Enzyme Catalysis Lab

The purpose of this lab was to observe and understand the effects of changes in temperature, pH, enzyme concentration, and substrate concentration on the reaction rate of an enzyme-catalyzed reaction. Another purpose of the lab was to explain how environmental factors affect the rate of enzyme-catalyzed reactions.  Catalase is found in all organisms that use oxygen for their metabolism.  The enzyme is found in high concentrations in a organelle in cells called the peroxisome.  One of the functions of catalase is to prevent a toxic gathering of hydrogen peroxide in cells.  It catalyses the conversion of H2O2 to H2O and O2.  H2O2 is a by-product of metabolic processes.  It is usually produced in peroxisomes when they partially oxidize fatty acids.   When catalase is not there, the reaction it catalyzes is spontaneous, but at very low rates that are not able to reduce the harmful effects of hydrogen peroxide.

Data

Graphs and Charts

Discussion

The lab showed that the shorter the amount of time catalase spent eating away at the hydrogen peroxide the more the catalase hydrogen peroxide solution used up KMnO4 before it turned a slight hue of pink. Unfortunately our results may not have been accurate considering the first three values show a dramatic decrease, then followed by a higher forth value which causes a valley in the graph. The rest of the data points show a gradual decline in the amount of KMnO4 used as the length of the reaction time increased. So our lab did show an inconsistency from the reaction that lasted a minute, which skewed our data. However, ignoring this single plot point the rest of our data supports the statement that the longer the catalase was able to react with the hydrogen peroxide the less potassium permanganate was required to cause or emit a slight pink hue change in the solution. So in conclusion, the results of the lab support and prove what they should. How we collected data for enzyme activity, catalaseactivity, and base line assay is proven correctly. The lab is considered a success. The data we collected give the correct numbers or gave a number that is very close. The only time numbers were a little off were in the case of reading the burette when titration. The reading of the initial and final were important because it effected the percentage of spontaneously decomposes and the base line. The lab was done correctly and had right results.

 

 Reference:

"Enzyme Catalysis." Wikipedia. Wikimedia Foundation, 11 Feb. 2014. Web. 09 Nov. 2014.

"Enzymes Are Catalysts." Enzymes Are Catalysts. N.p., n.d. Web. 09 Nov. 2014.

"LabBench." LabBench. N.p., n.d. Web. 08 Nov. 2014.

"The Mechanism of Enzyme Catalysis." The Mechanism of Enzyme Catalysis. N.p., n.d. Web. 09 Nov. 2014.