Amylase Is An Enzyme Commonly Found In Human Saliva. It

An enzyme also known as a protein, is a biological catalyst which speeds up chemical reactions by lowering the activation energy to increase the rate in which the reaction occurs. The enzyme used was amylase, which breaks down starch molecules into maltose. PH, substrate concentration, salt concentration, and temperature. When enzymes reach a low temperature, the activity is slowed down of molecule movement, but the enzyme is not destroyed. Once enzymes are placed in optimal temperatures once again, it will restore its activity to a normal rate. When enzymes reach too high above optimal temperature, the enzyme is denatured and cannot be restored. In the experiment performed the activity of breaking down starch in fungal and bacterial amylase was being tested at a range of temperatures and time. The fungal and bacterial amylase work best at optimal temperature. Amylase will function best at sixty degrees Celsius at 10 minutes when starch had been one hundred percent hydrolyzed. Hydrolyzed is the breakdown of molecules through addition of water. The experiments independent variables were the time, temperature and enzyme used. The dependent variable was the enzyme activity that broke down the starch into maltose. The controlled variables were the temperature baths, the iodine drop amount, the mixture drop amount, and location of experiment. The control group was the zero minutes without amylase at

Amylase is an enzyme found in the human body. It is made in only two places, the pancreas and in the salivary glands. Amylase is an important enzyme because it breaks down starch. The enzyme works by binding with the starch substrate and breaking it down to its base component of glucose. There is a difference in the way that salivary and pancreatic amylase work. The salivary amylase breaks down the simple carbohydrates in the form of starch, starting the digestion process. Pancreatic amylase works to process the more complex carbohydrates that are in the stomach and intestines. The efficiency of the enzyme depends on environmental factors including temperature, pH level, inhibitors, activators, number of enzymes available, and number of substrates

specific enzyme (Knowles, 1991). One part of the enzyme, salivary amylase, is that alpha amylase is in the saliva of most animals because this enzyme breaks down starch (Jacobsen, Melvaer, Hensten- Pettersen, 1972). In the presence of starch, this enzyme is present in saliva, but is not present when there is no starch present (Jacobsen, Melvaer, Hensten- Pettersen, 1972). The conditions for salivary amylase to have a reaction with starch would change in temperature and enzyme concentration, as well as, monitoring the pH levels (Jacobsen, Melvaer, Hensten- Pettersen, 1972). Salivary amylase is an enzyme is human saliva that helps in digestion of specific substrates, such as starch (Hudman, Friend, Hartman, Ashton, Catron, 1957). It breaks down starch molecules by splitting maltose from the non-reducing end of a gluten molecule (Jacobsen, Melvaer, Hensten-Pettersen, 1972).

Amylase is an enzyme that is in human’s saliva as well as the pancreas. Enzymes are biological catalysts that speed up a chemical reaction. They break down complex molecules into simple ones. In this case, amylase converts starches (complex molecule) into simple sugars. That is why foods like potatoes for example, may taste sweet to us, because they contain starch. The optimum pH for pancreatic amylase is the pH of 7. In the experiment I have used buffer solutions with the pHs of 2.8, 4 and 6.5. I have also used iodine and starch. Normally, iodine is orange-yellow, however when you add starch to it, the solution will turn blue-black.

2. Salivary amylase, an enzyme in saliva that breaks down starch, has an optimal pH of 6.7-7.0. Explain why salivary amylase is active

amylase enzyme and the optimal temperature for fungal and bacterial amylase. In order to make

In this lab our group observed the role of pancreatic amylase in the digestion of starch and the optimum temperature and pH that affects this enzyme. Enzymes are located inside of cells that increase the rate of a chemical reaction (Cooper, 2000). Most enzymes function in a narrow range of pH between 5 through 9 (Won-Park, Zipp, 2000). The temperature for which enzymes can function is limited as well ranging from 0 degrees Celsius (melting point) to 100 degrees Celsius (boiling point)(Won-Park, Zipp, 2000). When the temperature varies in range it can affect the enzyme either by affecting the constant of the reaction rate or by thermal denturization of the particular enzyme (Won-Park, Zipp, 2000). In this lab in particular the enzyme, which was of concern, was pancreatic amylase. This type of amylase comes from and is secreted from the pancreas to digest starch to break it down into a more simple form called maltose. Maltose is a disaccharide composed of two monosaccharides of glucose. The presence of glucose in our experiment can be identified by Benedicts solution, which shows that the reducing of sugars has taken place. If positive the solution will turn into a murky reddish color, where if it is negative it will stay clear in our reaction. We can also test if no reduction of sugars takes place by an iodine test. If starch is present the test will show a dark black color (Ophardt, 2003).

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

Experiment #2: Investigating the Effect of Environmental pH on the Activity of Porcine Pancreatic Amylase

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 objective of the lab was to examine the effects of environmental variables on the functions of an enzyme. To the point, an experiment was conducted to test the effect of pH on the function of the enzyme Amylase.

In Table one the solution remained brown since there is no starch present in the mixture in tube 1A.The solution turned blue black due to presence of starch in the solution in tube 2A.The solution remained brown since there is no starch present in the mixture in tube 3A.The solution turned blue black due to presence of undigested starch in the solution. Boiling amylase denatures the enzyme hence it cannot digest amylase in tube 4A.The solution remained brown since there is no starch present in the mixture. All is digested in tube 5A.In tube 6A the solution turned blue black due to presence of undigested starch in the solution. The extremely low temperatures inhibit the action of the enzyme amylase. There was no presence of maltose in tube

Enzymes are biological catalysts, mainly proteins for this experiment, generated by an organism to speed up chemical reactions. They have active sites on which the substrate is attached, and then broken up or joined. For this experiment we are going to work with the enzyme a-amylase. Amylase is an enzyme that breaks starch down into sugar. Amylase is present in human saliva, where it begins the chemical process of digestion. Foods that contain starch like rice and potatoes. Amylase turns some of their starch into sugar in the mouth. The pancreas makes

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

Hypothesis: If we decrease the level of pH in the enzyme Amylase, it will not be able to denature the carbohydrates in the potato starch solution after 10 drops because enzymes are very sensitive to pH levels and lowering it too much will compromise its ability to break them down.