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Properties of alkaline‐hydrolyzed waterfowl feather keratin
Author(s) -
Tsuda Yuichi,
Nomura Yoshihiro
Publication year - 2014
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1111/asj.12093
Subject(s) - hydrolysis , chemistry , keratin , acid hydrolysis , alkaline hydrolysis , biochemistry , biology , paleontology
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, F ourier 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.