Amylase : Human Amyylase The Hydrolysis Of Starme

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

1) Amylase is utilized to break down starch molecules into more simple sugars for use by the body. It performs this function by hydrolyzing glycosidic linkages in the polysaccharide chain.

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).

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.

Hydrolysis of starch for fungal amylase Aspergillus Oryzae and bacterial amylase Bacillus Licheniformis at different temperatures.

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

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

The effects of temperature on fungal amylase Aspergillus oryzae, and bacterial amylase, Bacillus licheniformis ability to break down starch into maltose was studied. The study determined the optimal temperature the Aspergillus oryzae and Bacillus licheniformis was able to break down the fastest. The starch catalysis was monitored by an Iodine test, a substance that turns blue-black in the presence of starch. Amylase catabolizes starch polymers into smaller subunits. Most organisms use the saccharide as a food source and to store energy (Lab Manual, 51). The test tubes were labeled with a different temperature (0°C, 25°C, 55°C, 85°C). Each test tube was placed in its respective water baths for five minutes. After the equilibration process, starch was placed in the first row of the first row of the spot plate. Iodine was then added to the row revealing a blue black color. The starch was then added to the amylase. After every two minute section a pipette was used to transfer the starch-amylase solution to place three drops of the solution into the spot plate row under the corresponding temperature. Iodine drops was placed in the row. Color changes were noted and recorded. The results showed Aspergillus oryzae was found to have an optimal temperature between 25°C and 55°C and Bacillus licheniformis was found to have an

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 a digestive enzyme. The enzyme is found in the salivary glands in your mouth

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).

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.

In this lab we looked at the role of pancreatic amylase in the digestion of starch and the effect that temperature and pH has on this enzyme. Enzyme’s work as catalysts that increase the rate of chemical reactions within cells (Cooper, 2000). In order to do this, enzymes must show two essential properties: these two fundamental properties of enzymes include increasing the rate of chemical reactions without being eternally altered by the reaction and accelerating the reaction rate with keeping the reactants and products in chemical equilibrium (Cooper, 2000). Enzymatic catalysis is necessary for life. Most biochemical reactions would not occur under the mild temperatures and pressures

Numerous enzymes are needed in dough to break down starch into simple sugars that yeast can digest. The process is a very complex one, and includes the enzymes alpha amylase and beta amylase. Starch occurs in two different forms, a branched form called amylopectin and an unbranched chain called amylose.