Abstract
Chicken feather keratin was solubilized by 0.1 n sodium hydroxide heating at 90°C for 15 min. A half of the starting keratin was recovered in a water soluble protein fraction but another half was dialyzed out as free amino acids. Many of these amino acids showed a different behavior on the column chromatography compared with the standards. Polypeptide production was not observed during the solubilization process of feather keratin by alkali. Solubilized feather keratin had an amino acid composition widely different from the ordinary feather keratin, rich in methionine, lysine and glutamic acid and poor in threonine, serine, cystine and arginine. Among the several methods tried to solubilize feather keratin, sodium hydroxide was the most drastic one in hydrolyzing the molecule.
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