Catalase Lab Report

The human body is an incredible system that is capable of working a multitude of diverse functions. Without the help of the many different protein molecules, the human body would not be able to function properly. One major group of proteins called enzymes are mandatory for essential life. These proteins are constantly at work assembling molecules, metabolizing energy, and fighting off infections. An enzyme is a macromolecule that acts as a catalyst that speeds up a chemical reaction without being consumed by the reaction. Without these proteins, these reactions would take place too slowly to keep us alive. Essential parts in your body like vitamins and minerals cannot do any work without

Enzymes are biological catalysts that speed up chemical reactions, without being used up or changed. Catalase is a globular protein molecule that is found in all living cells. A globular protein is a protein with its molecules curled up into a 'ball' shape. All enzymes have an active site. This is where another molecule(s) can bind with the enzyme. This molecule is known as the substrate. When the substrate binds with the enzyme, a product is produced. Enzymes are specific to their substrate, because the shape of their active site will only fit the shape of their substrate. It is said that the substrate is complimentary to their substrate.

Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is

Introduction:Enzymes are made up of proteins which are produced within living cells and act as catalysts which speed up chemical reactions. They are made up of long chains of amino acids containing carbon, hydrogen, oxygen and nitrogen. Enzymes are structured to be

The rate of reaction between Catalase and the hydrogen peroxide (H2O2) can vary depending on many factors including the enzyme concentration in a solution. In this investigation, the rate of reaction will be measured by the change in temperature of the liquefied spinach (catalase) over a period of 30 seconds, once the hydrogen peroxide (H2O2) has been added into the solution.

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,

As seen on table 1, the hypothesis in the introduction of this lab has been supported by the procedures. As the temperature varied from catalases optimal of 37° C, the reaction rate of catalase decreased. 37°C had the highest reaction rate of the three, at 3, while 4°C had the middle rate of reaction at 2.5, and 100° C had the lowest reaction rate of 0.5.

The purpose of this experiment is to learn the effects of a certain enzyme (Peroxidase) concentration, to figure out the temperature and pH effects on Peroxidase activity and the effect of an inhibitor. The procedure includes using pH5, H202, Enzyme Extract, and Guaiacol and calibrating a spectrophotometer to determine the effect of enzyme concentration. As the experiment continues, the same reagents are used with the spectrophotometer to determine the temperature and pH effects on Peroxidase activity. Lastly, to determine the effect of an inhibitor on Peroxidase, an inhibitor is added to the extract. It was found that an increase in enzyme concentration also caused an increase in the reaction rate. The reaction rate of peroxidase increases at 40oC. Peroxidase performed the best under pH5 and declined as it became more basic. The inhibitor (Hydroxy-lamine) caused a decline in the reaction rate. The significance of this experiment is to find the optimal living conditions for Peroxidase. This enzyme is vital because it gets rid of hydrogen peroxide, which is toxic to living environments.

Introduction Enzymes serve important roles in the biological processes that are undertaken in human bodies. Enzymes are most important as their role as proteins which speed up chemical reactions in the body, which make them catalytic proteins (Agarwal, 2006). The unique structure of enzymes allows them to fit into a specific type of chemical, called a substrate (Robinson, 2006). The functionality of an enzyme is determined by its active site. The active site of an enzyme is the location on the enzyme where the substrate binds to produce a substance (Robinson, 2006).

“Enzymes are proteins that have catalytic functions” [1], “that speed up or slow down reactions”[2], “indispensable to maintenance and activity of life”[1]. They are each very specific, and will only work when a particular substrate fits in their active site. An active site is “a region on the surface of an enzyme where the substrate binds, and where the reaction occurs”[2].

Organisms cannot depend solely on spontaneous reactions for the production of materials because they occur slowly and are not responsive to the organism's needs (Martineau, Dean, et al, Laboratory Manual, 43). In order to speed up the reaction process, cells use enzymes as biological catalysts. Enzymes are able to speed up the reaction through lowering activation energy. Additionally, enzymes facilitate reactions without being consumed (manual,43). Each enzyme acts on a specific molecule or set of molecules referred to as the enzyme's substrate and the results of this reaction are called products (manual 43). As a result, enzymes promote a reaction so that substrates are converted into products on a faster pace (manual 43). Most enzymes are proteins whose structure is determined by its sequence of its amino acids. Enzymes are designed to function the best under physiological conditions of PH and temperature. Any change of these variables that change the conformation of the enzyme will destroy or enhance enzyme activity(manual, 43).

The biggest problem my group experienced was that as we moved into our second round of trails, we noticed consistently higher reaction times for the same concentration of enzyme. There are two possible explanations for this. The first is that we continued to use the same container of hydrogen peroxide every trail. The peroxide may have become diluted, reducing the rate at which the reaction could happen. This became apparent when we got to the lowest concentration trails. We were reasonably sure that these would both take a long time, so we did both trails simultaneously in two different containers: one old, one new. The trail conducted in the container of fresh peroxide finished in just over six minutes, however the trail conducted in the used

This lab tested the effectiveness of the catalase enzyme, against hydrogen peroxide, in varying temperature conditions. The hydrogen peroxide was heated or cooled to 5 different temperatures: the first sample was cooled to 8° to test the rate of reaction in cold temperatures, the next sample was heated to 30° to resemble human body temperature which is 37° (HealthLinkBC, 2016), the third and fourth samples were set to 50° and 70°, respectively, to measure the effects heat on the enzymes, the last sample was left at room temperature, 24°, and used as a control. According to enzyme theory, as the temperature of a reaction increases, the amount of energy within a system increases, allowing reactions to occur more readily, and at a faster rate

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.

The enzyme catalase is found in almost every living organism with exposure to oxygen. To be specific, catalase is found in an organelle called peroxisome. The job of a catalase is to take hydrogen peroxide, or H2O2, and hydrolyze it into oxygen gas, O2 and water, H2O. All enzymes are made so that there is an active site, and the active site is made so that only a certain substrate can bind with it. In this case, hydrogen peroxide is the substrate and the catalase is the enzyme. The hydrogen peroxide fits right in the active site of the catalase.