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The effect of temperature on enzyme activity

The hypothesis, aim, methods, results, conclusion and discussion of an experiment showing how changing the temperature effects the activity of trypsin.

Molly B

on 10 December 2012

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Transcript of The effect of temperature on enzyme activity

HYPOTHESIS AIM METHOD RESULTS The higher the temperature will be, the quicker the solution will become clear, and so the rate of reaction will increase. Although when the temperature becomes hotter than around 30°c (37°c being the peak), the rate of reaction will decrease due to the denaturing of the enzyme. To record the time taken for a suspension of casein mixed with trypsin to become clear for different temperatures, and therefore investigate how temperature effects the rate of reaction between an enzyme and substrate. DISCUSSION The effect of temperature on the activity of the enzyme, trypsin 1) Set up a water bath at 15°c 2) Pipette 3cm^3 of casein suspension into one test tube and 3cm^3 of trypsin solution into another tube 3) Stand both tubes in the water bath and leave them for several minutes to reach the temperature of the water bath 4) Meanwhile, set up a control tube containing 5cm^3 of casein suspension plus 5cm^3 of distilled water. Stand this tube in the water bath 5) Mix the enzyme and substrate together but don't put back into the water bath 6) Observe the contents of the tube carefully, checking against a piece of card with a black cross, and record the time taken for the suspension to become clear 7) Repeat this procedure at temperatures of 30°c, 50°c, 65°c and 80°c. Use the same volumes of casein suspension and enzyme solution each time. Table Graph CONCLUSION The results show that, at first, as the temperature increased, the time taken decreased, resulting in the rate of reaction increasing. Although after 30°c, the time taken increased, therefore the rate of reaction decreased. POSSIBLE SOURCES OF ERROR, HOW COULD THEY BE RESOLVED? The time taken to see the cross could have been judged differently as different people were recording when the cross was visible. This could have been improved by using the same person to judge when the cross was seen, or even better, a light meter. As the test tubes were removed from the water baths to put in the enzyme and check against the piece of card, the temperature of the solution in the test tube would not have stayed constant and so would have affected the rate of reaction. This could have been improved if a laminate/water proof piece of card was used to check when the suspension became clear.
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