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Collision Theory
Effect of Temperature on
Enzyme Activity
As we can see from the graph at low temperatures the rate of reaction is
very slow. This is because particles absorb less Kinetic Energy so move
relatively slowly. Therefore, substrate molecules will not collide with the
active site so the substrate at a fast enough rate.
As temperature increases, i.e. on the graph from 20 to 40 degrees the
collisions happen more frequently as molecules absorb more kinetic
energy therefore move faster. These molecules can then enter the active
site more often as they have more energy. This makes it easier for bonds
to be formed or broken by the enzyme, therefore a faster rate of reaction.
At 40 degrees we can infer from the graph that this is the optimum
temperature, the maximum rate of reaction.
After 40 degrees however we see a decline in the rate of reaction faster
than the rate increasing at the beginning. This is because at a
temperature which is too high the hydrogen bonds in the enzymes begin
to break causing the tertiary structure of the enzyme to change this is
Def: pH is the power of hydrogen. The lower the pH the more acidic it is.
From the graph we can a symmetrical graph in which the rate of reaction
increases as pH increases is equal to the rate of reaction decreasing when
the pH is too alkaline. The optimum pH for most enzymes as seen in the
graph is 7. There are exceptions such as in the stomach where the
optimum pH is around 1-2.
Hydrogen ions can interact with the R groups of the amino acids
therefore affecting ionization. This affects the ionic bonding within the
group which can affect the tertiary structure of enzymes. The shape of an
active site can change which reduces the chances of collisions. It could
also denature enzymes.