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Investigating the effects of concentration on amylase activity
Investigating the effect of amylase concentration
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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. …show more content…
However, the decrease varied depending on the temperature. The lowest temperature, 4 degrees Celsius, experienced a very low decrease of amylose percentage. Temperature at 22 degrees Celsius and 37 degrees Celsius, both had a drastic decrease in amylose percentage. While the highest temperature, 70 degrees Celsius, experienced an increase of amylose percentage. In conclusion, as the temperature increases the percentage of amylose decreases; however, if the temperature gets too high the percentage of amylose will begin to increase. The percentage of amylose increases at high temperatures because there is less enzyme activity at high temperatures. However, when the temperature is lower, more enzyme activity will be present, which results in the decrease of amylose percentage. This is why there is a decrease of amylose percentage in 4, 22, and 37 degrees Celsius. In this experiment the optimal temperature is 37 degrees Celsius, this is because this is the average human body temperature. Therefore, amylase works better at temperatures it is familiar
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
The affects of pH, temperature, and salt concentration on the enzyme lactase were all expected to have an effect on enzymatic activity, compared to an untreated 25oC control. The reactions incubated at 37oC were hypothesized to increase the enzymatic activity, because it is normal human body temperature. This hypothesis was supported by the results. The reaction incubated to 60oC was expected to decrease the enzymatic activity, because it is much higher than normal body temperature, however this hypothesis was not supported. When incubated to 0oC, the reaction rate was hypothesized to decrease, and according to the results the hypothesis was supported. Both in low and high pH, the reaction rate was hypothesized to decrease, which was also supported by the results. Lastly, the reaction rate was hypothesized to decrease in a higher salt concentration, which was also supported by the results.
Enzymes are proteins that increase the speed of reactions in cells. They are catalysts in these reactions which means that they increase the speed of the reaction without being consumed or changed during the reactions. Cofactors are required by some enzymes to be able to carry out their reactions by obtaining the correct shape to bind to the other molecules of the reaction. Chelating agents are compounds that can disrupt enzyme reactions by binding to metallic ions and change the shape of an enzyme. Catechol is an organic molecule present under the surface of plants. When plants are injured, catechol is exposed to oxygen and benzoquinone is released because of the oxidation of catechol. Catecholase aids in the reaction to produce
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
...e substances at 37.5̊C due to the fact that in the previous experiment, this was found to be the optimum temperature that catalase reacts at. It was because of this constant that I used the set of data of the catalase at 37.5̊C from the first experiment to provide a neutral environment for the experiment. The way in which the data was collected for the first experiment was identical to that needed to be done by the second. From this data, it was determined that the neutral environment for the catalase had the best results, which makes it clear that when the enzyme is in a pH of the opposite extremes such as basic or acidic, it is un able to function properly. When it is too basic then the enzyme will become inactive and when the enzyme is too acidic then the enzyme will denature, both rendering it unable to function at its optimum efficiency that all enzymes need.
The temperature of amylase The temperature of starch Room temperature Concentration Ph values The variable I will be changing is the volume of amylase. Safety: The sand is To make sure I carry out this experiment safely I will make sure I wear a pair of goggles. I will ensure I keep my stool under the table and all
Investigating the Effect of Enzyme Concentration on the Hydrolysis of Starch with Amylase Aim: Investigate the effect of enzyme concentration on the rate of an enzyme-controlled reaction. Using amylase and starch as my example. Introduction: I am investigating the effect of the concentration of the enzyme, amylase on the time taken for the enzyme to fully breakdown the substrate, starch to a sugar solution. The varied variable will be the concentration and all other variables are going to be fixed. The different concentrations will be: 0.5% 0.75% 1.0% 1.5% 2% An enzyme is a class of protein, which acts as a biological catalyst to speed up the rate of reaction with its substrates.
Generally, chemical reactions speed up as temperature’s raised. This happens because as the temperature gets higher, more of the reacting molecules have enough kinetic energy to undergo the reactions. It is the same with enzyme reactions; however, if the temperature of an enzyme-catalyzed reaction is raised further then its optimum; the enzyme becomes denatured. Catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide to water and oxygen. The optimum temperature for catalase is 37 degrees. The purpose of the lab is to measure and explain the affects of enzyme and substrate concentration on reaction rates of an enzyme catalyzed reaction (in a controlled experiment). Basically to learn about how temperature impacts enzyme activity (catalase). My hypothesis is as the temperature increases the enzyme activity of catalase will increase up to a certain point where the enzyme will start to denature and the activity will
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 mixture for that table’s flask was 15 mL Sucrose, 10 mL of RO water and 10 mL of Yeast, which the flask was then placed in an incubator at 37 degrees Celsius. In my hypothesis for comparison #4 the measurements would go up again with every 15 min. intervals because of the high tempeture and also be higher that then Controlled Table’s measurements. Hypothesis was right for the first part but was wrong for the second part of the comparison, the measurements did increase in the table’s personal flask but the measurements did not get higher than the Controlled Table’s measurements, see chart below. In conclusion, I feel that the substitution of glucose for sucrose made the enzymes work just as hard as the Controlled Table’s flask but just not as much because sucrose was too strong for the enzymes to
The reason for this is that as you increase the temperature of the enzyme and the substrate molecules you also increase the energy in the form of kinetic energy which they possess. Because the enzymes and substrate molecules are moving faster the chance of them colliding in a certain time and area is increased. Thus the chance of the hydrogen peroxide molecules binding with the Catalase molecules active site and reacting is higher. However after a certain point increasing the temperature will begin to hinder the activity of the potato catalase.
Enzyme concentration is directly proportional to the rate of reaction provided the substrate concentration is maintained at a high level and the pH and temperature are kept constant. We know that the substrate concentration is maintained at the same level in all samples, this done by ensuring that all samples are of equal mass and we know that all the samples were placed in an incubator at 40°C thus ensuring that the temperature effects the rate of reaction in all samples in the same way. Graph: - From 0% ¬> 0.25% concentration we can see the greatest rate of reaction as there is an abundance of substrate molecules available to combine with the active site of the enzymes producing a large gradient on the graph. As concentration increases from 0.25% ¬> 0.
At 0°C, enzymatic reaction of salivary amylase occurs slowly or not at all due to lack of energy and heat. As the temperature increases, its enzymatic also increases up until the optimum temperature. Figure 1 shows that the optimum temperature of salivary amylase is about 37°C.This applies to the human body since salivary amylase is suitable to function within these temperatures. After 37°C, the graph then steeply declines as a result of loss of activity. At 70°C and 100°C, salivary amylase is denatured. The molecular conformation of the enzyme becomes altered as the hydrogen bonds responsible for its secondary, tertiary and quaternary structures are
The temperature of the water shows if the temperature in which catalase reacts in has an effect on the amount of oxygen produced. Every enzyme has an optimum amount of pH, which allows it to have a higher reaction velocity (WBC).The higher the reaction velocity the more reactive the enzyme is. Measuring the different amount of pH solutions and their effect on the amount of oxygen produced can show the optimum pH for catalase and the effect pH has on catalase. The data that these three independent variables will yield will allow us to better understand the effects concentration, temperature and pH have on the enzyme catalase. If catalase reacts at full concentration, 37 degrees celsius and a pH of eight the enzyme catalase will produce more oxygen than if it is at room temperature, a lower concentration and a more acidic base because the higher temperature will allow molecules to move faster and have a higher chance to collide and react, a higher concentration will create a higher enzyme to substrate ratio which allows it to react more and finally a more basic pH will allow it catalase to have a higher reaction