The Optimal Temperature Of Bacillus Lichenformis Bacterial Amylase And Aspergillus Oryzae Fungal Essay

Enzymes are biological catalysts that speed up chemical reactions, without being used up or changed. Catalase is a globular protein molecule that is found in all living cells. A globular protein is a protein with its molecules curled up into a 'ball' shape. All enzymes have an active site. This is where another molecule(s) can bind with the enzyme. This molecule is known as the substrate. When the substrate binds with the enzyme, a product is produced. Enzymes are specific to their substrate, because the shape of their active site will only fit the shape of their substrate. It is said that the substrate is complimentary to their substrate.

Enzymes are biological catalysts, which speed up the rate of reaction without being used up during the reaction, which take place in living organisms. They do this by lowering the activation energy. The activation energy is the energy needed to start the reaction.

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

Effects of Temperature Variation on the rate of Enzymatic Activity of Peroxidase Abstract In order to examine the effects of temperature on the enzyme peroxidase we measure amount of accumulated electron donor guaiacol, which turns brown when oxidized during the reaction of hydrogen peroxide and peroxidase, via a spectrophotometer at various temperatures. We measured two sets of temperature variations: one in which the reactions happened at various temperatures, and on in which the reactants were allowed to return to room temperature after this increase/decrease in temperature before reacting. We found that extremely cold and hot temperatures showed the least amount of absorption change, as well as the least amount of absorption change even once recovered back to room temperature due to the denaturing of peroxidase in these extreme temperatures.

Lichenformis and A. Oryzae experience high rates of reaction at 55 degrees Celsius. The numbers in the number column represents the color that the amylase changes to when poured into the wells. This column goes from 5 to 1, 5 meaning the amylase became black due to denaturation or the rate of reaction was too low, 4 meaning it became brown, 3 meaning it became a brownish orange color, 2 meaning it became orange, and 1 meaning it became completely yellow because the enzyme is at its exact optimal temperature. The B. Lichenformis in the 55 degree column was orange at the 6, 8, and 10 minutes rows while the A. Oryzae in the 55 degree column was orange at the 6 minute row but was an orange-yellow in the 8 and 10 minutes rows. At the 0 degrees column, the B. Lichenformis mixed with iodine created a black mixture at the 0 minute row, the starch-amylase mixture poured into the iodine filled wells in the 2, 4, and 6 minutes row made a brown mixture, and the 8 and 10 minutes row made an orange-brown color. At the 0 degree column for the A. Oryzae, the amylase mixed with the iodine turned black at the 0 minute row and brown at the 2,4,6,8, and 10 minutes row. At the 40 degrees column, the B. Lichenformis turned black at the 0 minutes row but was a brownish orange at the 2, 4, 6, and 8 minutes row but then became black at the 10 minutes row while the A. Oryzae was black at the 0 minutes row, a brownish-orange at the 2, 4, 6, and 8 minutes row and

Enzymes are biological catalyst that are made up of proteins. Each type of enzyme can only function in its specific reaction, and enzymes work best in their optimal pH and temperature range. There are two types of reactions that were discussed in which enzymes are involved. The first type of reaction is a catabolic reaction. A catabolic reaction uses enzymes to break the covalent bond in a polymer resulting in smaller monomers as the product. The second type of reaction is an anabolic reaction. In an anabolic reaction, the monomer or substrate binds to the active site of an enzyme where a covalent bond is formed, thus producing a

The effects of temperature on fungal amylase Aspergillus oryzae, and bacterial amylase, Bacillus licheniformis ability to break down starch into maltose was studied. The study determined the optimal temperature the Aspergillus oryzae and Bacillus licheniformis was able to break down the fastest. The starch catalysis was monitored by an Iodine test, a substance that turns blue-black in the presence of starch. Amylase catabolizes starch polymers into smaller subunits. Most organisms use the saccharide as a food source and to store energy (Lab Manual, 51). The test tubes were labeled with a different temperature (0°C, 25°C, 55°C, 85°C). Each test tube was placed in its respective water baths for five minutes. After the equilibration process, starch was placed in the first row of the first row of the spot plate. Iodine was then added to the row revealing a blue black color. The starch was then added to the amylase. After every two minute section a pipette was used to transfer the starch-amylase solution to place three drops of the solution into the spot plate row under the corresponding temperature. Iodine drops was placed in the row. Color changes were noted and recorded. The results showed Aspergillus oryzae was found to have an optimal temperature between 25°C and 55°C and Bacillus licheniformis was found to have an

The enzyme, Amylase is significant to the commercial world and it is important to know the optimal conditions for amylase activity to be able to use amylase efficiently. To determine the optimal temperature for both fungal and bacterial amylase, an Iodine test was used to visually measure starch catalysis. A mixture of starch and amylase, either bacterial or fungal, were placed in four different temperatures, 0⁰C, 25⁰C, 55⁰C, and 85⁰C, and then added to iodine to observe amylase activity. A light yellow color means a weak presence of starch which indicates a high activity rate for amylase while a dark blue-black color means a strong presence of starch which indicates a low activity rate for amylase. Observed was an optimal temperature of 55⁰C for bacterial amylase which showed the lightest yellow color and an optimal temperature around 25⁰C for fungal amylase which showed the lightest yellow color.

An enzyme is a catalyst that accelerates chemical reactions within a cell (Campbell, 2010). Enzymes decrease a reaction’s activation energy making it easier for a reaction to occur. Enzymes possess an active site where an enzyme binds with a substrate and catalyzes the substrate. Under mild conditions, many reactions would take years to occur without enzyme catalysis. Enzymes increase the rate of cellular reactions and decrease their reaction time (Cooper, 2000). Cells contain numerous enzymes that each catalyzes a specific reaction.

In living organisms, chemical reactions are catalyzed with the help of molecules called enzymes. These molecules, which are proteins, all have a specific shape. This shape directly relates to the function of the enzyme. Enzyme’s fulfill their catalytic function by lowering a chemical reaction’s activation energy. They do this by binding to a substrate, the molecule(s) the enzyme will react with, at the enzyme’s active site.

Enzymes are large protein molecules that act as biological catalysts, accelerating chemical reactions without being consumed to any appreciable extent themselves.

Step are as follows; first, label two separate sets of spot plates. One for bacterial amylase and another for fungal amylase on each plate write the differentiating temperatures beginning from lowest to highest (0C, 25C, 65C, and 85C), temperature are as implemented by lab director. On the side of each plate label the time periods, ranging from 0 to 10 minutes in two-minute intervals. Next, four test tubes should be filled with bacterial amylase and labeled with a B, and another four with fungal amylase and labeled with an F. After five minutes, use plastic pipettes to gather some enough starch from SB (starch bacteria) from each temperature and place three drops into the 0-minute row wells. Then add 3 drops of iodine to the equilibration.Following, remove and place each grouped and labeled test tubes correctly labeled B and SB from each temperature and place them in their respective environments for five minutes to equilibrate.

Specific enzymes made up of proteins are used in biology to speed up a chemical reaction of any kind. Since a spontaneous chemical reaction can occur without help from any outside energy it could potentially prolong the reaction to where it becomes almost unnoticeable since it can take years for it to happen. For this reason, enzymes take action as a catalyst that speed up the reaction rate without completely being absorbed (Campbell et al., 2010). Enzymes are a form of regulation that allow for a through pathway in chemical reactions. It is able to perform as a catalyst by lowering the activation energy which is the energy required to drive the reactant to the top of the energy barrier allowing the downhill part to begin. An

In this experiment we wanted to determine the optimal temperatures for fungal, Aspergillus oryzae, and bacterial, Bacillus licheniformis. In order to see if any of the starch was broken down, Iodine was mixed with the starch-amylase substance. In four spot plates, the groups labeled the different temperatures, once the iodine came in contact with the starch, the result would be a reaction that turns the fluid into this dark blue/black color. In a span of 10 minutes, with occasional check ups on the solution every 2 minutes, the amylase-starch solution was placed into five types of temperature, all being Celsius. The five temperatures were 0 degrees, 25 degrees, 55 degrees, and 85 degrees Celsius. The solution would change colors, so in order to measure the changes, a scale was used. Such scale was a 1-5 scale, with colors next to each number. One being the lightest color, or yellow, and 5 being the darkest color, or black. Based on the change of color, we could tell how fast it hydrolyzed the starch in a span of 10 minutes. To keep record of the results, the results were put in Data Tables used from the Lab Manual. The average optimal temperature for Bacteria Amylase was 85 degrees Celsius, while the Fungal was 55 degrees Celsius. You can see this by looking for the

The optimal temperature range of bacterial amylase, Aspergillus oryzae, were found and compared to the optimal temperature range of fungal amylase, Bacillus licheniformis, by testing the ability of the enzymes to hydrolyze starch after being exposed to different temperatures. The starch hydrolyzing ability of both the fungal amylase and the bacterial amylase was determined by mixing both amylases with starch and placing several tubes of the respective mixtures in four different temperatures each. Over the span of minutes, samples would be taken from each of the tubes and would be mixed with iodine. Due to the tendency of starch to color into a dark blackish-blue when combined with iodine, the degree of starch hydrolysis was then determined using a color coding scheme. The optimal temperature for both Aspergillus oryzae amylase and Bacillus licheniformis amylase was found to be within the 25 degree to 55 degree Celsius range. More specifically, the bacterial amylase seemed to hydrolyze starch more effectively as it spent more time exposed to the 55 degree Celsius temperature, whereas the fungal amylase seemed to work the best mostly when it had been exposed to the 55 degree Celsius temperature for 8 minutes. Within the resulting