Kerratin Synthesis Lab Report

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Isolating Keratin protein is done through oxidation and reduction. Keratin can be converted into soluble proteins in acid and be digestible by trypsin or pepsin when oxidized. After oxidation, reduction occurs in an alkaline reaction (basic solutions) with optimum pH of 10-13. Reduction also considered as hydrolysis dissolves disulfide groups, which then starts unravelling the fibrous keratin structures. Reductants such as thioglycolic acid, potassium cyanide and sodium sulfide/sulfite can be used to dissolve the disulfide groups. Scientists normally uses thioglycolic acid as their reduction solution because it specifically dissociates the disulfide bonds to sulfhydryl groups without further altering the rest of the protein. The remaining proteins are then soluble in acidic solution, with a precise isoelectric point (pH at which molecule carry no net electrical charge). In doing so, proteins are then digested by pepsin and trypsin, attacking the protein molecule very slowly. This oxidation and reduction method can extract keratin effectively and efficiently. …show more content…

Its clinical significance was utilized when proteins were still called albuminoids. The earliest recorded use of keratin in medicine was by Li Shi-Zhen, a Chinese herbalist in 1596. His published book, Ben Cao Gang Mu recorded one of his prescription medicine Xue Yu Tan or “Crinis Carbonisatus”, made from ground ash of pyrolized human hair. His medicine was believed to accelerate wound healing and blood clotting. Around 1905, John Hoffmeier describe his unique way of isolating the keratin protein for his own prescriptions. He was using lime to extract keratin from an animal’s horns, using the extracted keratin and crosslinking formaldehyde to make a topical

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