Boiling denatures the enzyme, but freezing has no effect.
At
high temperatures (even if it’s not boiling, about 60°C is enough) hydrogen
bonds and other interactions between different amino acids of an enzyme are
broken. This is not degradation, no bonds are broken – only interactions
(London, Van der Waals, etc). This makes the protein to denature, which means
it will lose its 3D shape and become linear – no longer globular: it only
preserves its primary structure. This makes the enzyme to become useless: it
can’t make the substrate become product anymore. So the activity becomes
practically zero.
Freezing
DOES make a change in enzyme activity, but for other reasons which are not
denaturing (the enzyme has the same structure as before):
-Concentration:
Now some of the water has become ice and you have 2 phases, which are the
solution and the ice. So the solution has less water, and so a higher
concentration. Higher concentration means… higher activity! So it has the same
structure, but it works more.
-Cell
disruption: Membranes are broken and this will release molecules that used to
be stored in an organelle. Sometimes this makes the enzyme find the substrate –
so it actually increases activity! As I said for concentration, this means the
enzyme has the same structure but it works more.