Neutral Ph Lab Report

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

Both low pH levels and high pH levels produced a low amount of catalase activity.

Most enzymes have an optimum pH of around 7, which is fairly neutral. To ensure the experiment is a fair test, I will use the same pH of hydrogen peroxide in every test.

These results shown from this experiment led us to conclude that enzymes work best at certain pH rates. For this particular enzyme, pH 7 worked best. When compared to high levels of pH, the lower levels worked better. The wrong level of pH can denature enzymes; therefore finding the right level is essential. The independent variable was the amount of pH, and the dependent being the rate of oxygen. The results are reliable as they are reinforced by the fact that enzymes typically work best at neutral pH

Peroxidase is a turnip enzyme; it is used in the oxidation of hydrogen peroxide to lower activation energy, speeding up the reaction. The activity of peroxidase is highly dependent on its environment and most importantly the pH level. Peroxidase has been the focus of many recent studies and is believed to possibly reduce swelling among other things. We conducted an experiment testing the effect different levels of pH had on the reaction rate of peroxidase. In the experiment we created different solutions all containing hydrogen peroxide, peroxidase, and guaiacol. However each cuvette contained a different pH level, 2,5,7,or

To improve the results from the experiment buffer solutions that were not whole pHs could have been used e.g. pH 4.5, 5.5 etc. This would have provided more reliable results as a wider range of results would have been produced. Using pHs with decimals would also help to more accurately determine the optimum pH as the optimum may have been above or below the pH stated in the hypothesis; 8. In this experiment however the optimum is taken at 8 because the graph does not rise again.

Table 2: Consists of color extract taken from a red cabbage for a natural indicator. The pH reading that was measured by using the pH meter and the result of the pH reading to determine whether the solution was acidic or basic.

The effectiveness of peroxidase was measured in a varying pH environment. The environment’s pH can range from   1-14, 7 being neutral, 7-1 being more and more acidic towards 1, and 8-14 being more and more basic towards 14 (Raven, 2011).

To prevent fluctuation in the pH, a solution known as a “buffer solution” was used in the experiment. Buffer solutions are mixtures of at least two chemicals which counteract the effect of acids and alkalis. Therefore, when a small quantity of alkali or acid solution is added the pH of the enzyme doesn’t change.

The purpose of this investigation is to discover the effect of pH on the activity of catalase, an enzyme which plays the integral role of converting hydrogen peroxide into water and oxygen, and discover which pH level it will work at the most efficient rate (the optimum). The original hypothesis states that that the optimum would be at a pH is 7, due to the liver, where catalase usually resides, being neutral. The experiment consists of introducing the catalase to hydrogen peroxide, after exposure to certain solutions; hydrogen peroxide, water and hydrochloric acids, all containing the adjusted pH, and measuring the height of froth formed, an observable representation of the activity of the enzyme. The final data indicated that

The Uptake of Neutral red dye by saccharomyces cerevisiae in the presence of a metabolic inhibitor

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.

will be working at the pH 7 the majority of the time and our bodies

Abstract: Enzymes, catalytic proteins that at as catalysis which makes the process of chemical reactions more easily. There are two main factors that actually affects enzymes and their functions which are temperature and pH. Throughout this experiment, the study how pH and peroxidase affects each other and the enzyme was made. The recordings of how the enzymes responded when it was exposed to four different pH levels to come up with an optimum pH which was predicted in the hypothesis and the IRV at the end.

This experiment is designed to analyze how the enzyme catalase activity is affected by the pH levels. The experiment has also been designed to outline all of the directions and the ways by which the observation can be made clearly and accurately. Yeast, will be used as the enzyme and hydrogen peroxide will be used as a substrate. This experiment will be used to determine the effects of the concentration of the hydrogen peroxide versus the rate of reaction of the enzyme catalase.