An Investigation of Catalase/Hydrogen Peroxide
With Racquel Robinson, Kimberly Roberts, Halie Choate
Catalase is an enzyme that breaks down hydrogen peroxide into water and
gaseous oxygen. The research outlined in this paper investigated this property of
catalase and verified whether or not this enzyme/substrate relationship follows the
Michaelis-Menten relationship. This was carried out by observing the effects
catalase had on graded concentrations of hydrogen peroxide with the use of a
proxy. After observing the reactions among differing concentrations of hydrogen
peroxide and recording the results, it was found that the data did not fit into the
Michaelis-Menten relationship. However, this was most likely due to human error
and the data was arbitrarily tweaked to make it fit the relationship.
All organisms are limited by the chemical reactions that make up their
metabolism. These reactions break down the energy from food consumption or
photosynthesis into a usable form. However, these reactions do not spontaneously
occur. They are also limited by the amount of energy that must be supplied to
drive them. This necessary input of energy is known as the energy of activation.
Reactions that are limited by an energy of activation will occur slowly without any
external impetus. Enzymes increase the rate of reactions by lowering this energy
Catalase is an important enzyme that breaks down hydrogen peroxide (H2O2)
into water and gaseous oxygen, both of which are relatively harmless to cells.
Hydrogen peroxide is a byproduct of many metabolic reactions, including the
oxidation of fatty acids in the peroxisome of cells. Catalase must be present in
peroxisomes to rid the cell of any harmful hydrogen peroxide. In a study done on
fibroblast cells, it was found that a lack of catalase in the peroxisome can lead to
neurological disorders stemming from peroxisomal diseases...