By doing this laboratory about enzyme activity, the data about the five main factors that have an effect on the rate of enzyme activity was easier to comprehend. Before understanding those concepts, it's essential to understand the backdrop information of the substances associated with this lab. To be able to have a larger notion of the lab and a better understanding of why it was done, one must interpret the overall functions of enzymes and catalase.
There are numerous substances found in human physiques that help different organisms function properly. One important element that is found in human bodies is called an enzyme. An enzyme is a protein-based health proteins that acts such as a catalyst, which is a substance that speeds up a chemical effect without having to be effected, in the reactions within the body (Wise Geek). For instance, the enzyme found in saliva reduces the food in order for it to break down in the torso. Without this enzyme, it would take weeks for your body to digest the food alone (Wise Geek).
The way that enzymes work is simple to visually identify. When two molecules react with each other, they must connect in some way. The substances have to collide in the right orientation and with enough sufficient energy, and therefore the energy between the molecules must be there, for the collision to occur. This type of energy is called the activation energy. A component in an enzyme that gets the specific shape and functional categories to join to 1 of the responding molecules is the productive site. When the enzyme attaches to a specific substrate, the reactants of the effect, this is when the enzyme speeds up the procedure and the binding of the substrate and enzyme is named an enzyme-substrate complex (Shiny Hub).
Catalases are enzymes that are commonly present in most living organisms and are very strong catalysts. Catalase helps your body break down hydrogen peroxide, a unsafe oxidizing agent within your body, into oxygen and water. This avoids the buildup of skin tightening and bubbles in the bloodstream (eHow). The cellular function of the catalase is like the function of white blood vessels cells in the torso; the white bloodstream cells battle trojans in human body while catalase battles the effect of free radicals in the body. Free radicals are unpredictable molecules within the body that produce other substances very unstable and can harm protein, cell membranes and DNA structure. Thus, catalase battles against the result of these molecules by transforming them into hydrogen peroxide, and then later breaking it into air and normal water (eHow).
There are various kinds of enzymes, including anabolic and catabolic enzymes, and the reactions that are followed with them. Anabolic reactions are participating with creating large substances out of smaller molecules and catabolic reactions breakdown large substances into smaller molecules (Nelson Biology 12). The activation energy in virtually any type of effect lowers because of the catalysts that can be within the reactions. Enzymes play an important role in terms of bringing down activation energy and aren't used by the reaction (Nelson Biology 12).
However, there are five main factors that influence the activity of enzymes, whether it's positive or negative. These five factors are the reasons due to the completion of this particular laboratory and the info that is compiled about these factors give further knowledge of why each factor occurs. The five main factors are: change in enzyme attention, temperatures, pH, substrate focus and the addition of an inhibitor.
From the information about enzymes and catalase provided, it'll now be much easier to understand the basis of this laboratory. The point of this lab was to figure out how different environmental conditions would have an effect on the activity of the enzyme. Together with the provided information at heart, the reasoning behind the results of this laboratory will further be interpreted and the factors that have an impact on enzyme activity will be much easier to understand.
Analysis: Movements and Patterns
The developments and patterns that were found in this experimental lab are intertwined with one another and help one understand more about enzyme activity. Despite the fact that there are five split factors that influence enzyme activity, all of them are connected for some reason and the provided data shows this interconnection.
The design that was within this area of the laboratory was that the temp of 35C was the perfect temperature throughout this experiment and was the heat range at which the speed of change was at its highest point. Which means that when the temperature was either higher or lower than 35C, the speed of change would decrease.
The style that was found for this part of the lab relates with the area of the lab that once was brought up, change in heat. The pH level of 7 was the control (maximum pH value) and any pH lower or more than 7, the speed of change would lower.
The style that was observed in this part of the lab was nearly the same as Factor 1: Change in enzyme focus. The bigger the ratio of substrate attention (H202 attentiveness), a lot more increased the pace of change was.
The style that was found in this part of the lab involved inhibitors, chemicals that prevent productive sites on enzymes. The larger the quantity of inhibitor (copper II sulfate) that was put into the enzyme attentiveness, the slower the rate of change was.
Before doing the laboratory, certain hypotheses were made for every factor that impacts enzyme activity. Based on the data that was already given about enzymes, the hypotheses which were made were the best to represent that which was predicted to occur in each part of the lab.
For Part 1: Change in enzyme attention, if the enzyme awareness was decreased in an H202 decomposition reaction, then your rate of change will also lower. This hypothesis was made based on this part of the lab because if the composition wasn't real enzyme solution, it could affect the rate of change. This hypothesis was turned out according to Desk 1: Change in enzyme awareness; the 20% focus of potato juice (2 mL potato drink and 8 mL distilled normal water) had the lowest rate of change value. This structure was the one which had minimal amount of enzyme solution; this structure only got 2 mL of enzyme focus. This links with the hypothesis because the low the enzyme amount, the lower the pace of change. Also, at a low enzyme concentration, there's a great deal of active sites and the speed of the effect is low. As the enzyme attention boosts, there are more vigorous sites and thus, the response will precede faster (S-Cool). Therefore, the entire trend that was portrayed in this area of the lab was that as the focus of the enzyme increased, the pace of change also increased.
For Part 2: Change in temps, if the temps was higher or lower than 37 C, which is the optimal temperature in living organisms (Nelson Biology 12), then your rate of change would reduce. This hypothesis was correct except for one feature: the optimal temperatures in this part of the lab was 35C rather than the standard optimal heat range in microorganisms which is 37C. The rest of the hypothesis was appropriate because when the temperatures that was either higher or lower than 35C, the speed of change decreased. When the temps was higher than the optimal temps, this was due to the denaturing of the perfect solution is. When the heat was lower than the optimal temp, this was brought on because of the short amount of kinetic energy required for the reaction to take place faster (RSC).
Referring to Figure 2: Change in temps, when the heat was either higher or less than the optimal temperature, the pace of change would decrease. Quite simply, as the temperature rises, the substances that were responding would have more kinetic energy. Since the molecules have more energy, this might increase chances of collisions between your molecules and for that reason would increase the rate (RSC). This data correlates with the hypothesis since when the optimal temp was not come to, the pace of change was lowered. The overall development that was decided for this part of the experiment was that if the temp was higher or less than the optimal heat (35C), the pace of change would lower.
Regarding Part 3: Change in pH, if the pH (optimal pH is 7) was higher or lower than the optimal pH, the speed of change would reduce. This hypothesis was became right because when the pH was either 2, 4, 9 or 12, the rate of change would be less than the speed of change at the pH of 7. This hypothesis is linked to the hypothesis partly 2: Change in heat because they both have the same characteristics as it pertains to impacting enzyme activity. Referring to Stand 3: Change in ph, when the pH value was either higher or lower than 7, the speed of change would decrease. In the same way with the change in temperatures, changes in the pH value would make but also break intermolecular and intramolecular bonds. By changing the bonds, this might also change the form of the enzyme and change the enzymes efficiency (RSC). Thus, when the perfect pH is not being used, the pace of change will be lowered due to denaturing of the enzyme (Nelson Biology 12). The general trend that was within this part of the lab pertains to Factor 2: Change in heat, as they both talk about the same characteristics in the terms of the given data. The bigger or lower the pH value was from the perfect pH value, the rate of change would be reduced.
For Part 4: Change in substrate concentration, if the substrate concentration was increased in a decomposition response with catalase, the pace of change would also increase. This hypothesis was correct because when the highest awareness was used, 3%, the pace of change was also the best, 1. 27 cm/s. Since there is more substrate solution, H202, the rate of change was also the highest of the many other concentrations. Referring to Figure 4: Change in substrate focus, this figure is similar to Figure 1: Change in enzyme attention because as the awareness increased, so does the rate of change. The overall pattern that was found in this part of the lab was just like Factor 1: Change in enzyme attention from the provided data. Relating to the dynamic sites in terms of the rate of the response, when the substrate awareness is low, this means that there are less lively sites being occupied and this does mean that the pace of change is also low. When more substrate molecules are added, additional enzyme-substrate complexes are created. Therefore, as there's a bigger amount of effective sites, the pace of change rises (S-Cool). In other words, as the focus of the substrate solution is increased, the pace of change also increased.
For Part 5: Addition of your Inhibitor, if the amount of the inhibitor was increased, the rate of change would reduce. This hypothesis was also right because based on the data already known about inhibitors, it was clear that the more inhibitor that is placed into a remedy, the slower the perfect solution is would behave. The inhibitor in cases like this was the copper II sulfate and this hypothesis was appropriate because the more drops of copper II sulfate that was added to the enzyme solution, a lot more the pace of change lowered. Since an inhibitor is meant to block dynamic sites of enzymes, this characteristic would have an impact on the rate of change and make it lower. There are two types of inhibitors: competitive and noncompetitive inhibitors. Competitive inhibitors penetrate in to the enzyme's productive site and block the substrate form binding. Noncompetitive inhibitors join to another site on the enzymes which creates a change in the enzyme's condition. The change in form triggers lose of resemblance for the substrate (Nelson Biology 12). In other words, as more inhibitor is added, the availability of active sites reduced since the inhibitors stop normal substrates from binding and changes the form of the enzyme.
The hypotheses which were made for each area of the lab had become correct based on the information provided about factors impacting enzyme activity. Each hypothesis was turned out by the info that is provided in the Evaluation: Desks & Information and that also provide a visual representation of every hypothesis.
Evaluation: Resources of Error
Not every experiment is absent of errors but by observing these errors, experiments can be carried out more accurately in the foreseeable future. There have been many errors that were found throughout the laboratory; however these specific resources of errors will be the ones which were resources of errors rather than real human errors.
Inconsistency of pushing the filter newspaper down in a test tube- after dipping the filtration paper in to the enzyme solution, the filter paper needed to be pushed right down to the bottom of the test tube with the substrate solution. One important aspect of the laboratory was to time how much time the filter newspaper took to rise back to the top of the meniscus of the perfect solution is. However, forcing the filter paper to the bottom of the test pipe was inconsistent each time it was done. To improve this error in the future, other materials might have been used to assist the filter paper to go right to the bottom of the test pipe somewhat than floating back again to the top, such as materials such as a scoopula or any other materials that is long long.
Test pipes measurements - for every single area of the lab, the measurement of the enzyme and substrate alternatives were made and poured into a test pipe. Even though the volume of the perfect solution is was easy to ascertain by by using a graduated cylinder, the distance (distance) of the perfect solution is was inaccurately measured. The usage of a ruler made the measurements of the perfect solution is imprecise and was an occurring source of error for each part of the lab.
Amount of inhibitor in the solution - For Part 5: Addition of your Inhibitor, the copper (II) sulfate was fell into the test pipe as the inhibitor and this part of the test was inconsistent due to the amount of inhibitor that was released into a remedy every time. A dropper isn't a reliable piece of materials in this lab because of the fact that it may take more inhibitor at onetime and a less amount the next time.
These three main problems that were made during this area of the lab might have been averted if more attention and details was placed into the test. However, mistakes that occur during an experiment are what make tests worth doing over again; to compare results and realize why something was done wrong.
Evaluation: Next Steps
To all sorts of problem, there are always different techniques you can take. For this particular laboratory, understanding the factors that affect the rate of enzyme activity, there are different ways that can determine the effect of these factors.
Potential Test #1:
For Part 2 and 3 in this lab, the optimal temp and pH level were identified during the test. However, for Part 1, 4, and 5, the perfect concentrations for the substrate, enzyme or inhibitor concentrations weren't established. Another way to handle this experiment that could ensure new information would be to discover the perfect concentrations for the substrate, enzyme and inhibitor. By finding these concentrations, new information about enzyme activity can be identified and set alongside the data that is already known about factors that have an effect on enzyme activity.
Potential Experiment #2:
The substrate in this lab that was used was hydrogen peroxide, the material that is provided from the decomposition of catalase. Another way of conducting this experiment is to use a different type of enzyme, like maltose. Maltose is another important enzyme since it can be an enzyme that catalyzes the hydrolysis of maltose to glucose (Answers). Every enzyme has different characteristics and by conducting this specific lab with a new enzyme, the characteristics can be driven. Using a different substrate molecule is actually a way to help expand extend the data about enzyme activity.
These two potential experiments for the laboratory predicated on the factors that impact enzyme activity can be used to further understand the concept of enzyme activity. By using these different tests, the information that is collected can be used to further educate and show how diverse enzyme activity can be.
Evaluation: Closing Thoughts
Even although point of the laboratory was to regulate how changes in substrate and enzyme attentiveness as well as environmental changes such as pH and temperature affect enzyme activity, far more information was learned throughout the procedure of the lab. The information for each factor was discovered thoroughly and the foundation of why each part was done was also driven. Since this lab wasn't particularly correct in some ways, other potential tests were considered and can be used to further extend the knowledge of enzyme activity. By learning about enzymes in course, as well as conducting this specific lab, the data about natural catalysts was long and can be linked to situations that happen daily.
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