Wait a second!
More handpicked essays just for you.
More handpicked essays just for you.
The activity of catalase
The activity of catalase
Importance of enzymes in metabolism
Don’t take our word for it - see why 10 million students trust us with their essay needs.
Recommended: The activity of catalase
Introduction When chemical reactions occur in the body, enzymes are used to speed up the reactions and lower the energy of activation. The rate of reactions is increased due to the complex that is established by the enzyme and the substrate. This complex that forms between the two inhibit movement respective of the two and arranges the reactive groups of the substrates next to each other (1). Enzymes allow chemical equilibrium is able to be maintained throughout the reaction and are not consumed, while accelerating the reaction (2,3). Active sites on the enzymes are where the substrates bind, and the sites are specific to the substrate (2,3). The protein that makes up the enzyme has a particular shape, due to secondary and tertiary structures, …show more content…
It is also used as an antiseptic for injuries in hospitals and at homes. However, hydrogen peroxide is toxic to cells in high levels due to how readily it transforms to a hydroxyl radical, OH- (5). Catalase is an enzyme whose job is to break down hydrogen peroxide, so it does not convert to the hydroxyl radical. When hydrogen peroxide is present in the cell, catalase catalyzes a reaction that transforms hydrogen peroxide into water and oxygen gas. This reaction causes bubbles to form (4). Without catalase, hydrogen peroxide can kill the …show more content…
If enzymes are available, other factors contribute to the rate of the reaction, such as pH and temperature as mentioned earlier. Concentration of both the enzyme and the substrate also affects how quickly the reaction occurs within the cell. The amount of enzyme that exists in the cell can affect how much product is formed. The concentration of catalase where enzyme activity is the highest 20% due to the difference in concentrations of the substrate and the enzyme. Activity is the greatest when there is a larger ratio of substrate to enzyme
Catalase is a common enzyme that is produced in all living organisms. All living organisms are made up of cells and within the cells, enzymes function to increase the rate of chemical reactions. Enzymes function to create the same reactions using a lower amount of energy. The reactions of catalase play an important role to life, for example, it breaks down hydrogen peroxide into oxygen and water. Our group developed an experiment to test the rate of reaction of catalase in whole carrots and pinto beans with various concentrations of hydrogen peroxide. Almost all enzymes are proteins and proteins are made up of amino acids. The areas within an enzyme speed up the chemical reactions which are known as the active sites, and are also where the
This evidence alone suggests that higher increases in substrate concentration causes smaller and smaller increases in enzyme activity. As substrate concentration increases further, some substrate molecules may have to wait for an active site to become empty as they are already occupied with a substrate molecule. So, the rate of the reaction starts to level off resulting in a plateau in the graphs. This means that the reaction is already working at its maximum rate, and will continue working at that rate until all substrates are broken down. The only way the reaction rate would increase, is if more enzyme was added to the solution. This confirms that increases in substrate concentration above the optimum does not lead to greater enzyme activity. Therefore, the rate of reaction is in proportion to the substrate
When this substrate fits into the active site, it forms an enzyme-substrate complex. This means that an enzyme is specific. The bonds that hold enzymes together are quite weak and so are easily broken by conditions that are very different when compared with their optimum conditions. When these bonds are broken the enzyme, along with the active site, is deformed, thus deactivating the enzyme. This is known as a denatured enzyme.
All enzymes are proteins, which are specific to the molecule that they break down. This is known as the ‘lock and key’ theory, where the active site only allows a specific substrate to be broken down, eventually resulting in easier absorption (larger surface area). Enzymes are made up of a long chain of amino acids, which form together in such a way as to leave a specific pocket, into which a substrate (as long as it fits perfectly into the pocket) can fit into it like a key in a lock (hence the ‘lock and key’ theory). The reaction then takes place, and the product of the substrate is then released.
This hurdle is called the activation energy of the reaction. [IMAGE] By decreasing the activation energy, more substrate is changed to product in a certain amount of time. That is, the enzyme increases the rate of the reaction. [IMAGE] The activity of catalase can be measured by finding the rate of which the oxygen gas is released from the breakdown of Hydrogen Peroxide.
Purpose: The purpose of this lab is to explore the different factors which effect enzyme activity and the rates of reaction, such as particle size and temperature.
needed to activate the reacting molecules. They are specific that usually act on only one type of substrate, so each of them just. perform one particular reaction. Furthermore, only a small amount of enzyme is needed every time to speed up a reaction. Enzymes are globular proteins that have a precise three-dimensional structure.
Use the same plate from the TSA streak. Determine if catalase is produced through the break down of hydrogen peroxide. Proceed by adding reagent hydrogen peroxide and pay attention to bubbling. In other words, bubbling takes place due to breaking down hydrogen peroxide and the fabrication of oxygen gas (Benson, 2010). The control for this test is S. aureus.
Investigate the Effect of pH on Immobilised Yeast Cells on the Breakdown of Hydrogen Peroxide
Investigating Factors that Affect the Rate of Catalase Action Investigation into the factors which affect the rate of catalase action. Planning Aim: To investigate the affect of concentration of the enzyme catalase on the decomposition reaction of hydrogen peroxide. The enzyme: Catalase is an enzyme found within the cells of many different plants and animals. In this case, it is found in celery.
How the Concentration of the Substrate Affects the Reaction in the Catalase Inside Potato Cells
Investigating the Amount of Oxygen Given Off When Catalase Reacts with Hydrogen Peroxide My aim for this investigation is to measure the amount of oxygen given off when we react catalase (enzyme) with hydrogen peroxide (substrate), this means that I aim to investigate the effect of hydrogen on the activity of catalase. Background Information Enzymes such as Catalase are protein molecules that are found in living cells. They are used to speed up specific reaction in the cell. The enzymes are all very specific as each enzyme performs one particular reaction.
Louis Jacque Thenard discovered hydrogen peroxide in 1818. Hydrogen peroxide is a common compound that people use in their everyday lives. It is a strong oxidizing agent and a weak acid. Hydroxide peroxide does not come in 100% concentrations, however, it mostly comes in concentrations of three percent, ten percent and thirty-five percent. The concentrations vary anywhere from 3% - 90%. The chemical formula is similar to the formula of water however, it has an extra oxygen atom. Its formula is H2O2. It is also known as HO-OH, dihydrogen peroxide, Hioxy and Proxy. This compound is a molecular compound as it contains two elements that are non-metals. Hydrogen peroxide has covalent bonds because unlike ionic compounds that transfer electrons, they share their electrons in order to receive a full outer shell of eight electrons.
Changes in pH lead to the breaking of the ionic bonds that hold the tertiary structure of the enzyme in place. The enzyme begins to lose. its functional shape, particularly the shape of the active site, such. that the substrate will no longer fit into it, the enzyme is said to. be denatured.
The type seen throughout the human body involve enzyme catalysis. Enzymes are present throughout many key bodily processes and keep the body from malfunctioning. An enzyme catalyzes a reaction by having the substrate bind to its active site.2 This is known as the Lock and Key Theory, which states that only the correctly oriented key (substrate) fits into the key hole (active site) of the lock (enzyme).2 Although this theory makes sense, not all experimental data has explained this concept completely.2 Another theory to better accurately explain this catalysis is known as the Induced-Fit Theory.2 This theory explains how the substrate determines the final form of the enzyme and shows how it is moderately flexible.2 This more accurately explains why some substrates, although fit in the active site, do not react because the enzyme was too distorted.2 Enzymes and substrates only react when perfectly aligned and have the same