Egg Albumen Experiment

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Egg Albumen Experiment The purpose of this investigation is to establish which is the lowest concentration of Copper (II) Sulphate solution that will denature a sample of egg albumen (egg white) at room temperature. The base of the reaction is the globular protein (albumen) being denatured by a heavy metal (Copper (II)), the copper (II) reacts with the NH3 group causing it to denature, this means the proteins' secondary and tertiary structures are being altered and refolding into different shapes, this resulting in a change from the substance being clear to turning opaque.[1] As the concentration of the denaturants increases more folding and changing of shape will occur and therefore more denaturing will occur and at a faster rate. From this I can predict that that lowest concentration of the solution is approximately at 0.03m solution. The reason this is not lower, is that a lower concentration will have little effect on the protein. To conduct this experiment I will dilute the 0.1mol dm -3 using distilled water. The reason for choosing so is that I have found from previous experiments I have conducted during the year (namely food tests- protein with biuretts reagent) that distilled water is the best diluting agent as its chemical properties will not interfere with the reaction. The procedure for the experiment is as follows: Apparatus list ============== § Test tubes X 11 § 0.10 molar dm -3 Copper (II) Sulphate solution § distilled water § egg albumen from 3 eggs. § Syringe X 12 § colorimeter § tripod § 100ml beaker § Bunsen burner § test tube holder § safety glasses § gloves § test tube pen § test tube method ====== Before conducting the experiment I would conduct a simple test for the protein by placing a sample of the albumen into a test tube and add biurett reagent. This contains copper (II) sulphate and sodium hydroxide.

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