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Effects of Different Ph Level on Amylase in Starch

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Effects of Different pH Level on Amylase in Starch

Introduction
Amylase, a family of proteins that differ in isoforms, is a digestive enzyme found in saliva and pancreatic fluid that helps digest starch into simple sugars. (Scannapieco et. al., 1993). Amylase is the first step in digesting starch, which is used for the intake of carbohydrates or energy in humans. (Butterworth et. al., 2011). Amylase functions in the hydrolysis of starches, which produces glucose monomers. (Karp, 2010). This is essential in glycolysis and the harvesting of ATP. Since amylase is also a protein that performs enzymatic reactions, the secondary and tertiary structures are affected by external stimuli like pH. (Karp, 2010). When the structure is altered the affinity of the enzyme is changed. (Luesse, 2012). The point where the majority of enzymes are found to be most active is in the neutral pH range near 7. (Guyot et. al., 2000). Therefore, it can be said that extremely high or low pH’s denature an enzyme. By finding the specific pH at which amylase is most active, optimum production can be achieved. (Guyot et. al, 2000). In our experiment, we want to determine what pH levels is optimum for the enzymatic activity of amylase. To see if starch is broken down to glucose amylase, a spectrophotomer is used to see the amount of light that passed through. The more light that passes through the test tube means more starch was broken down into glucose. (Luesse, 2012). We hypothesized that the enzyme amylase will be most optimum around the pH of 7 and less active away from neutrality.
Bioinformatics is an online database by which, scientists can look up any known protein sequence and protein function. It focuses on the sequence and structure of DNA, RNA, and protein. (Goto et. al., 1998). Using bioinformatics, you can take an unknown protein and compare its sequence to any known protein.

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