Title: Examining Some Properties of the Enzyme -amylase
In this experiment a deeper meaning in the catalysts of reactions is studied. Catalysts accelerate chemical reactions without permanently changing the reaction. Enzymes, catalysts in biochemical reactions, are globular proteins which lower the activation energy needed to begin a reaction and therefore increase the rate at which efficient reactions can occur. Proteins (henceforth enzymes) are complex molecules made of amino acids in polypeptide chains held together by peptide bonds. The structure of proteins is broken up into primary, secondary, tertiary, and quaternary structures which create complex structures which can be separated and identified by paper chromatography, or more importantly spectrophotometry can determine the concentration of proteins in an aqueous solution.
Spectrophotometry is a quantitative analysis used to determine the amount or concentration of a substance ( -amylase) from its ability to absorb radiant energy. The substance is usually colored and radiant energy used is visible light, which passes through the solution and is either absorbed or transmitted. The spectrophotometer measures is an instrument
The reacting molecule in an enzymatic reaction is called a substrate. The purpose of this lab is to determine the maximum velocity and substrate concentration for the reaction of -amylase and starch. The substrate (starch) and the enzyme ( - amylase) come together for a short time and then break down to yield the products and enzyme. Once the enzyme configuration is altered in the reaction it is useless and becomes decomposed in the normal course of cellular metabolism. The rate of the enzymatic reaction, needed for figures three and four, is set by the rate at which the enzyme-substrate complex forms and then decomposes to form the product. The amount of time it takes the enzyme to effect the substrate and the frequency at which the complex (enzyme-substrate) forms. The frequency depends greatly on the concentration of the substrate. As the reaction proceeds, and starch is turned into the product by the enzyme the chances of the enzyme encountering a starch molecule becomes less and so the reaction rate decreases. Most starch is converted at the initial stage of the reaction and therefore the maximum reaction rate is highest at this stage in the reaction. From a resulting curve from of the enzymatic reaction, showing disappearance of substrate over time, the maximum velo
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