This
experiment
investigated
the
effect
of
temperature
on
the
activity
of
the
enzyme
catalase
by
measuring
the
rate
of
oxygen
gas
produced
during
the
breakdown
of
hydrogen
peroxide
.
The
results
supported
the
hypothesis
that
enzymatic
activity
increases
with
temperature
up
to
an
optimum
point
,
after
which
activity
declines
sharply
due
to
denaturation
.
The
highest
reaction
rate
was
observed
at
37°
C
,
with
an
average
of
4.8
mL
of
oxygen
produced
per
minute
,
confirming
that
the
enzyme
functions
most
efficiently
near
physiological
temperature
.
Activity
was
markedly
reduced
at
10°
C
,
where
the
average
rate
fell
to
1.2
mL
/
min
,
and
at
60°
C
,
where
it
dropped
to
0.4
mL
/
min
.
This
sharp
decline
at
high
temperature
is
consistent
with
the
irreversible
unfolding
of
the
enzyme
’
s
active
site
.
A
one
-
way
ANOVA
confirmed
that
the
differences
between
temperature
groups
were
statistically
significant
(
p
< 0.01).
Several
sources
of
error
may
have
influenced
the
measurements
,
including
minor
fluctuations
in
room
temperature
,
timing
precision
,
and
variations
in
enzyme
concentration
between
trials
.
These
were
partially
controlled
using
three
replicate
trials
per
condition
.
Future
experiments
could
extend
this
work
by
testing
a
narrower
range
of
temperatures
around
37°
C
,
examining
the
effect
of
substrate
concentration
,
or
measuring
enzyme
activity
at
different
pH
levels
.
Overall
,
the
findings
demonstrate
that
catalase
activity
is
strongly
temperature
-
dependent
,
with
peak
performance
at
37°
C
and
a
rapid
loss
of
function
outside
the
optimal
range
.
The
results
align
with
established
biochemical
principles
and
provide
a
reliable
basis
for
further
study
of
enzyme
kinetics
.
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