The Activity of Enzyme Catalase I. Introduction: What is an enzyme? It is! SSa protein serving as a catalyst, a chemical agent that changes the rate of the reaction without being consumed by the reaction!” (Campbell: Reece, 2002).
Each enzyme acts upon a chemical substance called substrate, which fits into the active site (the portion of the enzyme that attaches itself to the substrate) like a lock and key, and is converted into the products during the reaction. Meanwhile the enzyme is released to act on more substrate molecules available. All enzymes! | names usually end with the suffix! S Sase. !” Some examples are lactase, maltase, dehydrogenase, and catalase.
A Catalase enzyme, ! SS serves to protect the cell from the toxic effects of hydrogen peroxide by catalyzing its decomposition into molecular oxygen and water without the production of free radicals!” (Marley, 2001).
In simple terms, it catalyzes the decomposition substrate into products or H 2 O 2 (hydrogen peroxide) into H 2 O and O 2. 2 H 2 O 2 “^3 2 H 2 O + O 2 Many factors can affect enzyme activity including high temperature, low temperature, pH, inhibitors, strong acids, and bases, and certain other chemical substance, which denature with the loss of catalytic activity. The rate of the reaction is reliant on the concentration of the enzyme and the substrate. In the preparation of a catalase enzyme, tissues and organs are homogenized (grounded up) and put into a cold buffer solution. A catalase solution contains: several grams of liver and.
The Essay on Varying Effects of Enzyme Concentration on Reaction Rates of Malate Dehydrogenase
There are two different ways in which a substrate can bind to an active site. The first way is through the lock and key model. Certain substrates can bind only to certain active sites in the lock and key model. This is called the lock and key model because the active site is like the lock and the key is the substrate. Only certain keys can open certain locks. This accounts for the specificity; not ...
01 M sodium phosphate buffer. The measurement of the catalase activity is calculated by observing the time required for 10 ml of O 2 to develop as a result of the action of catalase on H 2 O 2. II. Purpose: To observe and measure the effect of different factors on the rate of an enzymatic reaction through: 1) enzyme concentration; 2) substrate concentration; 3) pH; 4) temperature; and 5) inhibitor. This will help us better understand which effects cell functions, especially since enzyme activity is crucial to cellular functions.
III. Hypothesis: I guessed that the effect of pH and cofactor inhibition would both produce a slower reaction rate than that of the baseline. I hypothesized that the effect of low pH would be slow because the pH of catalase is about 6. 8, and the buffer solution had a pH of 3. 5, which a high pH level can denature the enzymatic activity. I hypothesized that the effect of cofactor inhibition would be the slowest reaction because some enzymes require an inorganic ion like iron to be active.
In this experiment, iron is the cofactor inhibitor, which catalase requires. When iron is removed from the enzyme the activity is decreased and maybe even lost. Therefore, Hydroxylamine inhibits the catalase enzyme by using the iron atoms. IV. Procedure: – Water – 2 10 ml graduated cylinders -600 ml beaker – U-shaped glass delivery tube -rubber tubing – Glass tubing -Rubber stopper – 50 ml Erlenmeyer flask – Reaction mixture (3 ml buffer, 10 ml substrate (H 2 O 2), and 1 ml homogenates (catalase).
For the effect of pH on Enzyme Activity: 1) The experimenter filled one 10 ml graduated cylinders with water, plugged the top of the cylinder with their finger, and inverted it into the 600 ml beaker filled with water being careful not to let any water into the cylinder when removing finger.
The Essay on The Catalase Enzyme
Since we increased the number of discs to increase the concentration, we provided more surface area for the enzyme catalase to break down the hydrogen peroxide. From the results obtained from Group A,B,C and D, shown through the graphs, one can see that as the concentration is increased, as a result of the increase in the number of discs, the rate at which the enzyme breaks down the hydrogen ...
2) The experimenter then placed the one end of the U-shaped glass and rubber tubing instrument into the inverted graduated cylinder. 3) The experimenter then filled the other 10 ml graduated cylinder with 3 ml of the. 003 g/L enzyme, and 10 the substrate (H 2 O 2).
4) Next the experimenter filled the 50 ml Erlenmeyer flask with the three solutions above and quickly placed the other end of the U-shaped glass and rubber tubing with the rubber stopper in place into the Erlenmeyer flask. 5) With another experimenter timing, the experimenter then swirled the flask consistently until O 2 gas began to form inside the inverted 10 ml graduated cylinder.
When the O 2 gas reached 10 ml the time was stopped and recorded. For the effect of Co-Factor Inhibitor: 1) The experimenter filled one 10 ml graduated cylinders with water, plugged the top of the cylinder with their finger, and inverted it into the 600 ml beaker filled with water being careful not to let any water into the cylinder when removing finger. 2) The experimenter then placed the one end of the U-shaped glass and rubber tubing instrument into the inverted graduated cylinder. 3) The experimenter then filled the other 10 ml graduated cylinder with 3 ml of the. 003 g/L enzyme with inhibitor, and 10 the substrate (H 2 O 2).
4) Next the experimenter filled the 50 ml Erlenmeyer flask with the three solutions above and quickly placed the other end of the U-shaped glass and rubber tubing with the rubber stopper in place into the Erlenmeyer flask.
5) With another experimenter timing, the experimenter then swirled the flask consistently until O 2 gas began to form inside the inverted 10 ml graduated cylinder. When the O 2 gas reached 10 ml the time was stopped and recorded. For the Baseline: 1) The experimenter filled one 10 ml graduated cylinders with water, plugged the top of the cylinder with their finger, and inverted it into the 600 ml beaker filled with water being careful not to let any water into the cylinder when removing finger. 2) The experimenter then placed the one end of the U-shaped glass and rubber tubing instrument into the inverted graduated cylinder.
The Term Paper on Enzyme Kinetics Lab Report
This experimentation was to evaluate absorbance and the reaction rate of an enzyme, ‘-amylase in starch-iodine solution. We will be testing the relationship between enzymatic reaction affected by temperature and pH. Through the testing the enzyme at different temperatures, and different pH levels; it would determine at which temperature and pH level the enzyme worked the most efficiently. ...
3) The experimenter then filled the other 10 ml graduated cylinder with 3 ml of the. 003 g/L enzyme, and 10 the substrate (H 2 O 2).
4) Next the experimenter filled the 50 ml Erlenmeyer flask with the three solutions above and quickly placed the other end of the U-shaped glass and rubber tubing with the rubber stopper in place into the Erlenmeyer flask. 5) With another experimenter timing, the experimenter then swirled the flask consistently until O 2 gas began to form inside the inverted 10 ml graduated cylinder. When the O 2 gas reached 10 ml the time was stopped and recorded.
V. Results: From the data collected, the enzyme was affected more by the pH level than the co-factor inhibitor. This tells us that the inhibitor did no change at all, while the pH only affected the enzyme activity slightly. It is unusual because they both had that same pH and the same percent H 2 O 2 (substrate).
The only difference was that the co-factor included an inhibitor of hydroxylamine, which occupied the iron atoms so the catalase could not use it to be active… Discussion: In this experiment, my hypothesis came out to be true.
The results supported my hypothesis. My hypothesis was that the effect on pH would have a slower reaction rate, and the effect of co-factor inhibition would have an even slower reaction rate than that of the baseline. The table and graph above, both show that the data can clearly confirm my hypothesis. I feel that my data is firm and valid, because as the experimenter, I compared notes with other experimenters and found that our data were similarly close. Therefore, I feel very confident and satisfied with my conclusion. Some other experiments I would like to see conducted with topic would be: the enzyme activity of another enzyme such as dehydrogenase or maltase.
Perform the same steps just with a different enzyme and compare those results with those of the catalase enzyme. I guess that the results would be somewhat different, but not drastically. Many things could have caused this experiment to present inaccurate data. Some examples include: not consistently swirling the flask; not having a clean Erlenmeyer flask; not making sure your stopper is securely plugging your Erlenmeyer flask; when inverting your 10 ml graduated cylinder, air was present, and maybe not waiting the full 10 minutes to complete that experiment.
The Term Paper on Enzyme lab
Introduction Enzymes are the ultimate catalysts of living things. Enzymes are made of proteins which are structured and directed by amino acids chains. Enzymes attract and fit substrate molecules to an active site. The active site binds the substrate molecules covalently to enzyme forming an enzyme-substrate complex, which catalyzes the substrate molecule into a product. Enzymes have the ...
Any of these errors could have resulted in inaccurate data. Some answers were answered during this experiment, but some were left unanswered including: Would the high pH result in the same reaction rate? ; and If the inhibitor were changed would there be a reaction rate? An experiment that could be tested to answer these questions would be to try the effect of a high pH solution on the enzyme catalase, and use a different inhibitor on the enzyme catalase, and use the same steps to test it. Then compare those results with those of the previous experiment. The experimenter found this experiment to be fun, and short, but well put together and resourceful.
