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Cellular respiration research paper
Cellular respiration research paper
Cellular respiration research paper
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Thorough analysis of the graph displayed enough evidence suggesting that an increase in substrate concentration will increase the height of bubbles until it reaches the optimum amount of substrate concentration, resulting in a plateau in the graphs (figure 2). Hence; supported the hypothesis. Acting as the controlled group to lessen the effects of all variables except the independent variable, at 0% concentration, the height of foam produced is 0 mm. Attributions to these results is because at 0% substrate concentration, no molecules were present to occupy all the available active sites. As an outcome, the final volume of oxygen is none since there were no collisions taken place between the enzymes and substrate. Therefore, prevented the number of collisions to reach the activation energy. However, at 3% substrate concentration, the hydrogen peroxide decomposition showed an immediate peak of up to 3.8 mm in height. As the substrate concentration slowly increased, enzyme …show more content…
This evidence alone suggests that higher increases in substrate concentration causes smaller and smaller increases in enzyme activity. As substrate concentration increases further, some substrate molecules may have to wait for an active site to become empty as they are already occupied with a substrate molecule. So, the rate of the reaction starts to level off resulting in a plateau in the graphs. This means that the reaction is already working at its maximum rate, and will continue working at that rate until all substrates are broken down. The only way the reaction rate would increase, is if more enzyme was added to the solution. This confirms that increases in substrate concentration above the optimum does not lead to greater enzyme activity. Therefore, the rate of reaction is in proportion to the substrate
For example, substrate concentration, enzyme concentration, and temperature could all be factors that affected the chemical reactions in our experiment. The concentration of substrate, in this case, would not have an affect on how the bovine liver catalase and the yeast would react. The reason why is because in both instances, the substrate (hydrogen peroxide) concentration was 1.5%. Therefore, the hydrogen peroxide would saturate the enzyme and produce the maximum rate of the chemical reaction. The other factor that could affect the rate of reaction is enzyme concentration. Evidently, higher concentrations of catalase in the bovine liver produced faster reactions, and the opposite occurs for lower concentrations of catalase. More enzymes in the catalase solution would collide with the hydrogen peroxide substrate. However, the yeast would react slower than the 400 U/mL solution, but faster than the 40 U/mL. Based on this evidence, I would conclude that the yeast has a higher enzyme concentration than 40 U/mL, but lower than 400
For the heat inactivation, two sets of 11 tubes were set up. The indicated amounts of buffer, water, and ONPG listed in table 10 were added to each tube. In addition, the control enzyme (0.1ml) was added to each tube of the control set and the same amount of heated enzyme was added to each tube of the heated set. The absorbance readings were taken and recorded in table 10. Finally, two Lineweaver-Burk plots were created. The plot for the heated set is represented by graph 10 and graph 11 represents the control set. The Km and the Vmax for the heated set and the control set were determined.
EDTA, the chelating agent that binds with magnesium, had a high absorbency and strong color change to red. The correct cofactor was copper which with the chelating agent of PTU and citric acid which both bind strongly to copper which keeps it from binding with the enzyme. This was determined because in the trails, both PTU and citric acid had low absorbency and were clear or roughly clear in color. The catechol in each tube, which was the control for this experiment, allowed the cofactor that would be used in this reaction to be singled out. The way each chelating agent would affect the different cofactors displayed which was not needed for the reaction and which cofactors were needed for the reaction. An inconsistency that may have affected the data would be if the calibration tube malfunctioned in balancing the spectrophotometer to zero. There also could be errors if the calibration tube wasn’t used before each tube was tested in the spectrophotometer. The relationship of the cofactor and amount of enzyme activity would be that if the cofactor is inhibited or not, the enzyme activity would be higher if the cofactor is not inhibited but lower if it was inhibited by the chelating
Purpose: The purpose of this lab is to explore the different factors which effect enzyme activity and the rates of reaction, such as particle size and temperature.
Investigating the Effect of Substrate Concentration on Catalase Reaction. Planning -Aim : The aim of the experiment is to examine how the concentration of the substrate (Hydrogen Peroxide, H2O2) affects the rate of reaction. the enzyme (catalase).
According to the graph on amylase activity at various enzyme concentration (graph 1), the increase of enzyme dilution results in a slower decrease of amylose percentage. Looking at the graph, the amylose percentage decreases at a fast rate with the undiluted enzyme. However, the enzyme dilution with a concentration of 1:3 decreased at a slow rate over time. Additionally, the higher the enzyme dilution, the higher the amylose percentage. For example, in the graph it can be seen that the enzyme dilution with a 1:9 concentration increased over time. However, there is a drastic increase after four minutes, but this is most likely a result of the error that was encountered during the experiment. The undiluted enzyme and the enzyme dilution had a low amylose percentage because there was high enzyme activity. Also, there was an increase in amylose percentage with the enzyme dilution with a 1: 9 concentrations because there was low enzyme activity.
The [ES] complex can then undergo two different pathways; the complex can dissociate to [E] and [S], at a rate of k or it can shift equilibrium to the left with a rate constant of k2 to form [E] and product [P]1. In this model, the breakdown of the ES complex to yield P is the overall rate-limiting step. Three assumptions of a Michaelis-Menton plot are that a specific [ES] complex in rapid equilibrium between [E] and [S] is a necessary intermediate, the amount of substrate is more than the amount of enzyme so the [S] remains constant, and that this plot follows steady state assumptions. Steady state assumptions states that the intermediate stays the same concentration even if the starting materials and products are constantly changing.2 The rapid equilibrium between enzyme and substrate, and the enzyme-substrate complex yields a mathematical description regarded as the Michaelis-Menton
Investigate the Effect of pH on Immobilised Yeast Cells on the Breakdown of Hydrogen Peroxide
First, a molecule of hydrogen peroxide oxidizes the heme to an oxyferryl species. One oxygen atom is extracted and attached to the iron atom, and the rest is released as harmless water. Then, a second hydrogen peroxide molecule, which acts as a decreasing proxy to regenerate the resting enzyme state, is also broken apart and the pieces are combined with the iron-bound
How the Concentration of the Substrate Affects the Reaction in the Catalase Inside Potato Cells
site) then the quicker the starch (substrate) will be broken. down, resulting in a faster reaction rate. Therefore, a smaller amount. of amylase will result in a slower reaction rate. [ IMAGE] Text Box: Fischerâ€TMs †Lock and Keyâ€TM hypothesis (1890).
The reaction will increase with the increasing enzyme concentration when the molecules of hydrogen peroxide are freely available. The more concentrated the catalase the more chance of the
Enzymes are very specific in nature, which helps them in reactions. When an enzyme recognizes its specific substrate, the enzyme binds to the substrate in a region called the active site which is made of amino acids. Once the substrate binds, the enzyme changes its shape slightly to make an even tighter fit around the substrate, This is called induced fit and it allows for the enzyme to catalyze the reaction more easily. Another factor contributing to catalyses is the amount of substrate present; the more substrate molecules available, the more often they bind the active site. Once all of the enzyme's active sites are occupied by substrate, the enzyme is saturated ( Campbell 99). Enzyme's have optimal conditions under which they perform. These include temperature, pH, and salt concentration, amongst others. In this lab we only focused on pH and temperature. Each enzyme is specific to a certain optimal temperature and pH. When conditions are favorable, the reaction takes place at a faster rate, allowing for more substrates to collide with active sites of enzymes. However, if conditions get too extreme, the enzyme...
In this lab, it was determined how the rate of an enzyme-catalyzed reaction is affected by physical factors such as enzyme concentration, temperature, and substrate concentration affect. The question of what factors influence enzyme activity can be answered by the results of peroxidase activity and its relation to temperature and whether or not hydroxylamine causes a reaction change with enzyme activity. An enzyme is a protein produced by a living organism that serves as a biological catalyst. A catalyst is a substance that speeds up the rate of a chemical reaction and does so by lowering the activation energy of a reaction. With that energy reactants are brought together so that products can be formed.