Physicochemical properties of keratin extracted from wool by various methods

Abstract

Keratin from wool fibers was extracted with different extraction methods, for example oxidation, reduction, sulfitolysis, and superheated water hydrolysis. Different samples of extracted keratin were characterized by molecular weight determination, FT-IR and NIR spectroscopy, amino acid analysis, and thermal behavior. While using oxidation, reduction, and sulfitolysis, only the cleavage of disulfide bonds takes place; keratin hydrolysis leads to the breaking of peptide bonds with the formation of low molecular weight proteins and peptides. In the FT-IR spectra of keratoses, the formation of cysteic acid appears, as well as the formation of Bunte salts (–S–SO3–) after the cleavage of disulfide bonds by sulfitolysis. The amino acid composition confirms the transformation of amino acid cystine, which is totally converted into cysteic acid following oxidative extraction and almost completely destroyed during superheated water hydrolysis. Thermal behavior shows that keratoses, which are characterized by stronger ionic interaction and higher molecular weight, are the most temperature stable keratin, while hydrolyzed wool shows a poor thermal stability.