Characterizing Wool Keratin
January 2009
in “
Advances in Materials Science and Engineering
”
Studysummary This study demonstrated that keratin can be effectively extracted from wool using alkaline solutions and that the extracted keratin maintains reactivity similar to that from other low-value sources like cattle hair.
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The study characterized wool keratin using alkaline hydrolysis methods, achieving keratin powder recovery rates between 68% and 82%. By treating wool with NaOH solutions, keratin amides and disulfides were converted into acids and smaller protein fragments, which were analyzed using techniques like MALDI-TOF and SEM. The presence of Type II keratin intermediate filament and microfibrillar proteins was identified, along with specific amino acid sequences suggesting potential for enzymatic self-crosslinking. FTIR spectra confirmed cysteic acid formation and disulfide linkage cleavage. The research demonstrated the potential for producing high-value keratin products efficiently, maintaining keratin's structural integrity, and opening new market potentials for wool.
