Catalase Lab Report

The amount of catalase that reacts with the substrate (Hydrogen Peroxide) increases when we increase the mass of liver inside. As a result, more oxygen will be produced when the mass of liver is increased in the same amount of time. Variable Factor Description Independent (IV) Mass of liver Will be measured by grams, 1, 2 and 3 Dependent (DV) Amount of oxygen produced

Figure one depicts the reaction rate of peroxidase enzyme over time. The y-axis shows the absorbance of the assay solutions, and the x-axis depicts time it took for the reaction to occur in seconds.

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.

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.

Students will be observing normal catalase reaction, the effect of temperature on enzyme activity, and the effect of pH on enzyme activity in this experiment. The enzymes will all around perform better when exposed in room temperature than when it is exposed to hot and cold temperatures. This is based on the fact that the higher the temperature, the better the enzymes will perform, but as the temperature reaches a certain high degree, the enzymes will start to denature, or lose their function.

The aim of this study was to test the rate of reactivity of the enzyme catalase on hydrogen peroxide while subject to different concentrations of an inhibitor. The hypothesis was that hydrogen peroxide will be broken down by catalase into hydrogen and oxygen, where a higher concentration of inhibitor will yield less oxygen, resultant of a lower rate of reaction. Crushed potato samples of equal weight were placed in hydrogen peroxide solutions of various temperatures. The results showed that less gas was produced as the concentration of the inhibitor rose. This Is because more enzymes were inhibited, and so less active sites were available for reaction.

reaction rate increases. If the temperature of an enzyme gets to high the reaction rate will slow

It catalyses the hydrogen peroxide to oxygen and water, such as this formula: 2H2O2→O2+2H2O However, the effects of catalase is influenced by the substrate concentration. The different levels of the concentration will lead to different results of oxygen produced off the Hydrogen peroxide, Increasing the substrate concentration will increase the amount of the oxygen produced. Investigation Question: How Does increasing the concentration of Hydrogen Peroxide affect the amount of oxygen formed?

The question being answered by these experiments is: How do different conditions affect the productivity of enzymes? Enzymes are produced by cells and they act as catalysts, which means they are organic molecules that speed up chemical reactions. How effectively they work depends on the conditions they are in, such as level of temperature, pH level, substrate concentration, and salt concentration. In these experiments, Catalase will be placed in different conditions with hydrogen peroxide. How active the enzyme is in these different conditions will be measured by the amount of oxygen gas being produced. A very high increase in oxygen will indicate a high reaction rate and a low production of oxygen will show that there is a low reaction rate. On the other hand, if there is no change in the level of oxygen, it will indicate that the Catalase is denatured and is no longer functioning.

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.

The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,

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.

The independent variables are the range of temperatures and the range of hydrogen peroxide concentration. The dependent variable is the rate of catalase activity. The Catalase was taken from beef liver and was placed into a shaking thermostat machine to test for the amount of oxygen. The range of temperatures tested were 9.2 degrees to 30 degrees Celsius. The thermostat was filled with water at a specific temperature while the catalase was placed into six different bottles. A concentration of hydrogen peroxide was also added. With all firmly in place, the thermostat machine shook them for around a hundred times per minute. The entire reaction was examined at the pH of 7. The amount of oxygen was recorded for each temperature range and concentration. In conclusion, the catalase activity is the highest between 0 degrees and 10 degrees C because the amount of oxygen recorded was the greatest. When the temperature rose, the rate of catalase decreased. Between 10 to 20 degrees C, the catalase’s activity was smaller than the activity produced between 0 degrees and 10 degrees. Finally, between 20 to 30 degrees C, the catalase production rate was the lowest out of the three temperature ranges. Also, when the temperature was decreased while the H2O2 concentration was increased, the catalase’s activity was high and it plateaued for some time possibly due to the amount of H2O2. To conclude, when

Catalase breakdown hydrogen peroxide into water and oxygen. This experiment was to test the reaction on catalytic activity

The experiment gave us an insight of how pH affects catalase activity. We hypothesized that the enzyme activity will be quicker near neutral pH levels, than in acidic or basic solutions. The expectation was the optimum rate of enzyme would be at near or at neutral solution, while the rate would be really slow in acidic or basic solutions, such as in solutions of HCl and NaOH. Our experimentation ran into some errors because we used tap water which didn’t have a neutral pH of 7; instead it was 5, which is considered to be acidic. So, our experiment included pH’s of 0, 5, and 13.