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Catalase activity on hydrogen peroxide
Catalase activity on hydrogen peroxide
The effect of catalase on hydrogen peroxide
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Discussion
The data from the experiment supports the hypothesis that as the hydrogen peroxide concentration increases, the rate of reaction will increase until it reaches equilibrium. The rate of reaction follows the similar trend of rapidly increasing until reaching a plateau, as shown in Figure 4. The catalase reaction rate grew exponentially from 0.00 s-1 at 0 v/v% to 0.77 s-1 at 3 v/v%, and then the reaction rate significantly slows down to 0.65 s-1 at 5 v/v% (Figure 1 and 2).
Figure 4: The relationship between increasing substrate concentration and the rate of reaction of the enzyme. The effect of increasing hydrogen peroxide concentration on the activity of catalase follows the same trend (RCS, n.d.).
However, there were not enough samples
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However, it is possible for the rate of reaction to slow down and reach equilibrium, the state where the reaction rate is not increasing nor decreasing, for several reasons (Worthington Biochemical Corporation, 2015). The main reason that this may occur is from the ratio between enzymes and substrates. If the substrate concentration is too high, there would not be enough enzymes to catalyse the reactions, after which the reactions could only go at the reaction rate for that number of enzymes (Crierie & Gregg 2010 p.24-27). Other reasons may be inhibitors or environmental factors, such as pH and temperature (Crierie & Gregg 2010, p.27). In this practical, as the concentration increased, the amount of yeast enzyme catalase did not significantly change, thus making it impossible for the graph to be exponentially …show more content…
Enzyme activity is impacted by temperature; the colder it gets, the slower the enzyme activity (Crierie & Gregg 2010, p.26). In this experiment, the solutions were tested from 0 v/v% to 5 v/v%, meaning that 5 v/v% were done last. This would mean that the enzyme activity would be slower at that point than it was at the beginning of the lesson, when 0 v/v% was tested. This may have impacted on the 5 v/v% data, because it was slightly lower than expected (the expected level was near 3 v/v% data
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
In both solutions of catalase there is a steady increase in reaction relative to the hydrogen peroxide concentration as it increases. A significant jump is observed in the carrot catalase solution between .25% and .5% whereas the pinto bean catalase solution has a steady increase. Each solution doesn’t generate much more reaction to the next increment of hydrogen peroxide concentration, 1%. In general it stayed level. This continued to be a trend for the pinto bean catalase solution, plateauing through to the 6% concentration of hydrogen peroxide. This is known as the point of saturation.
The rate law determines how the speed of a reaction occurs, thus allowing the study of the overall mechanism formation in reactions. In the general form of the rate law, it is A + B C or r=k[A]x[B]y. The rate of reaction can be affected by the concentrations such as A and B in the previous equation, order of reactions, and the rate constant with each species in an overall chemical reaction. As a result, the rate law must be determined experimentally. In general, in a multi-step reaction, there will be one reaction that is slower than the others.
The Effect of Temperature on the Activity of the Enzyme Catalase Introduction: The catalase is added to hydrogen peroxide (H²0²), a vigorous reaction occurs and oxygen gas is evolved. This experiment investigates the effect of temperature on the rate at which the enzyme works by measuring the amount of oxygen evolved over a period of time. The experiment was carried out varying the temperature and recording the results. It was then repeated but we removed the catalase (potato) and added Lead Nitrate in its place, we again tested this experiment at two different temperatures and recorded the results. Once all the experiments were calculated, comparisons against two other groups were recorded.
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).
Hydrogen Peroxide does not need the enzymes in the catalase to separate into Oxygen and Water. The catalase are only used to increase the rate of reaction.
Investigating Factors that Affect the Rate of Catalase Action Investigation into the factors which affect the rate of catalase action. Planning Aim: To investigate the affect of concentration of the enzyme catalase on the decomposition reaction of hydrogen peroxide. The enzyme: Catalase is an enzyme found within the cells of many different plants and animals. In this case, it is found in celery.
Many factors, for example, pH and temperature affects the way enzymes work by either increasing the rate or determining the type of product produced (). The report, therefore, analyses the effects of the enzyme peroxidase in metabolic reactions and determining its optimum temperature in the reactions.
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...
The results of this experiment showed a specific pattern. As the temperature increased, the absorbance recorded by the spectrophotometer increased indicating that the activity of peroxidase enzyme has increased.At 4C the absorbance was low indicating a low peroxidase activity or reaction rate. At 23C the absorbance increased indicating an increase in peroxidase activity. At 32C the absorbance reached its maximum indicating that peroxidase activity reached its highest value and so 32 C could be considered as the optimum temperature of peroxidase enzyme. Yet as the temperature increased up to 60C, the absorbance decreased greatly indicating that peroxidase activity has decreased. This happened because at low temperature such as 4 C the kinetic energy of both enzyme and substrate molecules was low so they moved very slowly, collided less frequently and formed less enzyme-substrate complexes and so little or no products. Yet, at 23 C, as the temperature increased, enzyme and substrate molecules
The Effect of pH on the Activity of Catalase Planning Experimental Work Secondary Resources Catalase is a type of enzyme found in different types of foods such as potatoes, apples and livers. It speeds up the disintegration of hydrogen peroxide into water because of the molecule of hydrogen peroxide (H2O2) but it remains unchanged at the end of the reaction.
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.
How the Concentration of the Substrate Affects the Reaction in the Catalase Inside Potato Cells Introduction Enzymes are made of proteins and they speed up reactions, this means that they act as catalysts. Hydrogen peroxide is a byproduct of our cell's activities and is very toxic. The enzymes in our bodies break down the hydrogen peroxide at certain temperatures they work best at body temperature, which is approximately 37 degrees. At high temperatures, the cells begin to denature. This means that the hydrogen peroxide is prevented from being broken down because they will not 'fit' into the enzyme.[IMAGE] Objective I am going to find out how the concentration of the substrate, hydrogen peroxide affects the reaction in the catalase inside the potato cells.
At low substrate concentration, most of these active sites remain unoccupied at any time. As the substrate concentration is increased ,the number of active sites which are occupied increases and hence the reaction rate also increases however at very high substrate concentration, virtually all the active sites are occupied at any time so that further increase in substrate concentration cannot further increase the formation of enzyme-substrate complex.