How does ethyl Alcohol inhibit the rate of catalyst enzyme activity?

1. How does ethyl Alcohol inhibit the rate of catalyst enzyme activity? By: JeranikaSemien

2. Introduction: • The general focus of this project is the study of enzymes and how they work. • The purpose of this experiment is to determine whether or not ethyl alcohol can inhibit the rate of catalytic enzyme activity. • The reason I choose this specific area to study was based on the fact that I like to make this occur. Mixing chemicals and watching them react is interesting to me, so, I choose to use a catalyst in hopes of enhancing some kind of reaction in the liver.

3. Background info.. • Enzymes are proteins that participate in cellular metabolic processes. The basic function of an enzyme is to increase the rate of a reaction. • Enzymes are important because they act as biological catalysts. This means that they bring molecules together in such a way that they can react.

4. Fast fact • All of the reactions that they catalyze are chemically possible (at least in theory) even in the absence of enzymes. However, in the absence of enzymes, these reactions could not occur fast enough to support life.

5. Info (cont’d) • Enzymes bind temporarily to one or more of the reactants of the reaction they catalyze. In doing so, they lower the amount of activation energy needed and thus speed up the reaction. Catalase is an enzyme reactant that catalyzes the decomposition of hydrogen peroxide into water and oxygen. One molecule of catalase can break 40 million molecules of hydrogen peroxide each second.

6. Carbonic anhydrase is found in red blood cells where it catalyzes the reaction. It enables red blood cells to transport carbon dioxide from the tissues to the lungs. One molecule of carbonic anhydrase can process one million molecules of CO2 each second.

7. In order to work, an enzyme must unite with at least one of its reactants. In most cases, the forces that hold the enzyme and its substrate are noncovalent. A noncovalent bond is a type of chemical bond, typically between macromolecules, that does not involve the sharing of pairs of electrons, but rather involves more dispersed variations of electromagnetic interactions. Four commonly mentioned types of non-covalent interactions include hydrogen bonds, ionic bonds, van der Waals forces, and hydrophobic interactions. The noncovalent interactions hold together the two strands DNA in the double helix, stabilize secondary and tertiary structures of proteins, and enable enzyme-substrate binding and antibody-antigen association

8. Other Inhibitors.. • There are many things that could inhibit a catalytic reaction. Some this include temperature, pH, and whether or not the enzymes are in competition with one another.

9. Hypothesis • The higher the concentration of the alcohol solution, the slower the rate of the enzyme activity will be.

10. Experimental design diagram DV: The rate of the enzyme activity. C: Same amount of liver; same amount of solution;

11. Materials • Beaker • Water • Ethyl alcohol • 6 equally cut pieces of liver • Oxygen probe • 100mL graduated cylinder • 6 Flasks • 10mL graduated cylinder • Scalpel or knife • Hydrogen peroxide

13. Procedures • Add 90mL of water and 10mL of ethyl alcohol to a beaker. Label beaker 1% solution. • Add one piece of liver to a flask. • Once liver is added and labeled, pour in 100mL of solution. • Measure 10mL of hydrogen peroxide and add to the flask. • Quickly attach the oxygen probe to the flask. • Press Start on the Logger Pro programing option. • Give flask a final whoosh and allow it to collect data for 5 minutes. • Repeat steps 1 thru 7 for remaining solutions of concentration.

17. DAta

19. Analysis.. • The data received from this experiment varies too much to make conclusive generalizations. I hypothesized that the concentration of the alcohol solution was directly related to the reaction rate of the enzyme; the higher the concentration level, the slower the reaction time will be. The data collected from this experiment does support my hypothesis but the data varies too much to conclude that it is accurate. The data was collect for a period of 5 minutes. It took the .2% solution 4.75 min +/- .25 min to reach 33.01 which is the maximum amount of oxygen that was able to be created with the given circumstances. It took the .4% solution 3.50min +/- .25 min, .6% solution 4.75 min +/- .25 min, .8% solution 3.00 min +/- .25 min, and the 1% solution 2.25 min+/- .25 min.

20. Limitations • I thought that by conducting this experiment a steady correlation between concentrations would be made. For example, as the concentration increases, the reaction time decreases (my hypothesis) or even an opposing theory, like as the concentration increases, the reaction time is faster. Instead, I received what seemed to be a scatter plot of data. No exact correlation could be made. This can be due to human errors and flaws within my experiment. Although I tried to keep it as close to the time as possible, the time it takes to pour in the alcohol, attach the probe, and press start on the lab pro software varied approx. +/- 4.00 sec. Also, the measurements of the solutions may have been off by +/- .05 mL. All of these things could have affected the array of different figures collected.

21. Changes • One thing that I learned from conducting this experiment is that that there are many things that can inhibit the reaction time of an enzyme. These things include temperature and pH. In hopes of actually attaining conclusive data, a few adjustments can be made. The first thing I would change is the way I collected the data. Instead of using the oxygen probe, I would use the stopper and syringe method. This means that a stopper would be attached to the flask and the syringe to a cord. As oxygen is formed, it would cause the syringe to move. I would then record the oxygen displaced by reading the number on the syringe.

22. Works cited