Analyzing the results
Here is a table of the Michaelis-Menten parameters you calculated:
Preservative |
Vmax |
Km |
none |
0.1 |
1.25 mM |
PHBA |
0.1 |
2.50 mM |
phenylthiourea |
0.05 |
1.25 mM |
Here are the Michaelis-Menten graphs of for each of these sets of parameters:
graph
One of these preservatives works by disabling the enzyme itself. The other preservative works by competing for the active sites on the substrate. Can you tell which is which?
If a preservative (partially) disables an enzyme, would you expect the maximum rate of the reaction to stay the same, increase, or decrease?-> imagine the enzyme chained to a heavy weight or beat up by a schoolyard bully. Clearly it won't be able to work as fast as before, so Vmax should decrease.
If a preservative competes for binding sites, would you expect the maximum rate of the reaction to stay the same, increase, or decrease? -> If the amount of substrate was infinite then it wouldn't matter that there was a competitor out there, so Vmax should stay the same
If a preservative (partially) disables an enzyme, would you expect to reach half of Vmax with the same, less, or more of the substrate? ->
If a preservative (partially) disables an enzyme, would you expect to reach half of Vmax with the same, less, or more of the substrate? ->
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