Hydrogen Peroxidase Lab Report

The research and observations of this lab primarily focused on the enzyme activity of the enzyme Peroxidase. Peroxidase is a large protein and is composed of more than three hundred amino acids. The enzyme was selected as it is easy to experiment with and effectively showcases the effects of varying independent variables, such as pH and temperature. Peroxidase catalyzes the decomposition reaction of the chemical Hydrogen Peroxide ( H2 O2 ) into water and an electron donating molecule, which stands for R in the written chemical equation. ( The equation is displayed below:

2) Yes, the rate of gas production increased as more yeast was added, since more enzyme was able to convert hydrogen peroxide more quickly.

In this experiment, the naturally occurring peroxidase is extracted from homogenized turnip (Brassica rapa) pulp (Coleman 2016). Its role in the environment is to remove toxic hydrogen peroxide during metabolic processes where oxygen is used (Coleman 2016). The goal of this experiment is to evaluate the change of absorbency of turnip peroxidase within a metabolic reaction utilizing oxygen. Any change noted is indicative of the peroxidase removing hydrogen peroxide. Within this experiment, the extract will be prepared, the amount of enzyme will be standardized, and the effect of changing the optimal conditions will be observed. If the enzyme concentration is increased then the rate of the reaction decrease. If the pH of solutions used is increased

If temperature of the water(enzyme environment) is increased to 35°C, then the enzyme activity will

The results of the three-part experiment provide a deeper knowledge about the factors that influence the rate of the reaction of the enzyme activity and how the factors influence the structure or function of the enzyme.

The preparation for the experiment started by gathering the solutions of enzyme Peroxidase, substrate hydrogen peroxide, the indicator guaiacol and distilled water. Two small spectrometer tubes and three large test tubes with numbered labels. In addition, one test tube rack, one pipet pump and a box of kimwipes were also gathered. Before the experiment, the spectrometer must be set up to use by flipping the power switch to on. Following, the machine was warmed up for 10 minutes and the filter lever was moved to the left. In addition, I set the wavelength to 500 nm with the wavelength control knob. Before the experiment, I had to create the blank solution by pipetting 0.1 ml of guaiacol, 1.0 ml of turnip extract and 8.9 ml water into tube #1. Following the creation of the blank, a control 2% solution was created.

5ml pipettes graduated in 0.1 ml units with suction devices or automatic pipetters and tips

The purpose of this experiment is to learn the effects of a certain enzyme (Peroxidase) concentration, to figure out the temperature and pH effects on Peroxidase activity and the effect of an inhibitor. The procedure includes using pH5, H202, Enzyme Extract, and Guaiacol and calibrating a spectrophotometer to determine the effect of enzyme concentration. As the experiment continues, the same reagents are used with the spectrophotometer to determine the temperature and pH effects on Peroxidase activity. Lastly, to determine the effect of an inhibitor on Peroxidase, an inhibitor is added to the extract. It was found that an increase in enzyme concentration also caused an increase in the reaction rate. The reaction rate of peroxidase increases at 40oC. Peroxidase performed the best under pH5 and declined as it became more basic. The inhibitor (Hydroxy-lamine) caused a decline in the reaction rate. The significance of this experiment is to find the optimal living conditions for Peroxidase. This enzyme is vital because it gets rid of hydrogen peroxide, which is toxic to living environments.

Higher levels of solution should produce higher levels of product. The independent variable for the control group data and the experiment data is the yeast concentration. The dependent variable for the control group data and the experiment data is how much oxygen is produced. The Constant for the control group data and the experiment data is time and amount of hydrogen peroxide. The products of the experiment will increase if the levels of reactants increase. Denatured yeast may cause change in the reaction of the experiment. For all trials of the control group, the concentration of yeast is 6ml. For the experiment data, the yeast concentration varies from 8mL, 10 mL, 12 mL, 14 mL, and 16 mL. The temperature may cause change in the reaction of the combination of yeast and hydrogen peroxide

The hypothesis is that catalase activity will increase exponentially with higher concentrations of hydrogen peroxide until all catalase active sites are filled, in which case the

Assessing Catalase's Rate of Hydrogen Peroxide Decomposition Under Varied Temperatures Through Gas Collection The goal of this lab was to determine the effect of temperature on the reaction rate of catalase. We created stock solutions of homogenized chicken liver, controlled the temperature through a water bath, and added the enzyme catalase to the hydrogen peroxide substrate. We then collected the gas through a water displacement setup and recorded how long each trial took to produce 2 ml, 4 ml, and 6 ml of oxygen. For rate of reaction, we found an initial positive relationship, a peak, and then a potential (not statistically proven) negative relationship as temperature increased past 38˚C. From our t-tests, we found

This is an experiment to examine how the concentration of the substrate hydrogen peroxide affects the rate of reaction of the enzyme catalase.

Hydrogen peroxide is a by-product of biochemical metabolism. The accumulation of hydrogen peroxide can be deadly, so it must be decomposed. One of the decomposing factors is an enzyme called Catalase. Catalase breaks hydrogen peroxide into water and oxygen. Since this is a decomposition reaction, it is exothermic. Hydrogen peroxide can gradually degenerate itself, it decomposes much faster with the help of Catalase which lowers the activation energy to the minimum energy barrier that hydrogen peroxide molecules should overcome to decompose.

The null hypothesis for the first experiment was that substrate concentration would have no effect on the reaction rate. It was hypothesized that the reaction rate would increase with rising substrate concentrations, until all active sites were bound. The null hypothesis for the second experiment was that temperature would not have an effect on reaction rates. It was hypothesized that until the enzyme is denatured, as temperature increased, so would the reaction rate.

There were three test tubes in which the experiment was held. A relatively equal sized portion of raw potato (this contained the enzyme [a biological catalyst] hydrogen peroxidase) was placed in each tube. Then, enough water to cover the potato was added. Proceeding this, each of the test tubes were assigned a temperature; cold, room temperature or warm (this was written on the tag so that they were not confused). The test tube destinated ‘cold’ was placed in a ice bath for five minutes. At the same time, the ‘hot’ test tube was placed in a hot water bath for five minutes. Meanwhile, the room temperature test tube sat at room temperature for five minutes. When the five minutes were over, the test tubes were returned to the rack (so that they were able to be observed). Then, the test tubes were allowed to sit at room temperature for five more minutes. Once that period of time was over, 2 ml of hydrogen peroxide (the substrate) was added to each tube.