Amylase Is An Enzyme Commonly Found In Human Saliva. It

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

How pH Affects the Break Down of Starch by the Enzyme Amylase Hypothesis: The optimum pH for the reaction of starch with amylase is pH 7. PH values lower or higher than this value will result in a slower rate of reaction. Amylase works in the range pH 3 to pH 11.

Specifically, alpha-amylase is produced by the salivary glands of Homo sapiens (Humans) as well as many other mammalian species and is encoded by the gene AMY1A (Tracey 2017, p.22). The enzyme alpha-amylase is able to uptake polysaccharides including starch and glycogen as a substrate then hydrolyze the alpha-1,4-glycosidic linkages that connect the monosaccharides together (Tracey 2017, p.37). This is the reason as to why salivary amylase is also referred to as alpha-amylase (Tracey 2017, p.22).

In this lab experiment the action of the enzyme Amylase was observed on starch (the substrate). Amylase changed the starch into a simpler form, the sugar maltose, which is soluble in water. Maltose then breaks down the glucose chains of starch in the pancreas and intestines. Amylase is present in human saliva, and begins to act on the starch in the food while still in the mouth. Exposure to heat or extreme PH (acid or base) will denature proteins. Enzymes, including amylase, are proteins; if denatured enzymes can no longer act as a catalyst for the reaction. In the presence of potassium iodide, starch turns a dark purple color; however maltose does not react with I2KI. The rate of fading of starch allows a quantitative measurement of reaction rate.

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

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

test the pH of the amylase a drop of the solution should be put on pH

And for our results of amylase activity, although there could be the amount of error happened in the personal result, the data that we used during the report was gathered from all of the data in whole bay, therefore, it helped to get a reliable

Effect of varying Temperatures on Enzymatic Activity of Bacterial and Fungal Amylase and hydrolysis of Starch

Amylase is an enzyme that is located in human saliva. It is solely accountable for breaking down starch as a way to start the breakdown of food and is one of the first steps of digestion. The time at which the enzyme starts the chemical reaction with starch is called the reaction rate. In order to study how amylase works against starch, this experiment consisted of two tests; each testing a different condition of amylase. The first test was to simply study the reaction between saliva and amylase and note the reaction rates. The second test was to see if increasing the pH would decrease the reaction rate or halt it all together. Saliva was collected, diluted, and tested for reactions between starch and amylase. Another sample of saliva was collected, diluted, and had its pH increased and tested for reaction rate. The findings after the experiment was conducted aligned with the original hypothesis. The change in pH did show a significant decrease in the reaction rate.

The aim of this experiment is to analyse the affects amylase inhibitors have on the rate of enzyme activity.

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.

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.

Therefore, we hypothesized that pancreatic amylase has an optimum pH and temperature for activity. If so, what are the pH and temperature? In order to do this we tested the activity of this enzyme under various pH values and temperatures.