Factors that affect enzyme action

The efficiency and activity depend on the tertiary structure of the enzyme (held together by weak
intermolecular bonds). Factors that affect these bonds impede the efficiency of the enzyme.
Enzyme concentration:
- To compare the rate of reaction of several solutions with different enzyme concentrations, one
must consider only the initial rate of reaction (at the beginning). This is because once the
reaction is under way, the amount of substrate in each reaction begins to vary as each
reaction converts substrate to product at different rates.
- Initial rate of reaction is directly proportional to enzyme concentration, provided that substrate
is in excess, because the more enzyme molecules, the more active sites can be filled at one
point in time.
Substrate concentration:
- Vmax: The point at which the enzyme is working at its maximum possible rate.
- The progression of the rate of reaction - substrate concentration graph:
At first, there are few substrate molecules and many active sites free. An increase in
substrate concentration will increase the rate.
Then, there are many substrate molecules and many active sites are occupied. So, the rate
of reaction cannot increase as rapidly.
Finally, there is an excess of substrate molecules, all of the active sites are engaged, and an
increase in substance concentration will not change the rate as it has reached Vmax.
Temperature:

- At low temperatures (around 0) the rate of enzyme catalysed reactions is very slow
because:
1. The molecules have low kinetic energy (low speed) and do no collide frequently.
2. When the molecules do collide, they do not possess the activation energy required for the
reaction to occur (like in fridges).
- Between 0 - 40 The rate of enzyme activity increase almost linearly because the molecules
gain kinetic energy (so they collide more frequently) and they have a greater energy than the
activation energy needed.
- For most enzymes, 40 is the optimum temperature. The optimum temperature is the
temperature at which enzyme activity is at its maximum and not all enzymes have the same
optimum temperature (e.g. optimum temp. for organisms in hot springs and deep sea thermal
vents can be 80).
- After the optimum temperature the rate of reaction begins to decrease because as the
molecules in the enzyme gain kinetic energy they begin to vibrate more, breaking
intermolecular bonds (especially hydrogen bonds). This causes the enzyme to be denatured
as its active site changes shape and substrate molecules can no longer fit.
pH:
- Most enzymes have an optimum pH of about 7.
- pH is a measure of the concentration of hydrogen ions.
- Changes in pH can cause the denaturation of the enzyme by changing the precise 3D shape
of the enzyme. This is because pH affects the ionisation of the substrate molecules or the R
groups of the amino acids in the active site, reducing the activity of enzymes by breaking
down ionic bonds.