Catalase Lab
From performing the pH experiment it has proven that pH buffer 7 is the optimum pH for catalase in potatoes. This is because the height of the bubbles was the highest of all three tests (pH 3, pH 7, pH 9) reaching an average height of 0.433 cm. See graph 3. While pH buffer 3’s average height was 0.233 cm only reaching a maximum height of 0.3 cm in Trial 3 and pH buffer 9’s average height being 0.333 cm only reaching a maximum height of 0.4 cm again in Trial 3. See table 1.
Therefore this supports my hypothesis: At pH buffer 7 the enzyme (catalase) will work most efficiently because at pH levels too high or too low will cause the enzyme to denature, because they alter the charged groups of amino acids that make up the active site causing certain ions to be attracted and cluster around the negatively charged group, therefore interfering with the binding of substrate and changing the rate of activity of the enzyme.
This is, because the ions that have clustered around the negatively charged amino acid group, that are in the active site, distort or change the shape of the active site therefore the substrate will …show more content…
See table 1. This does prove accuracy within the three trials (the height of bubbles produced is within this small range), however would have to keep in mind that this could also be from reading and recording the height incorrectly. More trials could be performed however to ensure accuracy.
My hypothesis for the temperature experiment was also proven correct: The enzyme activity will be at it’s highest/best when the temperature is 60oc, which is the temperature of boiled water in this experiment, because increased temperature increases the kinetic energy of the enzyme’s molecules causing there to be less time between collisions, resulting in more molecules reaching activation energy, which increases the rate of
Therefore this supports my hypothesis: At pH buffer 7 the enzyme (catalase) will work most efficiently because at pH levels too high or too low will cause the enzyme to denature, because they alter the charged groups of amino acids that make up the active site causing certain ions to be attracted and cluster around the negatively charged group, therefore interfering with the binding of substrate and changing the rate of activity of the enzyme.
This is, because the ions that have clustered around the negatively charged amino acid group, that are in the active site, distort or change the shape of the active site therefore the substrate will …show more content…
See table 1. This does prove accuracy within the three trials (the height of bubbles produced is within this small range), however would have to keep in mind that this could also be from reading and recording the height incorrectly. More trials could be performed however to ensure accuracy.
My hypothesis for the temperature experiment was also proven correct: The enzyme activity will be at it’s highest/best when the temperature is 60oc, which is the temperature of boiled water in this experiment, because increased temperature increases the kinetic energy of the enzyme’s molecules causing there to be less time between collisions, resulting in more molecules reaching activation energy, which increases the rate of