The influence of Temperature against the enzyme activity

experiment results Of our group,

on the first ball of tube di gelas chemical contains the ice does not
occur with changing colours on the test and test benedict iodium. This
is caused by an enzyme in the low temperature State of the stalled are
reversible so there is no occurrence of hydrolysis in starch and
necessary changes does not occur
colors.

On the second tube is stored at room temperature changes the color in

the second test. This occurs because at room temperature temperature
increase environment will meningkatakan of enzyme kinetic energy and
frequency of collisions between molecules of the enzyme and the
substrate, so that the enzyme is active and this activity that causes the
starch can be hydrolyzed so that changes color on both the
test.

On the third tube put the water bath 37-40 c-temperature also changes
the colors in the second test. This caused the enzyme has optimum
temperature 30-40 c so that at a temperature of maximum enzymatic
activity is running so that it can hydrolyze starch that makes test
changes on both the color of

. On the fourth tube is inserted into a water bath-temperature 75-80 c of

the second test which changes color. This occurs at a temperature so
the enzyme undergoes denaturation temperature which in such early
changes before the temperature rise prosesdenaturasi can increase the
speed of reaction, but the temperature increase at the time of the
occurrence would denaturation process start to reduce speed
reactions. This also happened on the tube

fifth. Conclusion
based on experiments that have been done, then it can be inferred that
the optimum temperature for amylase enzyme is 100 0 c

. 1. optimal enzyme Temperature 370C 600C is approaching the next

enzyme increased enzyme will undergo denaturation while approaching
the freezing point of the enzyme
is not active.
2. The influence of pH can be known with the formation of sediment with
the addition of the reagents benedict. the pH optimum of the enzyme
depending on the pH of the tissue around the enzyme there. But in
General, the pH of the enzyme was about 6-8.

3. The influence of the concentration of the enzyme can be seen from

the number of deposits after the change of reagents benedict. The
greater the concentration of the enzyme is getting higher enzyme
activity in breaking down the substrate catalyzed. In these experiments
that have the most optimum enzyme concentration is 0.5 ml.
4. The influence of substrate concentration can be seen with the
formation of deposits after the addition of the reagents benedict. The
substrate concentration is directly proportional to the speed of the
reaction to the maximum extent. If passing through a maximum addition
of substrate has no effect. In this experiment the enzymes which have
the optimum concentration of substrak is 1 ml.

2.2. The influence of pH of the Enzyme

Activity

From taking action against the results of

the experiment our group,
first on the tube with the addition of HCl
to 1 after berpH tested with iodium
solution changes color to Orange, yellow,
yellow, clear and turbid with sediment
formed green benedict test is easy,

the second on the tube with the addition

of aquades when it is tested with a
solution of iodium changes color to orange
and old test benedict formed complex
blue color nodes third, while on the tube
with the addition of Na2CO3 are berpH 14
after tested with a solution of iodium
formed the old orange and complex test
benedict formed deposits of orange. Here
our group experienced an error in the
amount of solution is lacking. In this
experiment is supposed to be on the
second tube blue complex formed with
test solution due to enzyme activity
shows iodium when maximum at pH
optimum, generally between pH 6-blue
complex formed 8.0 will be formed due to
hydrolysis in starch and on test benedict
will form deposits of red brick because
this disebabakan because of aldoses or
ketoses are in the form of a cyclic, which
means that they are in the form of
kesetimbangannya with a small number of
open-chain aldehyde or ketone cluster,
therefore it is an aldehyde or ketone is
able to reduce various kinds of reducing
agents which means starch hydrolyzed.
While the first and third tube is negative
because the enzyme undergoes
denaturation at low or high pH, which
causes a decrease in employment of
enzymes. Then test with a solution of
iodium and reagents benedict will not
produce positive results because it is not
the occurrence of

hydrolysis. Urease

DISCUSSION on the tube A, mixed with 1

ml of a solution of urine plus 2 drops of
phenolphtalein indicator and 10 drops of
soy suspension. The results of the
solution can show the color red
mudakarena enzymes work menguraian
ureum in urine into ammonium carbonate
bersifatbasa/alkalis, so when tested with
phenolphtalein indicator will show the
color pink which means pH range between
8.3-10.0 (alkaline/alkalis).
On the tube B, mix with 1 solution of urine
plus 2 drops of the phenolphtalein
indicator and 10 drops of soy that has
been heated suspension. The results of
the solution remains white, because the
enzyme that outlines the ureum be
ammonium carbonate is not functioning
properly, it inidikarenakan enzyme which
acts as a mediator has been
damaged/denaturation at high
temperature
. On the tube C, mixed with 1 ml of urea
solution plus 2 drops of the phenolphtalein
indicator and 10 drops of soy suspension
then added 10 drops of aqueous solutions
of HgCl2. results showed white anger
because the enzyme works by the
influence of minimum sangan sublimat
inhibitors. This is because ammonia
formed very slightly so that it does not
provide significant enough colour change
and presumably not pH changed
significantly as well. HgCl2 is a heavy
metal that can inhibit the enzyme work
irreversibel non-competitive. The Hgcl2
working with disturbed the enzyme
cofactors side so that the enzyme is not
activated and the reaction failed to take
place. However some enzymes that do not
bind to these inhibitors will be activated
and the outlines of urea into the
amoniumkarbonat can show little change
in color by

phenolphtalein indicator. conclusion

Enzyme urease urea revamp into
 ammonium carbonate and carbon
dioxide ...

Indicator indicates the presence of

ammonium carbonate PP with colorless
darilarutan shows the changes into a red
solution (is alkaline/alkalis).

of the enzyme urease can

damage/denaturation at high
temperature

Urease enzyme can be inhibited by a

heavy metal one is sublimat


Have a Better Translation?

On the tube 1, extract plus H2O2. When

extracts are given the H2O2, gelumbung-
air bubbles occur. This proves that the
enzyme catalase found in chicken liver
changing H2O2 into H2O or water, while
at the time included coal rib into it, arose
the coals. This proves that H2O2 also
elaborated into
O2. In an atmosphere of any liver showed
the presence of the enzyme catalase,
except the high-temperature atmosphere.
It's just a neutral atmosphere in the heart
of more optimal than the atmosphere of
other shows. Comparison of resistance of
the enzyme Catalase in various
atmosphere are: acid (1): base (3): low-
temperature (2)

Turmeric extract plus 1 tube of solution of

H2O2. The result was a bubble has
occurred and flames but very little

Tube 1 papaya leaf extract plus H2O2. The

result arising bubbles and flame
. Papaya leaf extract is the most variable
Enzyme Katalasenya good compared to
other variables. This is evidenced when
we tested the enzyme Catalase in papaya
leaf extract in any atmosphere always
showed the most good embers (light) this
means the O2 products in high papaya leaf
extract. It's just that in high temperature
extract of papaya leaves did not show the
presence of the enzyme Catalase.

. Catalase enzymes will break down at

 high temperatures.
2. Factors affecting the work of the
enzyme catalase is temperature, pH,
enzyme concentration
. 3. The enzyme catalase was
instrumental in unravelling the poison of
H2O2 into H2O and O2
