Experimental Analysis on Enzymatic Behavior of Human and Fungal Amylase

Topics: Enzyme, Temperature, Amylase Pages: 6 (1928 words) Published: February 13, 2012
Experimental Analysis on Enzymatic Behavior of Human and Fungal Amylase

Lab name and number: Enzymes, Lab #5
Panther I.D: 2640403
Shayra Medal
Instructor: Emily Nodine
Section U21
October 26, 2011

Abstract Section
The concept of this experiment was to analyze the enzyme Amylase and its environmental behavior. Amylase breaks down the biological macromolecule, carbohydrates, specifically starch into condensed subunits categorized as monosaccharaides or disaccharides. Two types of variables were human and fungal Amylase. Sum of six trials for both variables were conducted with two minutes intervals was measured for the duration. After every two minutes, the components were taken out of their controlled environment and joined with Iodine to observe visual change. The results gave supported facts that human amylase catalyzes at optimal level at forty-five degrees and fungal amylase at sixty degrees. At temperatures other than optimal for both observations concluded less progression to the visual change (Venturi, 2009). Amylase in a mixture of starch produced different color variations when stimulated with its independent variable of temperature showing its effectiveness. The dependent variable was the visual change of color from variations of black to yellow. According to our experiment data all enzymes do not establish one optimal temperature in which they can catalyze. If this were false the results of having all enzymes work in all temperatures would be chaotic. This is the data found to why enzymes were not able to catalyze at the highest temperature which was ninety degrees. This resulted in high levels of starch being left. Introduction Section

The presence of enzymes is essential for life’s existence. The human body as well as other Eukaryotic organisms need for biological processes are influenced by enzymes. These Enzymes go through a series of chemical reactions such as breaking hydrogen bonds which, causes the activation energy to be lowered. Enzymes lower the activation energy that is essential for a chemical reaction to start(Venturi, 2009). Their specialized three-dimensional figure joins to substrates, which are specified molecules that process with the reaction, to bind to the active sites. After being produced, products are set free from the active site allowing new substrates to enter the site continuing the catabolic process. For enzymes to function optimally, several factors must be in accordance. The first is PH. If the environment is acidic or at the lower end of the PH scale, it will affect the stability of the enzyme. The average PH in which enzymes operate is in the range from 6 to 8. The ph level of the solution that the enzyme is in must be is between 4.5-5.2 (Jeremy Mark, 2002) . Temperature as well plays a major role in the productivity of all enzymes. In a cold environment, the enzymes catabolic activity is delayed. At high temperatures the enzymes are denatured due to its protein structure. Denatured simply means the protein shape is deformed rendering the induced fit of the protein. Additional information, that affects an enzymes ability to perform are inhibitors. Inhibitors bind to the active site of enzymes, preventing the substrate from binding to the active site. When inhibitors bind to the active site it is known as competitive inhibition. In contrast if an inhibitor binds to an active site and morph the shape of the active site it would be known as non-competitive inhibition (Reeve, 2001). This will prevent any other substrate to bind due to its specificity in shape. In contrast, to inhibitors there are cofactors which assist in the aid of catabolization . Cofactors weaken the bonds aiding the enzymes. Method Section

The hypothesis was that the two extremities of temperatures being 0 degrees and 95 degrees Celsius would either denature the process of breaking down the starch or delay the process due to freezing temperatures. The null...

Cited: Section
-Tymoczko, John L.; Stryer Berg Tymoczko; Stryer, Lubert; Berg, Jeremy Mark (2002). Biochemistry. San Francisco: W.H. Freeman. ISBN 0-7167-4955-6
-Eric C. R. Reeve, ed (2001-06-23). "Enzyme Activity". Encyclopedia of genetics. USA: Fitzroy Dearborn Publishers, I. pp. 157. ISBN 9781884964343. Retrieved 2011-10-20.
-Udani J, Hardy M, Madsen DC (March 2004). "Blocking carbohydrate absorption and weight loss: a clinical trial using Phase 2 brand proprietary fractionated white bean extract". Altern Med Rev 9 (1): 63–9.
- Robert Hill and Joseph Needham, The Chemistry of Life: Eight Lectures on the History of Biochemistry (London, England: Cambridge University Press, 1970), page 17
-Venturi, S.; Venturi, M. (2009). "Iodine in evolution of salivary glands and in oral health". Nutrition and Health 20 (2): 119–134.
-Thomas Pitzer, General Biology 1: Laboratory Manual (Mc Graw Hill, 2006), Page 49
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