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The effect of temperature on the activity of trypsin.

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The effect of temperature on the activity of trypsin. Aim To investigate the effect of temperature on the activity of trypsin, using protein coated photographic film. Apparatus * 4 cut photographic filmstrips * Trypsin solution (0.5%) * 3 test tubes * Test tube rack * Graduated pipette filler * Water bath * Thermometer * White tile * Stop watch Method 1. Set up 4 water baths at 30 C, 40 C, 50 C and 60 C. Put a thermometer in each water bath to check the temperature. 2. Set the graduated pipette at 5cm and pipette 5cm of trypsin solution into each of the 4 test tubes. 3. Place one test tubes in each of the different water baths set at different temperatures, but because there are only 3 test tubes you can use the same test tube for 30 C and 40 C. 4. Leave the test tubes in the water baths for several minutes to reach the temperature of the water bath. ...read more.


It rose from 0.003 to 0.008 making a change of 0.005. This shows that as the temperature increase the rate of reaction (measured in reciprocal) increases. This is because the temperature provides more kinetic energy to the molecules involved, which means that more collisions can occur between the enzyme and the substrate making the rate of increase. At 50 C to 60 C the rate of reaction still increases but there is not a very large change, only by 0.002. This could be due to the denaturing of the enzyme which starts above 40 C. The bonds holding the structure of the enzyme together will be broken and the active site (where reaction take place) loses it's shape and will no longer work. Hence the fact that reactions involving enzymes get slower at higher temperatures. On the graph for the class results it also shows that between 40 C and 50 C there is a very large change in the rate of reaction. ...read more.


So the rate of reaction is slower. But a higher concentration there is less competition for the active site so the whole process is quicker. There were many sources of error in this experiment as it was the first time I have done this sort of experiment. If I kept repeating the experiment then the error percentage would decrease. The enzymes being denatured also effected results of the experiment. This could be improved by using a different solution for every different temperature. When the film was dropped into the solution of trypsin, not looking /checking the film constantly could have increased the time in the experiment by a little. Checking the filmstrip for 30 C and 40 C every minute and the higher temperatures every 30 seconds could reduce this. Another error was that fact that I could not really tell when the filmstrip had gone clear. This is hard to improve but if I did experiment again I would know what to expect. Additional work could be carried out to this experiment, like repeating the experiment but using a wider range of temperatures. ...read more.

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