Catalase Enzyme Lab

In order to see the effects of pH and temperature on the enzymatic reaction of catechol oxidase when separated from potato tissue. We used a spectrophotometer to measure how much blue light energy is absorbed by benzoquinone. Benzoquinone is a product of catechol when it has been oxidized by different temperatures and pHs. We hypothesized that the benzoquinone absorbance rate would be faster when the pH added to the cuvettes were greater than the pH of the potato tissue. The pH of the potato tissue was pH 6. Our results show that pH 7 had the faster absorbance rate, slightly slower at pH 4, and slowest at pH

Catalase is an important enzyme that protects cells from oxidative damage, which hydrogen peroxide can cause. It is an incredibly efficient enzyme where one catalase molecule can convert millions of hydrogen peroxide molecules each second.

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.

Purpose of the Lab: In this lab I learned the different effects of substrates concentrations have on catalase activity. Introduction: Before you get started on this we should touch base on some critical points, these will help you perform and understand the experiment. Enzymes are protein molecules that are found in every living cell.

Enzymes are catalytic proteins, meaning they speed up – but do not create – chemical

This experiment was performed to determine the resultant effect of temperature change on the reaction between the enzyme catalase and hydrogen peroxide. This experiment was performed by measuring and comparing the amount of oxygen bubbles produced and the absorbance of the catalase and hydrogen peroxide solution over time at room temperature, 2°C, 50°C, and 60°C. The overall result of this experiment proved that this reaction works best at room temperature, slows down when the temperature is lowered, and does not take place when the temperature gets too high due to the enzyme denaturing at these higher temperatures. The hypothesis that was

Enzymes are biological catalysts that speed up chemical reactions, without being used up or changed. Catalase is a globular protein molecule that is found in all living cells. A globular protein is a protein with its molecules curled up into a 'ball' shape. All enzymes have an active site. This is where another molecule(s) can bind with the enzyme. This molecule is known as the substrate. When the substrate binds with the enzyme, a product is produced. Enzymes are specific to their substrate, because the shape of their active site will only fit the shape of their substrate. It is said that the substrate is complimentary to their substrate.

Enzymes such as Catalase are protein molecules that are found in living cells. They are used to speed up specific reactions in the cells. Each enzyme just performs one particular reaction so they are all very specific. Catalase enzymes found in living cells e.g. in yeast, potato or liver, speed up (in our case) the breaking down of hydrogen peroxide.

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.

(Johnson Matthey, unk.) In this experiment, effect of temperature on catalase will be looked at. The hypothesis is that if the temperature is increased, then the enzyme activity will increase up to the point of too much increase in temperature, which will cause activity to slow and stop due to the denaturing of the enzyme. The dependent variable is the oxygen production of the enzyme catalase as it breaks down hydrogen peroxide, and the independent variable will be varied temperatures of 0, 23, 37, and 55 degrees Celsius.

Introduction: Enzymes are defined as being molecules that function as biological catalysts, increasing the rate of reaction without being consumed by the reaction. They allow molecules to use less energy to create the reaction. Each enzyme has a specific shape for its substrate and only that substrate can bind to the enzyme to create the reaction. If environmental factors change such as PH levels or temperature this could cause enzymes to change their shape and therefore their function. If the enzyme structure changes the molecules can’t bind to them causing the reactions to not be able to be made. The enzyme for this experiment was the catalase enzyme which is used for the degradation of hydrogen peroxide, it is a protective enzyme located in nearly all animal cells. After researching the topic finding the ways enzymes are effected by certain environmental factors drove to do the experiment. My hypothesis for this reaction was if the temperature goes up the enzyme reaction will go down because of denaturation. According to my hypothesis at 0 degrees Celsius the enzyme reaction should be the highest and at 23 degrees it should go down at 37 it should keep going down and at 55 degrees the enzyme reaction rate should be the lowest. This experiment is so important because the catalase enzyme breaks down H2O2 which is poisonous to our bodies and turns it into two chemicals that are not harmful to us,

What are the effects of different temperatures on the decomposition of Hydrogen Peroxide with the Enzyme Catalase. Different enzymes work best at different optimal temperatures, and with this experiment we hope to discover which temperatures are unideal for Catalase. The substrate is H2O2 which binds to the active site of the enzyme Catalase. The reaction in question is as written below:

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,

Temperature can affect the reaction of catechol oxidase by speeding up or slowing down the reaction. I was able to see what happened to the absorbance after changing the temperature of the catechol oxidase solution. I did this by heating and cooling the solutions to measure the absorbances in hot, cold, warm, and room temperature. Then the data was compared to see how the temperature effected the solution. The catechol oxidase solutions reacted best in room temperature (twenty-three degrees Celsius) and the worst in the cold (zero degrees Celsius). I concluded that temperature really does affect the way catechol oxidase reacts.