Peroxidase Experiment

Abstract
Over a two week period of time in the laboratory, we experimented and tested the reaction rate of a peroxidase enzyme and the factors that affected it, both positively and negatively. The purpose of these experiments was to probe and manipulate the activity of the enzyme peroxidase by varying temperature, pH, the amount of enzyme compared to the substrate and the effect of hydroxylamine. Peroxidase activity is expressed when the potato extract is subjected to stresses such as low temperature (El-hilali et al., 2012). The most eye catching factors that we tested for their impact on enzyme activity involved change in pH, temperature, boiling extract, and the effects of probing the active site with hydroxylamine. In the first part of
An enzyme is typically a protein with a specific three-dimensional shape. As previously mentioned above a small part of this shape forms the active site, where the enzyme combines with the substrate. The substrate actually fits into the active site, which is why enzymes are specific to the reaction they catalyze. (Campbell, N,
In regards to peroxidase, several points can be made about the overall effects of these factors. Factors such as temperature and pH have been shown to have an effect on the performance of enzymes (Vishwanatha, K.S., Food Chemistry. 2: 402-407; 2009). Adjusting the temperature will produce one of two results; if the enzymatic reaction occurs and the enzyme is colder than the optimum temperature, fewer collisions between enzyme and substrate will occur thus reducing the rate of the reaction. On the other hand, if the enzyme has been heated to a higher temperature than the optimum but not high enough to denature the enzyme, more of these collisions will occur and the reaction rate should speed up (Table 2, Graph 2). The second of the common factors is pH. Everything in the world has extremes on each end of the spectrum where the body, cell, etc. stops reacting to its environment. This goes for enzymes as well. If a solution is too basic or too acidic in comparison to the enzymes optimum pH, the enzyme will begin to degrade until it eventually stops reacting all together. It is important that students and biologists understand these and other optimal conditions for enzymes to react in. For the pH aspect of the experiment the group predicted, through reading of the laboratory manual and general knowledge of enzyme properties, that the rate would vary based on both