An Observation of Potato Enzyme, Peroxidase, Activity
May 27, 2014
Lab Instructor: Mr. Johnathan LaCombe
A class of biology students at Indiana University Purdue University Indianapolis recently constructed a series of experiments to measure the activity level of potato root enzyme, peroxidase. The purpose of the experiment was to observe and measure the enzyme activity, as a rate of reaction, when different levels of the variables are introduced. The experiments introduced four variables (enzyme concentration, substrate concentration, pH buffer, and enzyme inhibitor). The findings, though varying in absolution on 2 of the experiments, are fairly in-line with hypothesized outcomes, yielding a linear correlation for enzyme activity in both the substrate and enzyme concentration experiments, and an assumed, but not definitive correlation for both pH buffer and enzyme inhibitor experiments.
Enzyme, Substrate, Buffer, Spectrophotometer, Oxidize, Concentration, Inhibitor
Enzymes are protein molecules that govern virtually all cellular activities in living organisms.
These biological catalysts convert a specific substrate into one or more products without being changed themselves. The general approach for enzyme activity is as follows. The enzyme preparation is mixed with a substrate at a controlled temperature and pH and incubated for a suitable period. The progression of the reaction can be measured in a variety of ways. One way is to choose a substrate for a particular enzyme that produces a colored product that can be easily observed by the investigator and measured with an instrument such as a spectrophotometer. The more product formed, the higher the absorbance, and the higher the reading on the spectrophotometer. (Marrs, 2014)
The purpose of the experiment was to observe and measure the enzyme activity when different levels of the variables were introduced, thus providing additional information about the nature of the enzyme when such variables...