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An Experiment To Investigate The Effect Of Temperature on The Action Of The Enzyme Trypsin On Casein

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AN EXPERIMENT TO INVESTIGATE THE EFFECT OF TEMPERATURE ON THE ACTION OF THE ENZYME TRYPSIN ON CASEIN APPARATUS Casein suspension, 4 per cent; Trypsin solution, 0.5 per cent; Distilled water; Test tubes and rack; Water baths; Graduated pipettes or syringes Thermometers; Black card; Electronic timer; Marker pen, INTRODUCTION Casein is a protein found in milk. When a suspension of casein is hydrolysed, the suspension starts cloudy but becomes clearer as the products dissolve. This hydrolysis is catalysed by proteolytic enzymes such as trypsin. The aim of this experiment is to investigate the effect of temperature on the activity of trypsin, using a suspension of casein as the substrate. Changes in the clarity of the casein suspension will be easier to see if the tubes are checked periodically by holding them against a piece of black card. METHOD Set up the water baths with thermometers and maintain one at room temperature, one at 25�C, 35�C, 45�C, and 55�C. ...read more.


Each time a new control should be made up, and the same volumes of the Casein suspension and Trypsin solution. RESULTS TEMPERATURE OF WATER BATH (�C) TIME TAKEN TO BECOME CLEAR (SECONDS) 22.0 (Room temperature) 79.11 25.5 63.23 35.5 28.19 45.0 12.09 55.0 34.03 The table below is of the temperature of the water bath and the inverse of the time taken for the solution to become clear (which gives the relative rate). POINT TEMPERATURE OF WATER BATH (�C) RELATIVE RATE (T-1) 1 22.0 (Room temperature) 0.013 2 25.5 0.016 3 35.5 0.035 4 45.0 0.083 5 55.0 0.029 CONCLUSION The first graph shows the time taken for the solutions to become clear at the different temperatures. It shows a parabola and there is an almost inversely proportional relationship between 20�C to about 40�C. The second graph uses the principle that the inverse of the time taken gives the relative rate for the enzyme. The control test tube was set-up as to be used as a comparison between it (the original clarity) ...read more.


As a result the rate is seen to decrease. At a temperature of 25�C it takes 63 seconds where as at a temperature of 35�C it took 28 seconds. For temperatures above the said optimum temperature, rate is reduced as enzymes are now becoming denatured, that is the loss of shape, and hence the ability to catalyse the reaction. At a temperature of 45�C it takes 12 seconds where as at a temperature of 55�C it took 34 seconds. The graph or relative rate against temperature shows a 'finger like projection' with a peak at 450C. In order to further investigate this relationship it would be interesting to see the effects at a wider range of temperatures for example up to 800C. This could possibly produce a bell shaped curve. The significance that the optimum temperature of 45�C, is significant in that this is the temperature that can be found in most homiothermic mammals (mammals that maintain a more or less constant body temperature), where the modification of the protein Casein (here results in the solution becoming clear) occurs. This shows that the enzyme works best in conditions that are similar its native environment. ...read more.

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