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Investigating the effects of Copper Sulphate on the action of Catalase Enzyme breaking down Hydrogen Peroxide.

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Introduction

Investigating the effects of Copper Sulphate on the action of Catalase Enzyme breaking down Hydrogen Peroxide By Osman Khan Lee 12 Aim In my investigation I will be trying to find out how copper sulphate affects the action of catalase enzyme, which breaks down hydrogen peroxide. This enzyme is found in potatoes. Fair Test To ensure that my experiment is a fair test I will make sure that I have only one variable at a time, which will therefore allow me to draw accurate conclusions. To do this I will keep several things the same: - Number of dimensions of each potato (i.e. the surface area). - Temperature of the reactants will remain at room temperature - Same volume of reaction mixture for each set of readings - pH level - Mixing and shaking of the reactants Diagram The diagram below illustrates the way I shall set up my apparatus, as well as a list of all the apparatus I intend to use. Burette Beaker 20ml, 10ml & 1ml Syringes Potatoes 20% Hydrogen peroxide Water 0.5M Copper Sulphate Clamp Stand Knife Tile Ruler Potato chipper Delivery tube Bung Clock Timer Simple Prediction I predict that as the amount of inhibitor in this experiment increases (copper sulphate) then the rate of the reaction will decrease. I predict this because the copper sulphate will compete with the hydrogen peroxide substrates for the active site of the catalase enzymes. As a result less hydrogen peroxide substrates will collide with an enzyme they can fuse with (due to the enzyme being occupied by a copper sulphate substrate) and therefore this will reduce the rate of the breakdown of hydrogen peroxide. In order to see how the amount of inhibitor truly affects the progress of the reaction I will keep all other potential variables the same. As stated earlier there are 5 or 6 key variables that may affect my experiment - The number of dimensions will affect the rate of the reaction. ...read more.

Middle

When the inhibitor copper sulphate is added to the reaction, instead of enzyme-substrate complexes forming, enzyme-inhibitor complexes form. This is a competitive inhibitor and as a result the rate of the reaction decreases. I predict that the copper sulphate, however, is a non-reversible inhibitor, due to the reaction slowing down so rapidly. I saw this in my preliminary results, in that even a small amount of inhibitor greatly reduced the rate of the reaction. 2Diagram showing how a non-competitive inhibitor works This diagram shows how a non-competitive permanent inhibitor works. It binds with some part of the enzyme, even though it doesn't have the same shape. In doing so the inhibitor modifies the structure of the active site. This means the substrates are no longer the correct shape to fit the active site and form an enzyme-substrate complex. As a result the reaction greatly slows down, as this enzyme is now out of use. The reason the enzyme changes shape can be explained by the reactivity series. Iron, which is present in enzymes, is displaced by the copper which is more reactive. Due to this change in structure the enzyme can not function. As well as this copper sulphate breaks disulphide bonds which are present in enzymes. It is these bonds and others which hold the specific shape of the enzyme. Due to the bond breaking the shape and structure changes, making the enzyme not function correctly. For these reasons I believe that the rate of the reaction will decrease when more copper sulphate is added. For these reasons I predict my graph will look something like the one shown below. Rate of Reaction 0ml copper sulphate 0.2ml " " 0.4ml 0.6ml 0.8ml 1.0ml Time Safety Due to hydrogen peroxide being corrosive I shall wear rubber gloves to ensure I do not spill any on my hands. I will also wear safety goggles to protect my eyes from any hydrogen peroxide that could get in my eyes and cause a big hazard. ...read more.

Conclusion

This means the temporary bonds can not form and due to this the substrate is not broken down. This is what occurred in my reaction when I added copper sulphate and is the reason for the reaction rate decreasing. It is therefore clear how enzymes function using the lock and key diagram. The key, which is the substrate, can not fit in the lock, i.e. the active site of the enzyme. As a result the door can not be opened, which in reaction terms means the reaction can not occur. The reaction between catalase enzyme and hydrogen peroxide is found in the human body. Catalase is found in the liver, and it is here that poisons are broken down. This means therefore that the hydrogen peroxide is a poison. Hydrogen peroxide is a corrosive one and would cause much harm to the body if left how it is. The enzyme is able to break up the hydrogen peroxide into oxygen and water, shown in the equation below. Hydrogen Peroxide (l) Oxygen (g) + Water (l) 2H2O2 O2 2H2O The enzyme works by lowering the activation energy required for the reaction to occur. As a result more hydrogen peroxide is converted more quickly, which means hydrogen peroxide causes less damage to our body than it could. Energy Reactants H2O2 Progress of Reaction Activation energy required without enzyme Activation energy required with enzyme As you can see from the graph above the presence of an enzyme means the activation energy required for the reaction to occur is lessened. The Ea (Activation energy) can be thought in terms of pushing a boulder up a hill. Doing so on your own is difficult and uses more energy. If however you have a shortcut the energy you require is less. This is exactly how an enzyme works- by finding a route for the reaction to occur which requires less energy. In this way enzymes speed up the rate of a reaction. 1 Diagram taken from Biology 1 Advanced Sciences 2 Diagram taken from Biology 1 Advanced Sciences ...read more.

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