The lab was also an opportunity to see a catalyzed reaction Lab Report 1 2015 Essay Lab Report 1 Purpose To develop an understanding of the metric system and use it to measure common objects. Different acids and methods could be used potentially as well, such as using hydrochloric acid, different kinds of buffers, and using pH strips to measure the exact levels of pH to where denaturation of catalase occurs. This matches the results I found, where pH of 7 allowed for the highest activity. Catalase is a very important enzyme in the body that helps to get rid of toxic substances, such as hydrogen peroxide, and without this very important enzyme the body would fall very ill. Other purposes of the lab were; to measure the effects of changes of temperature, pH, enzymes concentration, and substrate concentration on rates of an enzyme. Materials needed Beakers Bunsen burner Test tube Thermometer Stopwatch Test plate Glass rod Starch Amylase solution Water bath Iodine solution. As noted in the previous paragraph, a sudden change in pH will deactivate all enzyme activity.
All biological reactions within human cells depend on enzymes Wolfenden 1. Although hydrogen peroxide is produced to help defend against infections, a high level of this poisonous chemical could potentially harm the cells. We used different temperature catalases in order to test how temperature affects the rate of the chemical reaction. The DNA in cells codes all the information necessary to make many different enzymes and they are produced using this code whenever the cell feels the need for a particular enzyme. Catalase is utilized by organisms and cells to protect the organism from oxidative damage, in which the enzyme will convert the toxic hydrogen peroxide which acts as the substrate produced as a by-product from many other biochemical reactions through a decomposition reaction into water and molecular oxygen Collins and Dawson, 2013.
Lastly, Glass 5 had three tablespoons of vinegar added to the solution, in which no foaming occurred. The solutions were stirred and the steps for part two were repeated using different volumes of water and hydrogen peroxide, as shown on the table. If the color changes, then it is known that starches are present in the solution. Annie ChiangIB Biology HLPeriod 2Catalase Activity LabIntroduction:Enzymes are proteins that catalyze chemical reactions increase the rates of biological reactions. The reaction that will be investigated in this experiment is the decomposition of hydrogen peroxide:2 H2O2 liquid -- Catalase 2 H2O liquid + O2 gas When a catalase enzyme is added to a hydrogen peroxide solution, it becomes water and oxygen gas. The results support our hypothesis that as temperature increases the rate of the chemical reaction decreases. Without enzymes acting in the body as catalysts to speed up chemical reactions, the reactions needed to survive would be too slow, thus not enough to sustain life.
