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EFFECT OF PH ON AMYLASE ACTIVITY 2
Introduction
Chemically, enzymes are protein in nature and act as catalysts for the chemical reactions
that occur in living organisms (Adams, 2003). They attach themselves to slots on the substrates
called active sites to speed up a particular chemical reaction. There are different types of
enzymes each with a particular reaction in which it catalyses. Once the reaction is complete, the
enzyme de-touches from the substrate and attaches to another one for the same reaction. Adams
(2003) argues that the enzyme amylase found in saliva, helps to speed up or catalyzes starch
hydrolysis. Due to the fact enzymes are substances that are protein in nature; their structures
(Secondary and tertiary) are affected by pH, presence of heavy metals ions like zinc and
temperature. The activities of enzymes are linked with their structure. Therefore, any change in
the tertiary or secondary structure affects enzyme activity The Concentration of hydrogen ion
referred as pH in a solution affects the three dimensional structure of an enzyme just the same
way the temperature affect enzyme. This greatly affects the functions of an enzyme. A good
number of enzymes perform better near neutral pH ranges. Those found in the stomach of human
beings requires acidic pH to perform better while some others requires a basic PH ranges. This
experiment will examine the effect of pH on the activity of Amylase (Adams, 2003)
For this experiment, the following materials were used; 6 test tubes, 5.0ml distilled water,
4.0ml starch solution, 6ml pH buffers (3, 5, 6, 7, 8, and 9), 10ml amylase solution and 5ml iodine
solution were used. The mixture of starch and the amylase solution was put in the test tube
containing distilled water and different pH buffers ranging from 5 to 9 in each tube. The time for
the reaction to take place and the color to change in each of the test tubes was recorded to
Results
Figure 1 Table showing the PH, time, starch concentration and reaction rate
Tube Labeled A B C D E F
PH 3 5 6 7 8 9
Reaction rate(mg/ml per min) 0.0055 0.037 0.033 0.018 0.0032 -0.0006
In the table above, the rate of reaction increases from pH 3 up to the pH 5 and then decreases
steadily up to the pH of 9.0
0.045
Reaction Rate(mg/ml per minute)
0.04
0.035
0.03
0.025
0.02
0.015
0.01
0.005
0
-0.005 0 2 4 6 8 10
pH
Source: Adam, P., ed. (2003). ‘Molecules, Cells and Genes subject guide’, University of
NSW: Sydney.
EFFECT OF PH ON AMYLASE ACTIVITY 4
According to the graph above, there is a considerable sharp increase in reaction rate from
from the pH of 5.3 up to a pH of 8.0 and there is a dramatic less decrease after the pH of 8.0.
Discussion
In figure 2 above, the optimum Amylase pH is 5.3 which is quite acidic. The alkalinity
and acidity of the activity of enzyme with respect to the environment depend on enzyme
characteristics. Every enzyme has its optimum pH where the activity of the enzyme peaks. In
acidic environment, the rate of reaction increases to a pH of 5.3 and decrease there after.
Conclusion
This experiment showed that enzymes are very important substances that catalyze
chemical reactions in living cells of living things in ensuring food is digested and assimilated
into the body system. The conditions of the cell should however be conducive for the proper
functioning of enzymes because extreme condition of pH affects the rate of chemical reactions.
The pH in a solution affects the three dimensional structure of an enzyme just the same way the
temperature affect enzyme. This greatly affects the functions of an enzyme. A good number of
enzymes perform better near neutral pH ranges. Those found in the stomach of human beings
requires acidic PH to perform better while some others requires a basic pH ranges. From the
experiment the optimum pH of amylase is 5.3. Since all the enzymes have the same
characteristic and function in the cell, it is expected that the findings of this experiment can be
applied to other enzymes which may be catalyzing different reactions in the cell.
EFFECT OF PH ON AMYLASE ACTIVITY 5
References
Adam, P., ed. (2003). ‘Molecules, Cells and Genes subject guide’, University of NSW:
Sydney.