Protein Enzyme Lab
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
For the purpose of our lab, wavelength will not need to be found, but merely the spectrophotometer must be set to 560 nm. The optimal level of enzyme efficiency is important in not only simple experiments such as this, but in animal/human body upkeep and simple internal systems such as digestion. ) tends to increase molecular motion, and therefore increases the chances of the enzyme encountering a substrate. Certain physical environment factors of the enzyme such as temperature and pH can affect the reacting molecules and catalytic activity of the enzyme. 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 velocity at which that particular reaction occurs and the concentration of the substrate at which Vmax/2 occurs can be determined. A relationship between absorbance and concentration can be made by the Beer-Lambert Law which states absorbance is equal to a molar extinction coefficient times the concentration of the solution times the length of the light path through the solution. At really high temperatures the shape of tertiary structure of the protein can be changed, and thus the enzyme is not nearly as effective, and the reaction rate shall slow down. However great high temperatures may seem, there is a limit. The efficiency of enzymes can be graphed in a bell or spike shape. 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. The absorbances over a range of known concentrations of the substance are measured at lambda max, the wavelength which shows maximal absorbency. The concentration of a solution can be determined because the amount of light absorbed by a solution is dependent on its concentration. 0 is neutral, anything greater is base, anything less is acid. 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.
Common topics in this essay:
Beer-Lambert Law,
Properties Enzyme,
reaction rate,
enzymatic reaction,
concentration solution,
radiant energy,
tertiary structure protein,
chances enzyme encountering,
stage reaction,
maximum velocity,
enzyme encountering,
substrate concentration,
substrate reaction,
chances enzyme,
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Acceptance Essays
