The Extraction And Absorption Of Casein

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Part A Part A of this experiment examines the extraction and absorption of casein within milk. The foremost objective is to effectively remove the casein-rich curds from the milk by altering the pH using acetic acid. Then, the objective is to dry the curds so that only the proteins and various other materials remain. Afterwards, this part aims to evaluate the spectrum of copper (II) sulfate pentahydrate, then use this spectrum in comparison to a solution of Casein sodium potassium tartrate and NaOH in a copper (II) sulfate solution, also known as the biuret test. This denotes the presence of protein.1 The ultimate objective of this part is to characterize the protein Casein. Casein is a highly hydrophobic protein.1 However, it’s compact spherical particles are able to be held together through interactions with calcium in milk. This allows the hydrophobic protein to be suspended within the polar solution through the presence of calcium ions. When acid is added to a solution the number of H3O+ increases.1 Because proteins contain regions which are charged, the addition of large amounts of acid alters the charge of the side chains these changes can dramatically alter the non-covalent interactions of the side-chains.1 Essentially, the addition of the acid creates an environment which alters the charges of the side chains this causes significant changes to the forces within the protein folds, altering the protein. Because acid is added to the milk, it creates an environment

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