CONCLUSION

Enzymes are protein molecules, also

known as biological catalysts that lower the
needed activation energy for reactions to occur at
rates that are suitable for systems to carry out. In
this experiment, amylase enzyme was used and
analyzed. Amylase is a digestive enzyme that is
mainly found in the saliva of many organisms. It
breaks down large polysaccharides such as
starch, particularly catalyzing the hydrolysis of α-
1, 4-glycosidic linkages of these polysaccharides
to yield maltose, D-glucose and
oligosaccharides.

In the study of enzyme kinetics,

Michaelis-Menten and Lineweaver-Burk
equations are used to demonstrate the
relationship between substrate & enzyme. Rate
of reaction was not entirely dependent on
substrate concentration but, they can act only up
to a certain concentration when all enzyme
molecules are attached and acting on substrate
molecules and then work in a rate that never
surpass the maximum velocity, Vmax, even when
the substrate concentration increases. The rate of
enzymatic reaction can be followed through
monitoring and measuring the rate of products
appearance or disappearance of substrates.

The Michaelis constant, Km, is used to

describe the affinity the enzyme to its substrate.
The Km value is inversely proportional to the
affinity of enzyme to its substrate. Small value of
Km indicates that the affinity of enzyme to its
substrate is weak and it only requires small
amount of substrate to become saturated. Hence,
the Vmax is reached at relatively low substrate
concentrations. While a large Km indicates a
higher affinity of enzyme for its substrate and it
requires a high substrate concentration to
achieve Vmax.