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The Effect of Temperature on the Rate of Reaction of the Enzyme Catalayse and Hydrogen Peroxide

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Wednesday 17th January 2001 The Effect of Temperature on the Rate of Reaction of the Enzyme Catalayse and Hydrogen Peroxide; Aim; The effect of temperature on the rate at which enzymes work. Method; We set up the experiment as shown; Based upon a preliminary experiment we have decided to carry out the experiment as shown... 1. Extract the enzyme catalayse from 2g of celery by crushing with a pestle and mortar and adding 2ml of water. 2. Heat a water bath over a Bunsen burner until it reaches the desired temperature. This temperature will be maintained until the water is needed. 3. We will then place 5ml of H2O2 into a conical flask using a pippet and measuring cylinder. This chronicle flask will then be placed into the water bath, which has now been taken of the heat. 4. While the heat is equilibrating between the two liquids to the desired temperature (e.g. 50� C), we will fill an ice cream tub with water and invert a measuring cylinder full of water into the tub. 5. We will then add the celery paste containing the catalayse (which we crushed up in stage 1) into the conical flask containing the substrate H2O2. After doing this we will quickly place the cork (with a tube running through it) into the conical flask and quickly insert the delivery tube into the inverted measuring cylinder in the ice cream tub. 6. The reaction will then take place and the oxygen given off will then travel through the tube displacing the water in the inverted measuring cylinder. We will record the results on the basis of how much oxygen the reaction produces after a certain amount of time. Apparatus; * Bench mat * Celery (Containing the enzyme catalyse) * Conical Flask * Cork * Delivery tube * Gauze mat * Hydrogen Peroxide * Ice cream tub * Pestle and mortar * Pippet * Thermometer * Timer * Tripod * Two measuring cylinders * Water * Water bath (beaker) ...read more.


The rate of reaction will now be beginning to increase slowly between 10-20�C but then begin to react faster between 20-30�C. I think that the optimum temperature would be between 30-40�C (which is known as the steady state phase). I think this because within our bodies we have many different enzymes which all work at 37�C, as this is the temperature of the inner body. Beyond the optimum temperature I predict that the rate will begin to decline, this will be between 50-60�C. beyond 60�C I predict that the enzymes will denature, as the temperature will be too hot. The following uses the particle theory along with the active site and substrate theory to explain clearly why I think the catalayse would react in this way relative to how the temperature increases. Scientific Explanation; Active Site and Substrate Diagram; Biological catalysts speed up all reactions, which take place within our bodies and in all other organisms. These biological catalysts are made of proteins and are called enzymes. Enzymes are specific because each different reaction needs a different type of enzyme. This is what the above diagram shows. It illustrates how the active site of catalayse is specific to the substrate Hydrogen peroxide that will then brake down into two products; these are water and oxygen. This is the reaction that the enzymes participate in. At low temperatures the enzymes have less energy and so are less active. This means collisions between the catalayse and the H2O2 are lesser along with the reaction rate. Although as the temperature increases towards 50�C, reactions are faster and stronger causing the active site to deform, and no longer be compatible with the H2O2. This causes the enzyme to denature and no longer react. The following diagram illustrates this Results: When we carried out our experiment everything went to plan although a few anomalous results cropped up, but this was expected which is why we repeated each experiment three times to achieve a more accurate and common result. ...read more.


We used intervals of 10�C whereas if we had used 5�C intervals we would have had more results from which we would have had more plots on the graph. From these plots on the graph it would have enabled us to sketch and estimate a line of best fit, which would be more accurate and similar to the enzyme pattern. Our method could have been improved for accuracy of readings by getting better equipment such as measuring cylinders that go to a greater degree of accuracy. We could also have used pure catalayse if it is possible. Another point that could have improved our method is that when we heat the hydrogen peroxide to the desired temperature within the conical flask it defies the point of the experiment. This was to find out the effect of temperature upon the enzyme catalayse. So maybe instead of just heating the hydrogen peroxide we should have heated the catalayse as well, this may have given us more accurate results. This is because when we add the heated hydrogen peroxide to the unheated catalayse the reaction takes place almost immediately so the enzyme may not be under the full effect of the H2O2 temperature. I could not have obtained additional evidence from the information I had access to. After using this graph in my prediction and seeing that it proved to be accurate I can say that this graph is correct and should apply to most enzymes. So I could say that this could be a law, which explains the common pattern of an enzyme under the effect of temperature: Although this law only applies to one of the two variables which I listed in my planning on page 3. So to extend the enquiry I could look at the other factor, which was to experiment the effect of pH or the effect of substrate upon, enzymes and then I could also apply these experiments to other enzymes within other plants or even animals. By rajiv pudaruth 1 ...read more.

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