What is the function of enzymes in a living system?
Enzymes speed up metabolic reactions necessary for life. Without them certain vital processes would not take place and the body would be unable to function.
Difference enzymes work better under different conditions. Where in a human body might it be beneficial to have enzymes work in very acidic environments?
In areas, like the stomach, that have a pH of two would benefit by having enzymes that function well in acidic environments. An example of such an enzyme is pepsin.
There is a large amount of catalase found in a human liver. Does the liver break down more hydrogen peroxide in the summer or winter? Explain your answer.
More hydrogen peroxide will be broken down in the summer
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Potassium permanganate - used to titrate and determine the amount of decomposed hydrogen peroxide.
Sulfuric acid - was used to stop the reaction with catalase and hydrogen peroxide. It denatured the enzyme (catalase) and halted the reaction so the amount of hydrogen peroxide decomposed could be measured.
Before performing part D of the experiment, why was it necessary to establish a baseline?
The baseline is a control and shows the amount of decomposed hydrogen peroxide in the initial sample.
You may have observed the reaction of naturally-occurring catalase in tissue from either liver of potato. Design an experiment to determine if the amount of catalase varies from tissue to tissue (e.g. 200 g of liver compared to 200 g of potato).
Put the 100 g of potato in 1 petri dish and 100 g of liver in another petri dish. Then put equal amounts of hydrogen peroxide for an equal period of time in both dishes. Drain the dishes and titrate them with potassium permanganate simultaneously. The numbers can now be compared using the steps in the sample calculation above in the lab report. In order to compare perform a potassium permanganate titration on pure hydrogen peroxide.
Of the thousands of enzymes known, there is a family of enzymes called proteases that catalyze a reaction of breaking down proteins. What do you think would happen if you added a protease to your sample of catalase before proceeding with your experiment?
The catalase would be broken
The preparation for the experiment started by gathering the solutions of enzyme Peroxidase, substrate hydrogen peroxide, the indicator guaiacol and distilled water. Two small spectrometer tubes and three large test tubes with numbered labels. In addition, one test tube rack, one pipet pump and a box of kimwipes were also gathered. Before the experiment, the spectrometer must be set up to use by flipping the power switch to on. Following, the machine was warmed up for 10 minutes and the filter lever was moved to the left. In addition, I set the wavelength to 500 nm with the wavelength control knob. Before the experiment, I had to create the blank solution by pipetting 0.1 ml of guaiacol, 1.0 ml of turnip extract and 8.9 ml water into tube #1. Following the creation of the blank, a control 2% solution was created.
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
There are many types of enzymes and each has a specific job. Enzymes are particular types of proteins that help to speed up some reactions, such as reactants going to products. One of them is the amylase enzyme. Amylases are found in saliva, and pancreatic secretions of the small intestine. The function of amylase is to break down big molecules of starch into small molecules like glucose; this process is called hydrolysis. Enzymes are very specific; for example, amylase is the only enzyme that will break down starch. It is similar to the theory of the lock
The topic of this lab is on biochemistry.This experiment was conducted to show how cells prevent the build of hydrogen peroxide in tissues. My group consisted of Lekha, Ruth, and Jason. There were used two different concentrations of hydrogen peroxide through this experiment , 1.5% and 3%. By testing two different types it is easier to understand how the H2O2 and catalase react with one another. To do this both the yeast, which was our catalase, and H2O2 were mixed together in a beaker. Each concentration was tested out twice for more accurate results . 1.5% concentrated H2O2 had an average reaction rate of 10.5 seconds while 3% concentrated H2O2 had an average reaction rate of 7.5 seconds. From this experiment we learned that by increasing the concentration of H2O2 and chemically combining it with a catalase it will speed up the reaction. Enzymes speed up chemical reactions . The independent variable in this experiment was the concentration of the H2O2. Some key vocabulary words are Catalase, enzyme, hydrogen peroxide ( H2O2), and concentration.
Enzymes are biological catalysts, which speed up the rate of reaction without being used up during the reaction, which take place in living organisms. They do this by lowering the activation energy. The activation energy is the energy needed to start the reaction.
These results shown from this experiment led us to conclude that enzymes work best at certain pH rates. For this particular enzyme, pH 7 worked best. When compared to high levels of pH, the lower levels worked better. The wrong level of pH can denature enzymes; therefore finding the right level is essential. The independent variable was the amount of pH, and the dependent being the rate of oxygen. The results are reliable as they are reinforced by the fact that enzymes typically work best at neutral pH
There were three test tubes in which the experiment was held. A relatively equal sized portion of raw potato (this contained the enzyme [a biological catalyst] hydrogen peroxidase) was placed in each tube. Then, enough water to cover the potato was added. Proceeding this, each of the test tubes were assigned a temperature; cold, room temperature or warm (this was written on the tag so that they were not confused). The test tube destinated ‘cold’ was placed in a ice bath for five minutes. At the same time, the ‘hot’ test tube was placed in a hot water bath for five minutes. Meanwhile, the room temperature test tube sat at room temperature for five minutes. When the five minutes were over, the test tubes were returned to the rack (so that they were able to be observed). Then, the test tubes were allowed to sit at room temperature for five more minutes. Once that period of time was over, 2 ml of hydrogen peroxide (the substrate) was added to each tube.
We hypothesized that a medium pH buffer added to the hydrogen peroxide an peroxidase reaction would be the best condition for the enzyme activity due to it being the more neutral than the high, being basic, and low, being acidic, pH.
The aim of my investigation is to see how pH affects the activity of potato tissue catalase, during the decomposition of hydrogen peroxide to produce water and oxygen.
Enzymes are biological catalysts, which accelerate the speed of chemical reactions in the body without being used up or changed in the process. Animals and plants contain enzymes which help break down fats, carbohydrates and proteins into smaller molecules the cells can use to get energy and carry out the processes that allow the plant or animal to survive. Without enzymes, most physiological processes would not take place. Hundreds of different types of enzymes are present in plant and animal cells and each is very specific in its function.
Abstract: Enzymes, catalytic proteins that at as catalysis which makes the process of chemical reactions more easily. There are two main factors that actually affects enzymes and their functions which are temperature and pH. Throughout this experiment, the study how pH and peroxidase affects each other and the enzyme was made. The recordings of how the enzymes responded when it was exposed to four different pH levels to come up with an optimum pH which was predicted in the hypothesis and the IRV at the end.
Observing how the enzyme catalase found in chicken and beef livers breaks down hydrogen peroxide at varying pH levels and temperatures.
The experiments involved PH buffers of different pH were added to potato juice, water, and the enzyme catecholase. The mixture was then subjected to spectrophotometer at a wavelength of 420nm taking the absorbance readings. In the second experiment, a phosphate buffer of PH 7.0 was used in different measures together with different measurement of potato juice and the enzyme catecholase then subjected to the spectrophotometer at a wavelength of 420nm. The data collected inform of table and analyzed using descriptive statistics such as line graph and later interpreted, showing that PH and enzyme concentration do affect the rate of enzyme reaction
In the exercise # 2 we observed the effect of substrate concentration, enzyme concentration, pH and temperature on enzyme activity. All the data showed that once potato extract was added to catechol and water the reaction varied dependent on the level of catechol. As in
This experiment is designed to analyze how the enzyme catalase activity is affected by the pH levels. The experiment has also been designed to outline all of the directions and the ways by which the observation can be made clearly and accurately. Yeast, will be used as the enzyme and hydrogen peroxide will be used as a substrate. This experiment will be used to determine the effects of the concentration of the hydrogen peroxide versus the rate of reaction of the enzyme catalase.