title: Properties of alkaline-hydrolyzed waterfowl feather keratin.
abstract: The properties of hydrolyzed feather keratin (HFK) were compared to those of hydrolyzed wool keratin (HWK) with the aim of developing better ways to utilize feather keratin waste. Amino acid analysis showed that HFK contained more hydrophobic amino acids did than HWK. Although gel permeation chromatography indicated that HFK and HWK had more low-molecular weight peptides than their intact sources, Fourier transform infrared spectroscopy indicated that both hydrolyzed keratins retained their original secondary structure. The physical properties of HFK were evaluated by treating HFK to human hair fibers. HFK treatment enhanced significantly the surface hydrophobicity and strength of fibers, and HFK was more permeable into hair fibers. These results suggest that HFK is suitable for industrial applications to improve fibers. In addition, HFK may be suitable for raw material of products requiring both flexibility and hydrophobicity, such as films and biodegradable plastics.
authors.affiliation: Applied Protein Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Tokyo, Japan.
authors.forename: Yuichi
authors.initials: Y
authors.lastname: Tsuda
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Nomura
mesh_terms: D000468:Alkalies / Q000737:chemistry; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D063566:Biodegradable Plastics; D055598:Chemical Phenomena; D002850:Chromatography, Gel; D005241:Feathers / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D057927:Hydrophobic and Hydrophilic Interactions; D007633:Keratins / Q000737:chemistry*; D008970:Molecular Weight; D018583:Pliability; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D000468:Alkalies; D000596:Amino Acids; D063566:Biodegradable Plastics; D007633:Keratins
keywords: feather; keratin; properties and characterization