By finishing this lab about enzyme activity, the cognition about the five chief factors that affect the rate of enzyme activity was easier to grok. Before understanding those constructs, it ‘s important to understand the background information of the molecules involved with this lab. In order to hold a larger perceptual experience of the lab and a better apprehension of why it was done, one must construe the general maps of enzymes and catalase.
There are many substances found in human organic structures that help different beings function decently. One of import substance that is found in human organic structures is called an enzyme. An enzyme is a protein-based protein that acts like a accelerator, which is a substance that speeds up a chemical reaction without being effected, in the reactions within the organic structure ( Wise Geek ) . For illustration, the enzyme found in spit interruptions down the nutrient in order for it to digest in the organic structure. Without this enzyme, it would take hebdomads for the organic structure to digest the nutrient by itself ( Wise Geek ) .
The manner that enzymes work is easy to visually separate. When two molecules react with one another, they must link in some manner. The molecules have to clash in the right orientation and with adequate sufficient energy, intending that the energy between the molecules must be present, for the hit to happen. This type of energy is called the activation energy. A portion in an enzyme that has the specific form and functional groups to fall in to one of the reacting molecules is the active site. When the enzyme attaches to a specific substrate, the reactants of the reaction, this is when the enzyme speeds up the procedure and the binding of the substrate and enzyme is called an enzyme-substrate composite ( Bright Hub ) .
Catalases are enzymes that are normally present in most living beings and are really strong accelerators. Catalase helps the organic structure interrupt down H peroxide, a harmful oxidizing agent found in the organic structure, into O and H2O. This prevents the buildup of C dioxide bubbles in the blood watercourse ( eHow ) . The cellular map of a catalase is like the map of white blood cells in the organic structure ; the white blood cells conflict viruses in human organic structures while catalase battles the consequence of free groups in the organic structure. Free groups are unstable molecules found in the organic structure that make other molecules really unstable and can damage proteins, cell membranes and DNA construction. Therefore, catalase conflicts against the consequence of these molecules by transforming them into H peroxide, and so subsequently interrupting it into O and H2O ( eHow ) .
There are many types of enzymes, including anabolic and katabolic enzymes, and the reactions that are accompanied with them. Anabolic reactions are involved with making big molecules out of smaller molecules and katabolic reactions break down big molecules into smaller molecules ( Nelson Biology 12 ) . The activation energy in any type of reaction lowers due to the accelerators that can be found in the reactions. Enzymes play an of import function in footings of take downing activation energy and are n’t consumed by the reaction ( Nelson Biology 12 ) .
However, there are five chief factors that affect the activity of enzymes, whether it ‘s positive or negative. These five factors are the grounds due to the completion of this peculiar lab and the information that is gathered about these factors give farther cognition of why each factor occurs. The five chief factors are: alteration in enzyme concentration, temperature, pH, substrate concentration and the add-on of an inhibitor.
From the information about enzymes and catalase provided, it will now be easier to understand the footing of this lab. The point of this lab was to calculate out how different environmental conditions would impact the activity of the enzyme. With the provided information in head, the logical thinking behind the consequences of this lab will farther be interpreted and the factors that affect enzyme activity will be easier to understand.
Analysis: Tendencies and Forms
The tendencies and forms that were found during this experimental lab are all intertwined with one another and assist one understand more about enzyme activity. Even though there are five separate factors that affect enzyme activity, they are all connected in some manner and the provided information shows this connexion.
Table 1: Change in enzyme concentration
- Enzyme concentration & A ; composings
- Distance ( centimeter )
- Time ( s )
- Rate of Change ( cm/s )
- Other observations
- 100 % concentration ( 10 milliliter murphy juice )
- 8 centimeter
- 3.02 s
- 2.65 cm/s
- – bubbles appeared
- 80 % concentration ( 8 milliliter murphy juice, 2 milliliter distilled H2O )
- 8 centimeter
- 5.06 s
- 1.58 cm/s
- – fewer bubbles than old composing
- 60 % concentration ( 6 milliliter murphy juice, 4 milliliter distilled H2O )
- 8 centimeter
- 6.28 s
- 1.27 cm/s
- – fewer bubbles than old composing
- 40 % concentration ( 4 milliliter murphy juice, 6 milliliter distilled H2O )
- 8 centimeter
- 7.5 s
- 1.07 cm/s
- – fewer bubbles than old composing
- 20 % concentration ( 2 milliliter murphy juice,
- 8 centimeter
- 19.65 s
- 0.41 cm/s
- – no bubbles appeared
- Figure 1: Change in enzyme concentration
- Factor 1: Change in enzyme concentration
The form that was determined from this portion of the lab was that the larger the sum of enzyme concentration, which is the sum of murphy juice, the more the rate of alteration increased. The lower the enzyme concentration, the rate of alteration decreased.
- Table 2: Change in temperature
- Figure 2: Change in temperature
- Factor 2: Change in temperature
The form that was found in this portion of the lab was that the temperature of 35°C was the optimum temperature throughout this experiment and was the temperature at which the rate of alteration was at its highest point. This means that when the temperature was either higher or lower than 35°C, the rate of alteration would diminish.
Table 3: Change in pH
- Sum of H2O2 ( milliliter )
- Sum of Distilled Water ( milliliter )
- Sum of pH Buffer ( milliliter )
- pH Level
- Vertical Distance Travelled by Filter Paper Towards Meniscus
- Time taken by filter paper phonograph record to travel to meniscus ( s )
- Upward speed of Filter Paper Disc ( cm/s )
- 10 milliliter
- 5 milliliter
- –
- 7 ( Control )
- 8.15
- 6.6
- 1.23
- 10 milliliter
- –
- 5 milliliter
- 2
- 7.98.15
- 16.65
- 0.47
- 10 milliliter
- –
- 5 milliliter
- 4
- 8.15
- 7.05
- 1.16
- 10 milliliter
- –
- 5 milliliter
- 9
- 8.1
- 10.4
- 0.78
- 10 milliliter
- –
- 5 milliliter
- 12
- 7.85
- 8.14
- 0.96
- Figure 3: Change in pH
- Factor 3: Change in pH
The form that was found for this portion of the lab relates with the portion of the lab that was antecedently mentioned, alteration in temperature. The pH degree of 7 was the control ( optimum pH value ) and any pH lower or higher than 7, the rate of alteration would diminish.
Table 4: Change in substrate concentration
- Concentration of H202 of Distilled Water Test
- Time of catalase to go from the underside of the trial tubing to the top ( s )
- Distance of underside of trial tubing to substrate ( centimeter )
- Rate of alteration of the catalyzed reaction ( cm/s )
- 15 milliliter of H202
- 3 %
- 1
- 5.89
- 8.0
- 1.36
- 2
- 6.86
- 8.0
- 1.17
- Entire
- 6.38
- 8.0
- 1.27
- 13 milliliter of H202 2.6 %
- 1
- 8.13
- 8.0
- 0.98
- 2
- 7.11
- 8.0
- 1.13
- Entire
- 7.62
- 8.0
- 1.01
- 10 milliliter of H202 2 %
- 1
- 8.65
- 8.0
- 0.87
- 2
- 12.8
- 8.0
- 0.63
- Entire
- 10.73
- 8.0
- 0.75
- 7.5 milliliter of H202 1.5 %
- 1
- 9.43
- 8.0
- 0.84
- 2
- 12.53
- 8.0
- 0.64
- Entire
- 10.98
- 8.0
- 0.74
- 5 milliliter of H202 1 %
- 1
- 10.37
- 8.0
- 0.77
- 2
- 12.88
- 8.0
- 0.62
- Entire
- 12.63
- 8.0
- 0.70
- Figure 4: Change in substrate concentration
- Factor 4: Change in substrate concentration
The form that was observed in this portion of the lab was really similar to Factor 1: Change in enzyme concentration. The higher the per centum of substrate concentration ( H202 concentration ) , the more increased the rate of alteration was.
Table 5: Addition of an Inhibitor
- Experiment Number
- Sum of Inhibitor ( Cu ( II ) sulfate beads )
- Time ( s )
- Distance ( centimeter )
- Rate of alteration ( cm/s )
- 1
- 0
- 4.13
- 8.0
- 1.94
- 2
- 1
- 4.68
- 8.0
- 1.71
- 3
- 5
- 5.57
- 8.0
- 1.44
- 4
- 10
- 6.66
- 8.0
- 1.20
- 5
- 15
- 8.57
- 8.0
- 0.93
- Figure 5: Addition of an Inhibitor
- Factor 5: Addition of an Inhibitor
The form that was found in this portion of the lab involved inhibitors, chemicals that block active sites on enzymes. The larger the sum of inhibitor ( Cu II sulphate ) that was added to the enzyme concentration, the slower the rate of alteration was.
Evaluation: Decision
Before carry oning the lab, certain hypotheses were made for each factor that affects enzyme activity. Based on the cognition that was already given about enzymes, the hypotheses that were made were the best to stand for what was predicted to happen in each portion of the lab.
For Part 1: Change in enzyme concentration, if the enzyme concentration was decreased in an H202 decomposition reaction, so the rate of alteration will besides diminish. This hypothesis was made based on this portion of the lab because if the composing was n’t pure enzyme solution, it would impact the rate of alteration. This hypothesis was proved harmonizing to Table 1: Change in enzyme concentration ; the 20 % concentration of murphy juice ( 2 milliliter murphy juice and 8 milliliter distilled H2O ) had the lowest rate of alteration value. This composing was the 1 that had the least sum of enzyme solution ; this composing merely had 2 milliliter of enzyme concentration. This connects with the hypothesis because the lower the enzyme concentration, the lower the rate of alteration. Besides, at a low enzyme concentration, there is a great sum of active sites and the rate of the reaction is low. As the enzyme concentration additions, there are more active sites and therefore, the reaction will predate faster ( S-Cool ) . Therefore, the overall tendency that was portrayed in this portion of the lab was that as the concentration of the enzyme increased, the rate of alteration besides increased.
For Part 2: Change in temperature, if the temperature was higher or lower than 37 °C, which is the optimum temperature in life beings ( Nelson Biology 12 ) , so the rate of alteration would diminish. This hypothesis was right except for one feature: the optimum temperature in this portion of the lab was 35°C alternatively of the normal optimum temperature in beings which is 37°C. The remainder of the hypothesis was accurate since when the temperature that was either higher or lower than 35°C, the rate of alteration decreased. When the temperature was higher than the optimum temperature, this was due to the denaturing of the solution. When the temperature was lower than the optimum temperature, this was caused due to the short sum of kinetic energy required for the reaction to happen faster ( RSC ) .
Mentioning to Figure 2: Change in temperature, when the temperature was either higher or lower than the optimum temperature, the rate of alteration would diminish. In other words, as the temperature rises, the molecules that were responding would hold more kinetic energy. Since the molecules have more energy, this would increase opportunities of hits between the molecules and hence would increase the rate ( RSC ) . This information correlates with the hypothesis because when the optimum temperature was non reached, the rate of alteration was decreased. The overall tendency that was determined for this portion of the experiment was that if the temperature was higher or lower than the optimum temperature ( 35°C ) , the rate of alteration would diminish.
Sing Part 3: Change in pH, if the pH ( optimum pH is 7 ) was higher or lower than the optimum pH, the rate of alteration would diminish. This hypothesis was proved to be right because when the pH was either 2, 4, 9 or 12, the rate of alteration would be lower than the rate of alteration at the pH of 7. This hypothesis is connected to the hypothesis in Part 2: Change in temperature because they both have the same features when it comes to impacting enzyme activity. Mentioning to Table 3: Change in pH, when the pH value was either higher or lower than 7, the rate of alteration would diminish. Similarly with the alteration in temperature, alterations in the pH value would do but besides interrupt intermolecular and intramolecular bonds. By altering the bonds, this would besides alter the form of the enzyme and alter the enzymes efficiency ( RSC ) . Therefore, when the optimum pH is non being used, the rate of alteration will be decreased due to denaturing of the enzyme ( Nelson Biology 12 ) . The general tendency that was found in this portion of the lab relates to Factor 2: Change in temperature, as they both portion the same features in the footings of the given informations. The higher or lower the pH value was from the optimum pH value, the rate of alteration would be decreased.
For Part 4: Change in substrate concentration, if the substrate concentration was increased in a decomposition reaction with catalase, the rate of alteration would besides increase. This hypothesis was accurate because when the highest concentration was used, 3 % , the rate of alteration was besides the highest, 1.27 cm/s. Since there was more substrate solution, H202, the rate of alteration was besides the highest out of all the other concentrations. Mentioning to Figure 4: Change in substrate concentration, this figure is similar to Calculate 1: Change in enzyme concentration because as the concentration increased, so did the rate of alteration. The overall tendency that was found in this portion of the lab was similar to Factor 1: Change in enzyme concentration from the provided information. Associating to the active sites in footings of the rate of the reaction, when the substrate concentration is low, this means that there are less active sites being occupied and this besides means that the rate of alteration is besides low. When more substrate molecules are added, extra enzyme-substrate composites are formed. Therefore, as there is a bigger sum of active sites, the rate of alteration additions ( S-Cool ) . In other words, as the concentration of the substrate solution is increased, the rate of alteration besides increased.
For Part 5: Addition of an Inhibitor, if the sum of the inhibitor was increased, the rate of alteration would diminish. This hypothesis was besides right because based on the cognition already known about inhibitors, it was clear that the more inhibitor that is put into a solution, the slower the solution would respond. The inhibitor in this instance was the Cu II sulphate and this hypothesis was accurate because the more beads of Cu II sulphate that was added to the enzyme solution, the more the rate of alteration decreased. Since an inhibitor is meant to barricade active sites of enzymes, this characteristic would impact the rate of alteration and do it diminish. There are two types of inhibitors: competitory and noncompetitive inhibitors. Competitive inhibitors penetrate into the enzyme ‘s active site and barricade the substrate signifier binding. Noncompetitive inhibitors join to another site on the enzymes which creates a alteration in the enzyme ‘s form. The alteration in form causes lose of resemblance for the substrate ( Nelson Biology 12 ) . In other words, as more inhibitor is added, the handiness of active sites decreased since the inhibitors block normal substrates from adhering and changes the form of the enzyme.
The hypotheses that were made for each portion of the lab came to be right based on the information provided about factors impacting enzyme activity. Each hypothesis was proved by the informations that is provided in the Analysis: Tables & A ; Figures and that besides give a ocular representation of each hypothesis.
Evaluation: Beginnings of Mistake
Not every experiment is absent of mistakes but by detecting these mistakes, experiments can be done more accurately in the hereafter. There were many mistakes that were found throughout the lab ; nevertheless these specific beginnings of mistakes are the 1s that were beginnings of mistakes instead than human mistakes.
Incompatibility of forcing the filter paper down in a trial tube- after dunking the filter paper into the enzyme solution, the filter paper had to be pushed down to the underside of the trial tubing with the substrate solution. One of import facet of the lab was to clip how long the filter paper took to lift back to the top of the semilunar cartilage of the solution. However, forcing the filter paper to the underside of the trial tubing was inconsistent each clip it was done. To better this mistake in the hereafter, other stuffs could hold been used to help the filter paper to travel right to the underside of the trial tubing instead than drifting back to the top, such as stuffs like a scoopula or any other stuff that is long in length.
Test tubing measurings – for each portion of the lab, the measuring of the enzyme and substrate solutions were made and poured into a trial tubing. Even though the volume of the solution was easy to find by utilizing a calibrated cylinder, the length ( distance ) of the solution was inaccurately measured. The usage of a swayer made the measurings of the solution imprecise and was an happening beginning of mistake for each portion of the lab.
Sum of inhibitor in the solution – For Part 5: Addition of an Inhibitor, the Cu ( II ) sulphate was dropped into the trial tubing as the inhibitor and this portion of the experiment was inconsistent due to the sum of inhibitor that was released into a solution each clip. A dropper is n’t a dependable piece of stuff in this lab due to the fact that it may take more inhibitor at one clip and a less amount the following clip.
These three chief mistakes that were made during this portion of the lab could hold been avoided if more attending and item was put into the experiment. However, mistakes that occur during an experiment are what make experiments deserving making over once more ; to compare consequences and understand why something was done incorrect.
Evaluation: Following Stairss
To every type of job, there are ever different attacks one can take. For this peculiar lab, understanding the factors that affect the rate of enzyme activity, there are other ways that can find the consequence of these factors.
Potential Experiment # 1:
For Part 2 and 3 in this lab, the optimum temperature and pH degree were determined during the experiment. However, for Part 1, 4, and 5, the optimum concentrations for the substrate, enzyme or inhibitor concentrations were n’t determined. Another manner to transport out this experiment that would guarantee new information would be to happen out the optimum concentrations for the substrate, enzyme and inhibitor. By happening these concentrations, new information about enzyme activity can be determined and compared to the information that is already known about factors that affect enzyme activity.
Potential Experiment # 2:
The substrate in this lab that was used was hydrogen peroxide, the substance that is provided from the decomposition of catalase. Another manner of carry oning this experiment could be to utilize another type of enzyme, like malt sugar. Maltose is another of import enzyme because it is an enzyme that catalyzes the hydrolysis of malt sugar to glucose ( Answers ) . Every enzyme has different features and by carry oning this specific lab with a different enzyme, the features can be determined. Using a different substrate molecule could be a manner to farther widen the cognition about enzyme activity.
These two possible experiments for the lab based on the factors that affect enzyme activity can be used to further understand the construct of enzyme activity. By utilizing these different experiments, the information that is gathered can be used to farther educate and demo how diverse enzyme activity can be.
Evaluation: Shutting Ideas
Even though the point of this lab was to find how alterations in substrate and enzyme concentration every bit good as environmental alterations such as pH and temperature affect enzyme activity, a batch more information was learned throughout the procedure of the lab. The information for each factor was learned exhaustively and the footing of why each portion was done was besides determined. Since this lab was n’t peculiarly precise in some ways, other possible experiments were thought out and can be used to further widen the cognition of enzyme activity. By larning about enzymes in category, every bit good as carry oning this specific lab, the cognition about biological accelerators was extended and can be connected to state of affairss that occur daily.
