Solanum Tuberosum Catalase Lab Report

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Measuring the Average Catalase Reaction Times of Solanum tuberosum Supernant in Hydrogen Peroxide

Julie Fitzgerald
Delano Woods

Biology 103: Botany
Professor Silady, Smith
February 23, 2017
INTRODUCTION
This investigation is geared towards observing the enzyme reaction times in Solanum tuberosum, also known as the common potato, depending on the temperature of the catalase. During the lab, students tested the reaction times of the catalase when placed in hydrogen peroxide when the supernant was at room temperature and heated. In this experiment, it is hypothesized that when the supernant is heated above room temperature the catalase-substrate decomposition reaction rate would be faster, therefore, decreasing the time taken for
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To start the procedure, one must first place a chunk of Solanum tuberosum into a mortar. Next they must add a small amount of sand, approximately one-half of a teaspoon or less, and approximately 1-mL of pH 7 buffer on top of the plant material in the mortar. The student must then grind the material until a watery paste has formed. Fill a microcentrifuge tube with the watery potato paste, place in a balanced microcentrifuge, and spin at approximately 10,000 RPM for 30 seconds. Remove the tube and make sure a pellet has formed at the bottom of the microcentrifuge tube. The student must then transfer the clean, separated, catalase-containing supernant (liquid) into a new microcentrifuge tube. To test the reactivity of the catalase recently separated from the material taken, the student must first punch out paper discs from filter paper. Please make sure the filter paper discs are handled with clean forceps to ensure sanitary practices and accuracy within the experiment. Gently dip a paper disc into the supernant using forceps and drop into 50-mL of a 3% hydrogen peroxide. Record the time it takes for the disc to rise to the top, remove used disc, and repeat for an entirety of 10 times, then change the hydrogen …show more content…
We can conclude that the reaction time increases with an increase in temperature, according to what our results have shown. One could say it is potentially because our room temperature could be the optimum temperature for this reaction to occur with the given plant’s catalase. In Preety and Hooda’s (2014) study, of immobilization and kinetics of catalase on calcium carbonate nanoparticles, her results showed that both enzymes showed an optimum temperature of 35C (p. 122). One could also say our hypothesis was falsified from the possibility the supernant was heated too much and a threshold was met to where the catalase was deconstructed and damaged, unable to react efficiently under the given conditions. We see this in a numerous amount of other studies. Eyster (1950) explains in his experiment, “Effects of Temperature on Catalase Activity”, that his, “tables will reveal that 55C was the temperature at and above which destruction of catalase occurred” (p. 274). Although Eyster’s experiment is 67 years old, we see similar results today. Hameed (2011) reported in his study that, “Catalase activity diminished under heat stress in all genotypes” (p. 283). He continued to support his findings saying, “Heat stress-induced cell death in wheat leaves was evident by

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