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Abstract
In lectures leading up to the experiment, it was stated clearly that variations in pH, temperature and substrate concentrations has profound effects on enzymes. This practical not only re-enforced these ideas, but explores the chemistry behind it. The idea of an enzyme denaturing after it has reached its optimum pH or temperature was clearly indicated by the first and second part of the experiment. The second part of the experiment also brought out the idea of the relationship between temperature and enzyme activity, which has been discussed as been inversely proportional to a certain point. Another useful concept drought into play is Michaelis-Menten's saturation curve, which states that as enzyme concentration increases so does the substrate concentration, which creates a saturated solution. The basis of this report will explore the concepts mention above.

Introduction
It is the common understanding to those in the science field that the activity of an enzyme is strongly effected by the pH, temperature and the changes in concentration of a substrate. Reflecting back on lectures it is safe to say that changes in pH alter the ionization of the charged amino acid, whereas changes in the temperature creates an unstable protein from increased kinetic energy, which in both cases results in the formation of a denatured species. The aim of this experiment was to reinforce the theory and to analyze the effects of pH, temperature and the effect of increasing the substrate concentration of an enzyme. Having said that, one needs to reflect back to the effect of substrate concentration of enzymes and put to use Michaelis-Menten's curve, which states by experimental calculations that keeping the amount of enzymes constant would gradually increase the substrate concentration of the given reaction.

The idea of increasing the pH was demonstrated in the first part of the experiment. Pre-incubating the test tubes starts the optimization period, this part of the...