Does Amylase Affect The Rate Of Enzyme Activity

Enzymes are known as protein catalysts. The name protein catalyst suggests that most enzymes are made of proteins. A catalyst is a substance that speeds up chemical reactions without being consumed in the process. (Giuseppe, M 2002, p.69). After a reaction has been catalyzed, the catalyst can be used again to catalyze the same reaction. Enzymes reduce the activation energy (minimal energy) it takes for a reaction to take place. Enzymes can either catabolize (destroy), or anabolize (build up) a chemical system.

There are many types of enzymes and each has a specific job. Enzymes are particular types of proteins that help to speed up some reactions, such as reactants going to products. One of them is the amylase enzyme. Amylases are found in saliva, and pancreatic secretions of the small intestine. The function of amylase is to break down big molecules of starch into small molecules like glucose; this process is called hydrolysis. Enzymes are very specific; for example, amylase is the only enzyme that will break down starch. It is similar to the theory of the lock

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).

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.

To understand how and why the experiment was performed, one must understand what enzymes and substrates are. Enzymes are defined as proteins that are capable of speeding up a chemical reaction by reducing the amount of activation energy needed to catalyze that reaction (Raven, Johnson and Mason 2014). Enzymes regulate these biochemical processes

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

Most organisms rely on enzymes to digest their food. In all reactions, there is an activation energy barrier. During digestion, foods must be broken down quickly so that the organism can get the nutrients it needs. In order for the food to be broken down, the activation barrier must be lowered. Without enzymes, many organisms would no longer be able to obtain the nutrients and energy they need to live. In this experiment, the goal was to understand how and why enzymes work in such specific ways, and to discover how enzymes function under different conditions.

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

Amylase is a form of a enzyme. It is an enzyme that hydrolyze, or in other words it breaks down carbohydrates. There are two forms of amylase which are alpha and beta amylase enzyme. Each form is in charge of a different job within one’s digestive system. The specific enzyme we are working with in this lab would be amylase, it will be used to break down starch into a disaccharide maltose. Amylase are found in a variety of places such as; salivary glands and cells in your pancreas in which, they are initially formed. Amylase is found in nature in places such as all raw fruits and vegetables, whole grains, raw nuts, sprouted seeds, and legumes (Attia, et. al, 2016).

My hypothesis stated “if you increase the temperature, amylase activity will also increase until the temperature is about 38°C, where amylase activity will then decrease”. Recall the line of the graph in Figure 1. At 0°C, there was no amylase activity because the enzyme could not function at too cool of an environment. However, when the temperature increased to 23°C, there was some amylase activity occurring. When the temperature increased to 38.5°C, the amylase was able to function properly because it was the perfect temperature so there was a large amount of amylase activity. At 84°C, the temperature is too warm for the amylase so it becomes inhibited and can no longer function properly. On the graph, the peak shows the optimum temperature, 38.5°C, and the negative slope indicates

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 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 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

To find the effect of temperature on the activity of an enzyme, the experiment deals with the steps as follows. First, 3 mL if pH 7 phosphate buffer was used to fill three different test tubes that were labeled 10, 24, and 50. These three test tubes were set in three different temperature settings. The first test tube was placed in an ice-water bath for ten minutes until it reached a temperature of 2° C or less. The second tube’s temperature setting was at room temperature until a temperature of 21°C was reached. The third tube was placed in a beaker of warm-water until the contents of the beaker reached a temperature setting of 60° C. There were four more test tubes that were included in the procedure. Two of the test tubes contained potato juice were one was put in ice and the other was placed in warm-water. The other two test tubes contained catechol. One test tube was put in ice and the other in warm water. After

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).