Enzyme Activity II: The Breakdown Of Starch Due To Amyylase

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Enzyme Activity II: The Breakdown of Starch Due to Amylase Enzyme
Ceara Sibley
Central Michigan University
Biology Lab 110 3:00-5:50
October 6, 2014

Introduction
The ultimate goal of this experiment is to determine how much starch a particular amount of amylase enzyme is able to convert into sugar in the span of one minute. Certain variables can change the amount of sugar converted, such as the pH or temperature of the given solution. Enzymes, natural catalyst, speed up chemical reactions through a process of folding. Small pockets called “active sites” are created through the folding and allow the reaction to take place more easily. How an enzyme is folded is very critical, interactions between different amino acids determine the certain functions of an enzyme. These interactions also allow for enzymes to keep their proper shape, if the enzymes are not folded properly or become unfolded, they will no longer function, and is said to be “denatured”.
The denaturing of enzymes is what causes the change in the conversion of sugar. Many environmental factors, such as extreme pH, temperature, or the absence of other molecules can lead to denaturing of enzymes. Most enzymes have very specific conditions in which they can work and survive under. When an amylase enzyme is folded and shaped properly it is fully functional. The amount of starch in the solution changes over time due to the corrosive properties of the amylase enzyme.
The purpose of this experiment is to measure and record the rate of the enzyme activity in the experimental conditions of pH. Extreme pH can denature an enzyme, leaving it unable to function. Each enzyme has an optimum pH where it works the best, for example intestinal enzymes have an optimum pH of 7.5 (Temperature). The knowledge of how enzymes work is very important in the biological world, it allows for scientist to have a better understanding of chemical reactions in nature and in laboratories. Enzymes also help speed up the reactions in our body, without these natural catalyst reactions would take place too slowly and individuals would die.(Who am I). By doing this experiment scientist will have a better understanding of why enzymes become denatured and what factors cause it. This experiment answers these questions by using amylase enzyme to break down starch. Hypothetically over time the starch will continue to breakdown into sugars due to the amylase enzyme, or overtime there will be no change in the starch. (Fulop).

Methods
The experiment began with the creation of the master mix, which consisted of the starch solution, buffer and enzyme amylase. The master mix was created to be tested on the experimental condition of pH. The master mix totaled to be 15 mL. An individual must note that the creation of the experimental solution must be in bulk to reduce experimental error. It is also very important that the amylase enzyme is not added until the individual is ready to start the experiment. Next the master mix tube was labeled with the assigned experimental condition of pH. After that, 3 drops of I2KI were added to five spectrophotometer cuvettes; this represented one time
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