I knew that the catalase was working, because it was evident that it was speeding up the chemical reaction of the hydrogen peroxide. The decomposition reaction of hydrogen peroxide into products water and oxygen occured very quickly as soon as the enzyme for hydrogen peroxide (catalase) was added into the graduated cylinder with the hydrogen peroxide. As a result, an increasing amount of foam was being produced; a mixture of the products water and oxygen. Catalase speeds up chemical reactions by lowering the activation energy required to initiate the chemical reaction. Therefore, after adding catalase to the substrate that needed to be broken down into it’s products, the reaction’s activation energy was lowered, and it did not need as much …show more content…
This is seen in the data in Part B, where the optimal temperature is seen to have occurred between 30ᐤC to 40ᐤC, which is why the foam height decreased going from 40ᐤC to 30ᐤC (144mm to 136mm). At this specific temperature of 37ᐤC, the enzyme catalase is able to function most effectively, which is approximately the temperature of the human body. At 37ᐤC, there will be an increase in the amount of kinetic energy in the molecule, which means there will be an increase in collisions in the molecules, allowing the enzyme to have it’s maximum activity. Generally, one would think that this trend would continue as the temperature continues to increase, but if it increases over 37ᐤC, the rate of reactivity of the enzyme will drop drastically, as the enzyme’s bonds start to break and it denatures. However, according to the class observations, it was noted that the temperature at which the foam height was the greatest was at 0ᐤC, which contrasts to the actual optimal temperature of catalase …show more content…
This is because the inhibitor, copper (II) sulfate interfered with the substrate (hydrogen peroxide) from binding to the enzyme (catalase). Therefore, the enzyme’s activity was reduced, as it was unable to breakdown the hydrogen peroxide as much, and was unable to produce as much foam as a result. After the second minute of combining the catalase with the inhibitor, and the hydrogen peroxide, it was evident that the production of the foam had ceased completely. After increasing from a foam height of 14-15mm, the foam height stayed at 15mm for the remainder of the 5 minutes, because the inhibitor had now interfered fully with the substrate binding to the enzyme, by deeming the enzyme
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
4.a) Describe the effect of low (pH 2) and high (pH 12) pH levels on catalase activity.
· I predict that the enzyme will work at its best at 37c because that
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.
This investigation will be carried out to investigate the rate of reaction of the enzyme catalase on the substrate hydrogen peroxide.
What would it mean if a known catalase positive bacteria did not produce bubbles after the addition of H2O2? It would mean that a different strain of bacteria was used that doesn’t react to hydrogen peroxide.
The hypothesis tested in this experiment was, if the temperature of enzyme catalysis were increased, then the reaction rate would increase, because enzyme-catalysis reacts by randomly colliding with substrate molecules, and the increase in temperature increases the speed of collision or reaction rate. The final data collected for the experiment was positive with my hypothesis. The coffee filter, covered in potato solution, sank and rose at a faster pace in the hydrogen peroxide when the temperatures were raised.
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,
Between 36.7°C and 4° C there was a decrease in reaction rate. This is majorly due to the fact that less enzyme-substrate complexes are formed as the kinetic energy is decreased and both the catalase and hydrogen peroxide have less collisions with one another (“The Kinetic Molecular Theory”). A temperature decrease would have also caused the molecules to be more tightly packed together, thereby reducing the flexibility of catalase, making enzyme-substrate complexes less likely to occur.
The independent variable in this investigation is pH. Each individual enzyme has it’s own pH characteristic. This is because the hydrogen and ionic bonds between –NH2 and –COOH groups of the polypeptides that make up the enzyme, fix the exact arrangement of the active site of an enzyme. It is crucial to be aware of how even small changes in the
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
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.
reaction rate increases. If the temperature of an enzyme gets to high the reaction rate will slow
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.
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: