Rate Of Decomposition Of Catalase

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

The goal of this lab was to find the effect of different substrate concentrations of hydrogen peroxide on the rate of catalase enzyme activity. This experiment was specifically meant to find a correlation between an increasing substrate concentration of hydrogen peroxide on the rate of catalase enzyme activity. Four test tubes were used, one filled with 5 milliliters of water and three with 5 milliliters of different concentration of hydrogen peroxide ranging from 0.5%, 1%, and 1.5%. Four drops of yeast solution were dropped into each test tube using a pipette. Then, a lab quest probe was attached to each of the test tubes. The test tubes were tapped twice every second in order to agitate the solution. The rates of the catalase enzyme activities were recorded after 400 seconds of tapping. After the lab, all the materials were cleaned. This experiment was repeated the next day. After both trials were completed, the average from the two trials was taken. Then, the data from the experiment was graphed, with the different substrate concentrations of hydrogen peroxide recorded on the x-axis and the average rates of catalase enzyme activity in kilopascals per second recorded on the y-axis. The experiment results showed that there was a positive correlation

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.

My graph shows there is an almost perfect positive correlation between the hydrogen peroxide concentration and the rate of the catalase enzyme reaction, with a correlation coefficient of 0.99. The rate of reaction at 1% concentration was 0.46cm3 oxygen produced per minute and the lowest recorded rate. For 3% was 1.33cm3 per minute, and for 6% was 2.17cm3 per minute and was the highest recorded rate. The

The purpose of this experiment was to simply measure oxygen production rates released from decomposed hydrogen peroxide under different conditions (concentration of enzymes, temperature, and PH level).

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

Objective: The purpose of this experiment was to discover the exact change of enzyme activity of catalase and how it corresponded to temperatures, by measuring the rate of appearance of a product. Introduction: Enzymes are substances produced by living organisms, in which act as a catalyst.

A rate is a measure of change that occurs in a given time whilst a

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,

In Part C of the lab, we repeated the same process as we did in Part A, but we used 3 different temperatures: 5oC, 37oC, 100oC. After we did the experiment for 5oC, it can be concluded that the enzyme was slightly inhibited because it started out at a gas level of 56, but at the last interval, it had a gas level of 60. That means it has not produced as much as it should have because the enzyme usually prefer to work in warmer environments, but if it is in a cold environment, then it will not produce as much as it should. After we did 37oC, it can be concluded that this was the optimal temperature of the yeast catalase because the gas level originally started at 11, but as time went on, the gas level started to increase a numerous amount and at the last interval, the gas level was 67. After we did 100oC, it can be concluded that the enzyme was almost entirely denatured because the gas level stayed at 0 for 5 intervals long, and when it increased, it barely increased. That happened because the enzyme has a melting point to which the enzyme functions and I believe the enzyme met its melting point because it could not produce nearly as much as it should have.

The enzyme is the yeast solution and the graph shows that, even though the amount of the enzyme did not change, the rate of reaction (shown by the volume of gas released) still continues on an upward trend. The function of the enzyme is to have the substrate attach itself to its active site, and if there is more substrate, higher the chances of them bumping into each other and catalyzing are. As the concentration of the hydrogen peroxide substrate increased, the data shows that the chances of bumping into the yeast enzyme increased as well, so more reactions took place and, therefore, more oxygen gas had been released. If the concentration of [H2O2] were to keep increasing, it can be hypothesized that the reactions would reach a peak and stall,

The result of our data isn’t accurate, and has flaws in terms of timing and accuracy. Next time, before I time the enzyme catalase for 2 minutes when I insert and get the enzyme catalase out, I will time 15 seconds, instead timing at random and inconsistently. Also, our experiment only used 4 different temperatures of the hydroperoxide, which consists the idea that next time we can increase the sample sizes by using more temperatures. Next time, we should find out the temperature when the enzyme catalase lose its its shape. Since the enzyme lost its shape until warm water that was 43° and lost its shape at hot water of 95.8° we can have more temperature between both the warm and the hot water.

This lowers the rate of reaction due to the lower concentration (as explained in the variables section). Once a Hydrogen peroxide molecule has decomposed it is no longer a consideration and cannot decompose again as it is no longer a Hydrogen peroxide molecule. This lowers the numbers of Hydrogen peroxide molecules present lowering the concentration thus lowering the rate of reaction, eventually lowering the rate of reaction to nil where all (or virtually all) Hydrogen peroxide molecules have decomposed. At this point no more products are produced as no more Hydrogen peroxide is reacting, as no more Hydrogen peroxide is colliding with catalyst particles, because it has all decomposed.