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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…
According to the data collected on the amylase activity at various pH levels (graph 2), the pH concentration effects the amylose percentage; it effects it by causing it to decrease. The higher the pH concentration, the faster the amylase decreases over time. However, a low pH concentration causes the amylose percentage to stay the same or increase. When looking at the graph, it can be seen that the amylose percentage with a pH concentration of 4 increased drastically then remained constant and increased by a small percentage. The cause of the decrease and increase of amylose percentage is a result of the different enzyme activity in each pH concentration. The amylose percentage with a pH of 4 increased because there was enzyme activity. However, as the pH concentration increases, there is more enzyme activity that is occurring. This explains why the amylose percentage decrease in pHs of 5, 6 and 7. Additionally, according to the graph the optimum pH concentration for amylase is 7. According to the data collected on the amylase activity at various temperature (graph 3), the percentage of amylose in all temperature either decreased or increased.
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
to.
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
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
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
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.
The graph of rate of reaction against temperature did show that the 2 factors were proportional, but only up to a point. After 60 degrees Celsius the next temperature measurement showed that the reaction did not occur. I believe that this is because at some point between 60 to 80 degrees Celsius the Trypsin enzyme became denatured, (this is where the heat distorts the enzyme in such a way that stops it from functioning). While it is said that rate of reaction and temperature are directly proportional this is not completely true. The graph plotted shows a slightly curved line from the reading at 20 degrees Celsius to the reading at 60 degrees Celsius, (the region of the graph that I believe shows direct proportion).
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.
Many advertisements sometimes mislead its consumers when selling out protein powder products. One particular manufacturer is claiming that when testing 1 gram of Tough Guy protein powder in 100 ml of H2O, the final concentration would measure between 0.40 mg/ml protein. To determine if the manufacturer is claiming to be true or not an experiment was conducted. By determining the amount of protein that is presented when Tough Guy protein powder is diluted in water by adding Bio-Rad assay (measuring the concentration of protein within a known and unknown samples). Measurement of color change will be needed by placing the solution into a spectrophotometer at 595 nm. Thus, determining its results.
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: = == ==
Purpose: This lab gives the idea about the enzyme. We will do two different experiments. Enzyme is a protein that made of strings of amino acids and it is helping to produce chemical reactions in the quickest way. In the first experiment, we are testing water, sucrose solution, salt solution, and hydrogen peroxide to see which can increase the bubbles. So we can understand that enzyme producing chemical reactions in the speed. In the second experiment, we are using temperature of room, boiling water, refrigerator, and freezer to see what will effect the enzyme.
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
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.
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.
...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.
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
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