This experiment consisted of setting up a control group of starch in various temperature and then placing both fungal amylases and bacterial amylases in a mixture of starch and placing the solution of amylase and starch in various temperatures of water. After a certain amount of time- different amount of time needs to be used in order to have reliable results- iodine is added in a well on spot plates, then two drops of the mixture of amylase-starch is added from each temperature used, by adding iodine into the plates the mixture will show how much starch was hydrolyzed, this is used to calculate the amount of enzymatic activity each mixture had at the different set temperatures and at the different times the solution was extracted from. The experiment was designed to find the optimal temperature in which both fungal amylase and bacterial amylase could function appropriately to produce an enzymatic reaction to a certain solution. The results concluded that bacterial amylase had an optimal temperature of around 60°C to 65°C. The fungal amylase on the other hand had an optimal temperature of around 40°C. These results show that the bacterial amylases have a higher optimal temperature than fungal amylases, meaning that bacterial amylases can react at higher temperature environments then the fungal amylases, that had a cooler optimal temperature that would denature at those high temperature conditions.
Before doing research on amylases, an explanation of enzymes is needed to fully understand each part of the experiment. An enzyme is a protein that helps speed up a chemical reaction (Raven, 2011). An enzyme is a catalyst, which is made by living cells; usually enzymes assist in developing the metabolic process of cells (Underkofler et al, 1958). The way in which enzymes speed up the chemical reaction is by lowering the activation energy, which the energy needed to start a reaction (Alberte et al, 2012). The way in which the chemical reactions occur is by having the substrates or the reactants bind to an active site of the enzyme- pockets of clefts (Raven, 2011), and form an enzyme-substrate complex, which is the form the to make by binding, this helps the substrate chemically bond and start the chain reactions needed in order to form the product or the end result (Alberte et al, 2012). The experiment shows an enzyme catabolizing starch molecules, representing the enzymatic activity of the amylase. When starch is catabolized it means that the reaction occurred by breaking down the starch molecules to maltose to produce energy from them (Raven, 2011). As well, it shows the starch going through hydrolysis, which is a reaction that breaks a bond by adding water to the bond (Raven, 2011). For an enzyme to properly function there are certain factors that it cannot be affected by, including: pH, substrate concentration, salt concentration, temperature etc. (Alberte et al, 2012). Enzymes are not only used in developing the metabolic process but also in daily life use. Amylase is one enzyme that is used often in daily life, due to it being produced by the body to break down starch (Alberte et al, 2012). Amylase has mostly been found in microorganisms such as bacteria and fungal which the experiment focused on, although some amylases have been found in both plants and animals (Pandey et al, 2000). Amylases as mentioned before have many different applications for daily life such as: in the use of food, pharmaceutical, textile etc. (Underkofler et al, 1958). The first use of an enzyme was in industries using fungal amylases as a pharmaceutical benefit to treat for digestive disorders in 1894 (Pandey et al, 2000) the preparation of the enzyme treatment was used by wheat bran koji culture adding the fungal amylase to it (Aiyer, 2005). In the food industry the use of amylases was used to convert...