The Effect of Temperature on the Enzyme Catalase

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.

· I predict that the enzyme will work at its best at 37c because that

The Effects of Varied Temperatures, pH Values, Enzyme Concentrations, and Substrate Concentrations on the Enzymatic Activity of Catecholase

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

The Impact of Temperature and pH on the Enzyme Activity of Catechol Oxidase in Solanum Tuberosum Samples

Abstract: The Effects of Temperature on Catechol Oxidase. Lania Ellis, 2014, 102 Student Center Dr. San Marcos, TX 78666.

The purpose of this lab was to study the effect of varying the substrate concentration of Hydrogen peroxide (H2O2) on the rate of peeled potato catalase enzyme activity, on the decomposition of H2O2. This experiment was carried out by diluting the 6% H2O2 with distilled water to decrease the concentration, and then placed in a test tube. A small piece of filler paper disc was coated with the enzyme before it was submerged to the bottom of the substrate hydrogen peroxide solution. The stop timer was started immediately when the filter paper disc touched the bottom and the timer was stopped when the filter paper reached the surface. The results of the experiment showed a linear correlation between concentration of the substrate and the rate of enzyme activity. Overall, as the concentration of H2O2 was decreased, the rate of reaction had decreased.

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,

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 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.

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.

If the temperature is too hot or too cold, then the reactivity and reaction rate of which the enzyme catalase breaks down hydrogen peroxide will decrease.

BACKGROUND: Catalase (the enzyme) is found in yeast, it breaks down hydrogen peroxide (the substrate) into water and oxygen according to this equation. 2H2O2(aq) -------------------> 2H2O(l) + O2(g) + catalase(aq) One molecule of catalase can break 40 million molecules of hydrogen peroxide each second. Factors that affect the rate of reaction § Increasing the temperature increases the kinetic energy at which the enzyme and substrate collide.

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 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.