Horseradish Peroxidase Experiment
Environmental Variables and their effect on Horseradish Peroxidase
Abstract
There are several factors that can affect the rate of reaction of peroxidase such as temperature, pH, concentration of peroxidase present and whether or not it has been boiled. Our experimental data demonstrated that peroxidase activity peaked between 23 degrees Celsius and 32 degrees Celsius. We found the pH to be 7 for optimal activity. As far as the concentration is concerned our results showed that as the concentration of horseradish peroxidase doubled so did the rate of reaction. Lastly, the boiled horseradish peroxidase proved to be denatured and did not yield any activity while the normal extract proceeded to react in an upwards fashion. In conclusion, the rate of reaction of horseradish peroxidase was optimal at neutral, room temperature conditions and it increased with concentration.
Introduction
The presence of enzymes in our bodies controls the multiple events happening simultaneously by lowering the activation energy of chemical reactions. (1) These enzymes perform best under a certain set of environmental conditions. The purpose of this laboratory investigation is to examine the activity or horseradish peroxidase, an enzyme, under a wide range of circumstances and key …show more content…
The first is figure out if concentration plays a part in the reaction rate. To begin this trial, we gathered 3 cuvettes in which we added horseradish peroxidase in the following amounts; .5 mL, 1.0 mL and 2.0 mL. In each of these cuvettes, we added 2.0 mL of H2O2, 1.0 mL of Guaiacol and enough pH 5 Buffer to fill each cuvette to 8.0 mL with all of the materials combined. Immediately after adding the materials in each cuvette, we placed it in the spectrophotometer to get an absorbance reading @ 500 nm in 20 second intervals commencing at 20 seconds and concluding at 120
Abstract
There are several factors that can affect the rate of reaction of peroxidase such as temperature, pH, concentration of peroxidase present and whether or not it has been boiled. Our experimental data demonstrated that peroxidase activity peaked between 23 degrees Celsius and 32 degrees Celsius. We found the pH to be 7 for optimal activity. As far as the concentration is concerned our results showed that as the concentration of horseradish peroxidase doubled so did the rate of reaction. Lastly, the boiled horseradish peroxidase proved to be denatured and did not yield any activity while the normal extract proceeded to react in an upwards fashion. In conclusion, the rate of reaction of horseradish peroxidase was optimal at neutral, room temperature conditions and it increased with concentration.
Introduction
The presence of enzymes in our bodies controls the multiple events happening simultaneously by lowering the activation energy of chemical reactions. (1) These enzymes perform best under a certain set of environmental conditions. The purpose of this laboratory investigation is to examine the activity or horseradish peroxidase, an enzyme, under a wide range of circumstances and key …show more content…
The first is figure out if concentration plays a part in the reaction rate. To begin this trial, we gathered 3 cuvettes in which we added horseradish peroxidase in the following amounts; .5 mL, 1.0 mL and 2.0 mL. In each of these cuvettes, we added 2.0 mL of H2O2, 1.0 mL of Guaiacol and enough pH 5 Buffer to fill each cuvette to 8.0 mL with all of the materials combined. Immediately after adding the materials in each cuvette, we placed it in the spectrophotometer to get an absorbance reading @ 500 nm in 20 second intervals commencing at 20 seconds and concluding at 120