Abstract:
Peroxidase is an enzyme that is found in turnips that reacts with hydrogen peroxide. When guaiacol is introduced the reaction turns brown allowing the reaction to be measured through a spectrometer. In this lab the concentration of the enzyme is investigated producing the result that when the concentration is increased so does the rate of the reaction. When boiled in this experiment, the enzymes rate of reaction increases. The rate of reaction in enzymes is dependent on the concentration and temperature.
Introduction: Enzymes are protein macromolecules whose function is to catalyze chemical reactions. In humans enzymes make it possible for reactions in cellular respiration to occur quickly. Enzymes are considered to be highly selective
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First was to create a baseline using 0.1mL of guaiacol, 0.2mL and 4.7mL pipetted into a test tube and 1.0mL of turnip extract and 4.0mL of distilled water pipetted into another. These two test tubes were mixed and immediately poured into a cuvette to collect the progression of the reaction. Once 120 seconds of the reaction is collected record the data. Next was the reaction for 2x enzyme concentrate. The steps are the same as the baseline except 2.0 mL of turnip extract was used. The amount of water is adjusted so the same total amount of mixture created for each reaction is the same. For the ½ x enzyme reaction the steps were repeated again from the baseline except for the turnip extract was .5mL and distilled water was adjusted. After all the data was collected and recorded the next investigation was set up. To determine the effect of boiling the enzyme in its reaction rate, similar steps were executed. A new baseline was created using the same measurements and steps as the first baseline. Once that baseline was created its reaction rate was collected and recorded using a spectrometer. For the experimental variable (boiling enzyme) the measurements were the same as the baseline. Before the two test tubes were combined, both test tubed were placed in a beaker on a hot …show more content…
The baseline produced the slope of 0.0011x and when doubled it produced the slope of the 2x concentration of 0.0022x. When the base line slope of 0.0011x is divided it just about matches the result of the ½ x concentration slope of 0.0005. This shows the whatever the concentration of the enzyme is, it will react as fast as it is concentrated. The second baseline produced the slope of 0.0026x and when compared to the boiled enzyme slope of 0.004x shows that the reaction rate actually increased. This deviates from what is expected, because at that high of a temp it would be expected to not react at all or very slightly. Errors that could have occurred in this experiment are cross contamination. Although steps had been taken to minimize this test tubes were not completely sterilized between different experiments. In regards to the boiling enzyme the enzyme may not have been in the boiling water long enough to produce the results expected. The hypothesis is partially supported, when the enzymes concentration is altered the rate of reaction correlates to the the concentration. The hypothesis however is not supported when discussing how boiling the enzyme effects the rate of reaction. The enzymes rate of reaction actually increases when boiled, contrary to the
As pH increases or decreases to get closer to the optimal pH --in this case it is 7 for this particular enzyme-- the rate of reaction peaks and is highest at that point, which is described by the molecular shape and structure of the enzyme at its optimal pH. When turnip peroxidase is at pH 7, the active site is able to fit perfectly with the substrate, therefore explaining why the reaction rate is fastest at this point. Accordingly, if the active site is disrupted, the substrate cannot fit perfectly causing the reaction rate to slow down. This can be supported by the data because the reaction rate gradually increased from pH 3 to pH 7 and reached its maximum at pH 7. Once it did reach the optimal pH, the reaction rate continuously decreased
Note the gradient of the line Exit the linear regression dialog and store the latest run data Add 2, 3, 4 drops of enzyme catalase solution to test tube 2, 3, 4 respectively and repeat the above procedure for each test tube. Access other groups results and fill table 4 RESULTS In this experiment it was found that increase in number of drops of enzyme suspension led to increased pressure as shown in the table 3.
After record your data and determine the absolute rate of the enzyme-catalyzed reaction. Based on the data and observations the hypothesis was accepted. It was accepted because when pH were changed to a variety of levels the transmittance began to get higher reaction rates. The increased absorbance means greater amount of product and a higher reaction rate will be produced.
It was hypothesized that the optimal pH for the enzyme was pH 7 while the 1.0 ml peroxidase would have the best reaction rate. At the end of the experiment the results prove the hypothesis to be incorrect. INTRODUCTION Enzymes are proteins that allow a reaction to speed up. These proteins are made up of monomers known as amino acids.
A control extract is prepared (5ml of DAE) to a test tube, which is then placed in boiling waterbath for 10minutes, after 10minutes remove the control extract and leave it to cool at room temperature. In order to determine the amylase activity, one drop of iodine is dropped into 21 labelled wells on the ceramic test plates. A reaction mixture is prepared, 5ml of buffer and 1ml of 0.5% starch solution to a test tube. Extract one drop from the reaction mixture to the well labelled T.
I) Introduction This lab was designed to test what effect multiple temperatures would have on the activity of an enzyme. It’s scientifically known that there’s a positive correlation between temperature and an enzyme’s rate of reaction. In other words, as temperature increases, so too does the rate of reaction of an enzyme.
Enzymes are a form of protein that lowers activation energy and speeds up reactions as a catalyst. They are made by the stringing together of an abundant amount of amino acids and folded into a specific shape for chemical reactions. Turnip Peroxidase is the enzyme used in this lab and is derived from the vegetable. Enzymes are not used up or permanently altered by their environment Peroxidases are found in a range of organisms and function to break down alcohol (H2O2) and creates byproducts of oxygen and water. In this experiment, the reducing agent guaiacol is added with the substrate, hydrogen peroxide, to create water and oxygen.
The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.
Objective: The purpose of this experiment is to determine the changes in activity level (if any) when enzymes are exposed to a variety of environments (in this case, temperature). Introduction: Enzymes are made up of a series of proteins known as amino acids. Enzymes are essential in almost all aspects of life.
purpose the propose of this experiment was too see if the chemical reaction of a enzyme can be made faster. Hypothesis I think that a warm environment would be best to make an enzyme’s reaction faster. because a protein can move faster in heat.
5 water bath were set up each to10 °C. (5 were used do the experiment faster) 5 cm3 of starch solution were added into the 5 test tubes that were labeled test tubes. Then 5 cm3 of amylase enzyme was added into the other 5 test tubes that were labeled. Put one of the starch solution test tube (preferably the one labeled 1) and one of the test tube containing amylase into the water bath (10 °C).
There are many factors which affects the rate of an enzyme catalyzed reaction. The rate of an enzyme controlled reaction is measured by 1.The amount of substrate change per unit time 2.The amount of product formed per unit time 3. The time taken for the completion of the reaction In investigating the effect of one factor : All the factors should be kept constant They must be maintained at suitable levels Only the initial rate should be measured.
H20 + 2 O2 This experiment will use 1% catalase solution and 3% hydrogen peroxide solution, both diluted into water so the reaction slows down. Temperature will be controlled in this experiment to change the reaction speed of the enzyme and the substrate, this is what the experiment is looking at. The effect of the temperature will be determined by how much gas is released in two minutes, which will change the pressure inside the test tube and will be measured by a gas
By observing figure 3, the more enzyme that is available, the faster the reaction rate is. The optimal enzyme concentration was chosen based on the R2 values from figure 2. The highest observable rate also had the best R2 number, which was closest to one. This enzyme concentration was used in part 2.
The 3 concentrations of enzymes were 0.5 ml, 1.0 ml, and 2.0 ml of turnip extract, while the substrate consisted of 0.1ml, 0.2 ml, and 0.4 ml of hydrogen peroxide. In a separate tube, the control was made up of turnip extract and guaiacol, known as the color reagent. This was recorded the absorbance every 20 seconds for 3 minutes.