Essay on Effect of Temperature on Rate of Reaction of Catalase

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Effect of Temperature on Rate of Reaction of Catalase


This investigation was in an attempt to try to find out how varying the temperature can affect an enzyme. The enzyme used was catalase which breaks down Hydrogen Peroxide, this gives off water and oxygen as effervescence. This effervescence is what is used to measure the reaction rate of the catalase. The optimal heat for enzyme activity is proven to be 37oC as anything above this denatures the enzyme. Denaturing is where the heat energy of breaks down the di-sulphide, ionic and hydrogen bonds that hold the tertiary structure together, this in turn changes the shape of the active site and so halts any reactions that the enzyme
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This is why the reaction rate rose with the temperature, however after a certain point (40oC), the enzymes were becoming denatured and this caused them to become useless which is why the reaction slowed to a halt after this temperature.

This was a poor experiment because:

The potato chips were very hard to get exactly the same. This inaccuracy caused the surface area to differ between chips, which means that a small linear error will make a big surface area error. To counter this, a machine should be used to cut the chips to a preset size and would be very accurate. Measuring effervescence was very inaccurate. The Bubbles tended to burst when they were made which caused the overall amount of bubbles to be inaccurate. To prevent this, a syringe could be used or the gas bubbled up through water to get an accurate measure of the amount produced. The temperature of the potato chip when it was placed into the substrate, this means that the enzymes may still be working while they are being heated to the desired temperature, so if the temperature was 80oC then the enzyme may work hard for the first minute or so because the potato is still heating up when in fact 80oC SHOULD cause the enzyme activity to become nil. This probably accounted for some anomalies we received after doing this

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