Catalase Enzyme Activity

H2O2 is commonly known as hydrogen peroxide and it is a strong oxidizer and a naturally produced compound in humans as a by-product of oxidative metabolism. Because of this, humans also produce the enzyme catalase peroxidases in order to convert small amounts of H2O2 into oxygen and water. It uses the following chemical formula:

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

The temperature can have a major impact on an enzyme. According to Campbell Biology author Reece etc. 2011 “The enzyme reaction will increase as the temperature increase with the increasing temperature….substrates collide with active sites more frequently when the molecules move rapidly.”(Reece etc 2011) Every enzyme hits its optimal temperature the reaction will be at its highest point.(Reece etc. 2011) When the

The human body is an incredible system that is capable of working a multitude of diverse functions. Without the help of the many different protein molecules, the human body would not be able to function properly. One major group of proteins called enzymes are mandatory for essential life. These proteins are constantly at work assembling molecules, metabolizing energy, and fighting off infections. An enzyme is a macromolecule that acts as a catalyst that speeds up a chemical reaction without being consumed by the reaction. Without these proteins, these reactions would take place too slowly to keep us alive. Essential parts in your body like vitamins and minerals cannot do any work without

Temperature controls the speed the enzymes work at. Higher temperatures increase the kinetic energy which increases the chance of collision therefore speeding up the rate of

It is expected that the change in temperature will initially increase as the concentration of the Catalase increases in the hydrogen peroxide (H2O2). As more Catalase is added into the hydrogen peroxide (H2O2), the rate of reaction is expected to increase due to a higher concentration of enzyme present and therefore a greater frequency of successful collisions between the enzyme and substrates resulting in a faster breakdown of the substrate. However, as the concentration of the Catalase approaches 100% concentrated, it is expected for the change in temperature (reaction rate) to plateau. This occurs as there is only a

These results show how temperature of extreme high, or low affects enzyme activity. The highest rate of enzyme activity occurred at 37 Cº. Anything that was hotter or cold than 37 Cº slowed the reaction rate. As I thought, 100 degrees would denature the enzyme, and that was the case. The data provided shows exactly what temperatures enzymes work best, and worst. The objective was achieved as we discovered the different reaction rates under different temperatures. The results are reliable, as we know enzymes do not work well when under extreme heat or denaturation occurs. What I learned in this experiment was that enzymes don’t work well under cold temperatures because they tend to move slower. My hypothesis did not quite match, because I thought they work best at lower temperatures.

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 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

Five different temperatures of enzyme (spinach extract) (5°C, 20°C, 35°C, 45°C and 65°C) were added to individual measuring cylinders -each filled with 7ml of Hydrogen Peroxide (H202). The height of foam (oxygen + water) produced by the reaction was recorded for each temperature of the catalase after 30 seconds, to find at which degrees the enzyme activity had the fastest reaction rate. The data collected from this experiment suggested that the enzyme extract had the greatest efficiency at 20 °C, and the temperatures greater displayed a decline in rate of reaction.

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.

This happened because there were some active sites that were empty, so the substrate was able to bind to them, but they slowly started to diminish, which caused the enzyme activity to vanish.

Within a cell, enzymes are used as a catalyst to increase the rate of chemical reaction. They do not consume themselves, rather they help in increasing the rate of reaction. Within the body, enzymes vary depending on their specific functions. For instance, hydrogen peroxide is a toxic chemical, but it breaks down into harmless oxygen and water. This reaction can be sped up using the enzyme catalyst produced by yeast. Hydrogen peroxide is produced as a byproduct in cellular reaction, because it is poisonous and must be broken down, therefore this reaction is important. The speeding up of the reaction is shown below:

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