Lets Watch Some Enzyme Catalysts Allie Duchin and Noah Gentry Period 6

Introduction: Enzymes are in the simplest form proteins. Like all proteins, enzymes have a special job; their job is to help speed along biochemical reactions. They essentially are catalysts to different reactions. In an enzyme-catalyzed reaction the substrate (original substance going through reaction) attaches itself to the active site (point of interaction) of the enzyme and the enzyme works to convert all of the substrate into a specific product or products. The enzyme remains the same as it did before the reaction and therefore can be reused as necessary. There are however, four ways in which an enzyme can become denatured or altered, which does not mean it is forever broken, but it cannot work until it reverts to its original state. These four ways to denature an enzyme are: Temperature, pH levels, Activations and Inhibitors, and Salt Concentration. Temperature and pH work similarly, because there are both specific temperatures and pH levels at which each enzyme works at, and if placed in any other temperature or pH than what a specific enzyme calls for, that enzyme will not work. Salt concentrations means that the needs to be some form of salt in the biochemical reaction in order for the amino acids in the enzyme to disperse among the substrate, otherwise if there is no salt the amino acids will attract to each other and not do its job. Activations and inhibitors do not denature an enzyme, but they alter it to work at different paces. Activations speed up reactions, whereas inhibitors slow down the enzymes processes.

Hypothesis: If an enzyme is not in a substrate, which has had its temperature, pH, salt concentrations altered, and then it will not go through the biochemical reaction because the enzyme will not reach the activation energy. If an enzyme is in a substrate to which activations or inhibitors have been added, then the enzyme will go through the biochemical at rates that were not expected. If none of the four things above have been added to the substrate then the reaction will occur and leave nothing but the desired products afterwards.

Pre-Lab (Exercise 2A Ques.) 1. a. Catalase b. Hydrogen Peroxide (H2O2) c. Oxygen gas (O2) and Water (H2O) d. You could test the pH of the new product. It would have a pH of 7 meaning it is water, which is neither an acid nor a base and Hydrogen peroxide is acidic so you would know that the O2 was the gas that evaporated. 2. If the catalase were to be boiled, it would not work,

because catalase only works in a cool environment. The enzyme would have been denatured.

3.

The liver or potato would deteriorate, because the enzyme

catalase is present in both of them. If the potato or liver were boiled beforehand it would need to cool before any reaction would take place, because once again the catalase is inside the liver or potato and therefore by heating it, the enzyme was denatured by altering it from its desired temperature. Materials Results The enzyme catalase sped up the decomposition reaction until sulfuric acid was added to the mixture. At this point the pH was too high for it to operate, and the protein was denatured. The rate of the reaction can be seen to slowly decrease, as most of the reactants have been turned into products after about two minutes. This happens because there is less reactant in the solution and as a result, less opportunity for catalase to bind to its substrate and form the product. KMnO4 H2O2 Catalase Sulfuric Acid 1Molar Beakers Pipets Burette

Data KMnO4
10 30 60 Time (seconds) 90 120 180 360

Base line Final reading Initial reading Amount KMnO4 consumed Amount of H2O2 used

3.4 8.6 6.1 2.5 .9

3.4 10.2 8.6 1.6 1.8

3.4 11.2 10.2 1 2.4

Ms. Weeg Didnt Collect Data

3.4 11.5 11.2 .3 3.1

3.4 11.6 11.5 .1 3.3

3.4 11.6 11.6 0 3.4

This table demonstrates the change in rate overtime.

Conclusion The rate of the reaction slowly decreases, in what is called an inverse relationship. This can be seen when the Amount of H2O2 present is calculated at different intervals during the reactions. In the table above, the difference in Amount of H2O2 used at each interval represents the rate of the reaction, in the sense that it shows how much H2O2 is being consumed in each time period. The rate of reaction in this case can be seen to asymptotically approach zero, and at the end of the 360 second test, only 1 drop of KMnO4 was needed to make the mixture change color, meaning that the reaction had effectively gone to completion.