Enzyme Lab

During these experimental procedures, the implication of multiple different temperatures on fungal and bacterial amylase was studied. In order to conduct this experiment, there were four different temperatures used. The four temperatures used were the following: 0 degrees Celsius, 25 degrees Celsius, 55 degrees Celsius, and 80 degrees Celsius - Each temperature for one fungal and one bacterial amylase. Drops of iodine were then placed in order to measure the effectiveness of the enzyme. This method is produced as the starch test. The enzyme was tested over the course of ten minutes to determine if starch hydrolysis stemmed. An effective enzyme would indicate a color variation between blue/black to a more yellowish color towards the end of the time intervals, whereas a not so effective enzyme would produce little to no change in color variation. According to the experiment, both the fungal amylase and bacterial amylase exhibited a optimal temperature. This was discovered by observing during which temperature and time period produced a yellow-like color the quickest. Amylase shared a similar optimal temperature of 55 degrees Celsius. Most of the amylases underwent changes at different points, but some enzymes displayed no effectiveness at all. Both amylases displayed this inactivity at 0 degrees Celsius. At 80 Celsius both the enzymes became denatured due to the high temperatures. In culmination, both fungal and bacterial amylase presented a array of change during it’s

The purpose of this experiment was to come up with the optimal temperature of the Fungal Amylase, Aspergillus oryzae, and the Bacterial Amylase, Bacillus liceniformis, as well as to identify if different temperatures would indeed affect the enzyme amylase by either slowing down the process or denaturing the enzyme. Enzymes are complex proteins, they can be thought of as a substance fabricated by a living organism that behaves as a stimulus, otherwise known as a catalyst, to cause a specific biochemical reaction. This experiment was performed by keeping the amylase mixed with starch at different temperatures, either in the heated water or in the ice bath. The temperatures varied at either 0, 25, 55, or 85 degrees Celsius. After a certain amount of time we would then move the test tubes containing the amylases and position them on a plate where iodine was then added to the starch amylase solution. We would do the same thing at different time intervals to see exactly how the enzyme catalyzed the starch. The hypothesis of this experiment was thought to be that the higher the temperature the slower the enzyme would then hydrolyze the starch. Both the Fungal and the Bacterial Amylase had an optimal temperature of 55 degrees Celsius as shown by our concluded results in this

The purpose of this experiment is to determine how the change of pH, enzyme concentration, and temperature affect the rate of enzyme reactions. In this experiment, three tests were performed. The first related the effects of different concentrations of the enzyme sucrase on a constant amount of a substrate. The second experiment was used to investigate the changes in enzyme productivity based on the temperature at which the reaction was allowed to occur. The third experiment tests the effect of how the pH of a substance affects the rate at which the enzyme catalyses sucrose.

We increased the substrate, catechol, while maintaining the enzyme, catecholase, at the same volume. We came to the hypothesis that if the substrate was increased, then the rate of reaction would increase as long as there is enzymes to react with. The third experiment involved how temperature would affect enzyme activity. This was done by placing certain vials in certain temperatures and then analyzing the data in the spectrophotometer. We came to the hypothesis that if the temperature was increased, then the reaction rate would increase until it reaches the optimal temperature after that the reaction rate would decrease. This is because the enzyme will start to denature if the temperatures get too high or too low. The fourth experiment deals with how pH affects enzyme activity. For this experiment different vials with catecholase and different pH’s were observed under a spectrophotometer to see how the enzyme would be affected. We found our hypothesis to be, if pH is raised, then the reaction rate will increase until it reaches the optimal pH. The reaction rate will increase until the optimal pH because after the optimal pH, the enzyme will start to denature and not function as it

In Experiment One, the data signifies that the velocity of the enzyme increased as the concentration of the substrate increased. However, the data from the second experiment draws inconclusive. The qualitative observations of the color change were a clear sign to start the experiment over again due to possible contamination, and that was not done. This could possibly be a reason why the data shown in the effects of temperature is so skewed. While temperature should rapidly increase the rate of enzyme activity until a certain point at which the enzyme denatures, the data shows denaturation of all enzymes besides Tubes 3 and 4, the color changing solutions in both parts of Experiment Two.

The experiment testing the effect of temperature on enzyme activity also utilized spectrophotometry. Since the IKI was blue, testing the amount of blue light absorbed required the spectrophotometer stay at 580 nanometers, the wavelength of blue light. Four test tubes were set up using different amounts of starch, amylase, buffer, and at different temperatures, all described in Table 1. Test tube 1, the negative control, contained 0 mL of starch, 1 mL of amylase, and 2 mL of buffer, all at room temperature. Test tube 2, the experimental control, contained 1 mL of starch, 1 mL

Bacterial amylases operate at higher temperatures than do fungal amylases. Fungal amylases react rapidly at lower temperatures; fungal amylases are used as an agent for alcohol fermentation for grain (Underkofler et al, 1958). Fungal amylases is said to be denatured – change shape (Alberte et al, 2012), at high temperatures above 60° C and bacterial amylases on the other hand are stable and show little denaturing at temperatures up to 85°C 3 The question answered by the experiment is if the temperature is not within the range of the enzymes (fungal and bacterial amylase) optimal temperature (higher temperature) then will the enzymes denature and if the enzymes are placed in lower temperature from optimal the activity then will it slow down enough to stop all reaction, meaning each enzyme will not be operating efficiently. Knowing about a bacterial amylases and fungal amylases optimal temperatures are important for knowing which food products and industrial products it can be used on to conserve the product because then the producer knows about which products it can be incorporated into depending on the temperature it is manufactured at.

An increase in enzyme concentration will increase enzyme substrate speed up the rate of reaction until the saturation point is reached. (Enzymes and...) Meaning that all the enzyme active sites are occupied by substrate and can no longer enhance in activity. For the next experiment we tested on was temperature. I hypothesis, that the enzyme energy will increase as the temperature rises and have little energy as it lowers. When the temperature rises the activity of the enzyme and substrate collisions increases as well. But, it will hit its maximum point where its bonds will begin to break down. We first measured the absorbance rate at 0 Celsius giving a us .001405 (1/s) and giving the product a light shade of brown. The reaction rate became more active as the temperature rose and the color would darken. But, when reaching over 40 Celsius that’s when the enzyme began to denature. Also, when reaching 100 Celsius the enzyme reaction rate was less than .0005 (1/s) and the solution stayed transparent. Next, we tested the pH, it’s a scale that measures 0 to 14, 0 being the most acidic and 14 being the most

The purpose of this laboratory experiment was twofold. First, it was a hands-on review of the scientific process itself, and how this actually plays out in a real laboratory setting. The second aspect of this exercise was to test knowledge gained on the role and structure of enzymes and to examine how temperature played a role in its functional capabilities.

My hypothesis stated “if you increase the temperature, amylase activity will also increase until the temperature is about 38°C, where amylase activity will then decrease”. Recall the line of the graph in Figure 1. At 0°C, there was no amylase activity because the enzyme could not function at too cool of an environment. However, when the temperature increased to 23°C, there was some amylase activity occurring. When the temperature increased to 38.5°C, the amylase was able to function properly because it was the perfect temperature so there was a large amount of amylase activity. At 84°C, the temperature is too warm for the amylase so it becomes inhibited and can no longer function properly. On the graph, the peak shows the optimum temperature, 38.5°C, and the negative slope indicates

The purpose of this experiment was to determine how temperature affects the rate of enzyme activity on its substrate. Using methods like, add 2 mL of hydrogen peroxide to each test tube and observe the rate of reaction. The result of this experiment was when temperatures are higher they tend to speed up the effect of enzyme activity, while lower temperatures decrease the rate of an enzyme reaction. However, if the temperature is too high, an enzyme will denature, which causes the shape of the enzyme to change. If the enzyme's shape changes, it cannot bind to the substrate. It is important to be very precise while adding enough distilled water to cover the potato, or hydrogen peroxide. Because, it is a possibility that it will lead to an error.

This experiment was performed to demonstrate how varying temperatures affects the activity of the enzyme, amylase. Also, it was conducted to determine the optimal temperature for the fungal, Aspergillus oryzae, and bacterial amylases by placing them both into different test tubes with differing temperature conditions. At varying time intervals, both enzymes were removed from their assigned temperatures. A drop of each enzyme will then be placed on two different spot plates with a pipette. All the wells on the spot plates contain three drops of iodine to clearly show whether a reaction has taken place. The pipette was used to mix the iodine with the starch enzyme to organize the levels of starch catabolism based on temperature. At the end of

The entirety of this experiment was to conclude if temperature had an effect on enzyme activity. The experiment tested the perimeters of enzyme activity and to see whether or not the temperature had an effect on the amount of substrate produced. Enzymes are especially well known for being catalyst within a reaction (Royal Society of Chemistry). A catalyst is, in this case an enzyme, which speeds up a reaction by lowering the activation energy required to start the reaction (Royal Society of Chemistry). Previous research has shown that while the temperature rises reacting molecules have more kinetic energy. The more kinetic energy each molecule has, the greater the chance of reaching its point of highest catalytic activity (Royal Society of

This experiment was needed to determine the optimal temperature at which the enzyme amylase best functions. Since an increase in temperature speeds up the movement in molecules, the substrate is supposed to come in contact with the active site of the enzyme more quickly and frequently until the heat becomes an obstacle by denaturing the structure of these enzymes and thus changing its function. There were a total of four different temperatures at which amylase activity was observed (Table 1). In order to ensure that temperature was the only manipulated variable, four test tubes were prepared with the same contents. Each tube contained about 2mL of the 1% starch solution, 4mL of deionized water, 1mL of a 6.8 pH buffer.

The following is an EEI designed to test the effects of temperature on the activity of the enzyme Amylase. This experiment on enzymes was done to help convey how environmental factors affect the activity of an enzyme. The experiment will revolve around changing one variable (temperature), measuring one variable (color of the samples in the spot plate/reaction rate/time) and keeping everything else the same (optimum pH/volume of reactants and the reagent). To test the effects of temperature on the activity of amylase, solutions of the enzyme and starch will be reacted with each other at controlled temperatures 70oC, 50oC, 37oC, room temperature and 4oC and below. To find out what effect these temperatures have on the activity of the enzyme, a sample of the resulting solution will be taken at allocated times and be placed onto a spot plate where a test for starch will be done by adding iodine reagent. The relative enzyme activity in the spot plate will be assessed as follows: