Investigation into the factors affecting the rate of enzyme reactions.

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Karl Long Biology Coursework

Biology- Investigation into the factors affecting the rate of enzyme reactions

Aim- we are going to investigate the concentration of pepsin affecting the rate of reaction between pepsin and albumen (egg white).

Variables-

  • Concentration- This affects the rate of this reaction because if there is more pepsin molecules within the mixture then there is more chance of collisions between pepsin and albumen molecules, which in turn increases the chance of the active site slotting on to the enzyme.
  • Temperature- this affects the rate of reaction because different enzymes work best at different temperatures with the usual temperature being37.2°c. If the temperature varies too much then the enzyme will not work to its full potential. As the temperature rises the enzymes begin to denature (deform so active site does not fit enzyme). The changes caused by denaturing are usually reversible but if they are too extreme then the changes are irreversible.
  • pH- the pH affects the rate of reaction because the enzymes all work best at specific pH’s depending on where they are used.

Prediction- I predict that as the concentration increases so will the rate of reaction, I believe this because as the concentration increases the number of pepsin particles will increase making the chance of a collision and the active site slotting on to the enzyme.

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Scientific Theory- In this experiment our aim is to test the rate of reaction under certain conditions. Enzymes are biological catalysts, i.e. they speed up a reaction without being used up. Enzymes work best at specific temperature and pH’s. They work best at 37.2°c and depending on where the enzymes work different pH’s. Pepsin the enzyme we are testing works best at pH 2. Each enzyme uses a lock and key system meaning they fit on the substance they are meant to break down and only that substance. Some examples of enzymes and its substrate are:

Proteins- Protease

Carbohydrates- ...

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