Protein Conformation Lab

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

This experiment looked at how substrate concentration can affect enzyme activity. In this case the substrate was hydrogen peroxide and the enzyme was catalase. Pieces of meat providing the catalase were added to increasing concentrations of hydrogen peroxide in order to measure the effect of hydrogen peroxide concentrations on the enzyme’s activity. The variable measured was oxygen produced, as water would be too difficult to measure with basic equipment.

An Investigation on the rate of reaction of the enzyme Catalase on the substrate Hydrogen peroxide.

The purpose of this experiment was to simply measure oxygen production rates released from decomposed hydrogen peroxide under different conditions (concentration of enzymes, temperature, and PH level).

Peroxidase is an enzyme found in potatoes that catalyzes the breakdown of hydrogen peroxide, H2O2, into O2 gas and water. We examined the different pH environments that can affect the enzyme activity during the breakdown of H2O2. In order to do this, we added different levels of pH, low, medium, and high, into different test tubes with the enzyme and H2O2, and we then inverted the tube. The amount of O2 gas produced was then measured and recorded. The result was that the higher pH produced more gas, followed by medium pH, then low pH. The enzymes were more active in the pH of about 10. It increased

The differences for the rates of reaction between the liver and potato are accounted for because liver contains more catalase enzymes than potatoes. This is because the liver is responsible for ridding toxins out of the body and as a result needs more catalase enzymes to do so; explaining the bigger reaction it had with the hydrogen peroxide.

The aim of my investigation is to see how pH affects the activity of potato tissue catalase, during the decomposition of hydrogen peroxide to produce water and oxygen.

It would change the pH of the liver or potato as HCl is very acidic and NaOH is very basic. Changes in pH can denature the protein in the enzymes which could result in no reaction. For most enzymes, they require a very specific pH, so when a solution becomes too acidic or too basic, no reaction can occur as the enzyme will become denatured by the abrupt change in pH.

An Enzyme is a protein, which is capable of starting a chemical reaction, which involves the formation or breakage of chemical bonds. A substrate is the surface or material on or from which an organism lives, grows, or obtains its nourishment. In this case it is hydrogen peroxide. This lab report will be explaining the experiment held to understand the effects of the changes in the amount of substrate on the enzyme’s reaction.

Observing how the enzyme catalase found in chicken and beef livers breaks down hydrogen peroxide at varying pH levels and temperatures.

When the beef liver was placed in different temperatures of H2O and hydrogen peroxide was added to both the blended beef liver, and the piece of liver, it made the solution bubble. The H2O substrate reacted with the catalase enzyme in the liver. The results of the experiment confirmed my hypothesis that extreme levels of pH will affect or damage the catalase whether it was the liver or the fresh/canned pineapple. When the catalase from beef liver was exposed to extreme levels of pH, the enzyme was either damaged or denatured. This was signified by the results of the levels of bubbles which were recorded at different levels when H2O was added to the enzyme with different levels of pH. It was also noted that the results indicated that the catalase activity can be enhanced by increasing the reaction temperature only to a certain extent; the extreme temperatures like with the boiling water will compromise the enzyme activity.

Should an enzyme denature they will no longer function properly because their active sites, where the substrates attach to, will change shape and no longer function. Substrates are reactants that bind with the active site of the enzymes. The substrate in our experiment was hydrogen peroxide and the enzyme itself was catalase which was extracted from potatoes. The products of this substrate-enzyme interaction were H20 and O2. The first test that was conducted involved the concentration of enzymes in potato cells.

The purpose of this lab report is to investigate the effect of substrate concentration on enzyme activity as tested with the enzyme catalase and the substrate hydrogen peroxide at several concentrations to produce oxygen. It was assumed that an increase in hydrogen peroxide concentration would decrease the amount of time the paper circle with the enzyme catalase present on it, sowing an increase in enzyme activity. Therefore it can be hypothesised that there would be an effect on catalase activity from the increase in hydrogen peroxide concentration measured in time for the paper circle to ride to the top of the solution.

Testing the Effects of Temperature on the Decomposition of Hydrogen Peroxide with the Enzyme Catalase

Hydrogen peroxide is a toxic byproduct of cellular functions. To maintain hydrogen peroxide levels the catalase enzyme deconstructs hydrogen peroxide and reconstructs the reactants into oxygen gas and water. The catalase enzyme is found inside cells of most plants and animals. Regulating the levels of hydrogen peroxide is crucial in homeostasis and analyzing it’s optimal conditions for performance is just as important. To understand the optimal environment for this enzyme, they are put into different environments based off protein activity (enzymes are proteins). Catalase samples will be put into different hydrogen peroxide environments based off pH and temperature. The more active the enzyme, the more oxygen and water it will produce. Enzyme activity can be seen through the release of oxygen in the hydrogen peroxide. Since oxygen cannot be accurately measured, the data will consist of the longevity of the reaction in different environments. If the pH is higher than 7, then the reaction rate will increase due to the ample amount of hydrogen ions in the hydrogen peroxide. However the pH level cannot be higher than 10 or else there will be too many hydrogen atoms in the peroxide for the enzyme to be able to deconstruct them. If the temperature is increased, then the reaction rate will increase due to the ample amount of energy and movement in the hydrogen peroxide and enzyme.