title: Thermal behavior of fowl feather keratin.
abstract: Differential scanning calorimetry (DSC) was applied to elucidate the thermal behavior of fowl feather keratins (barbs, rachis, and calamus) with different morphological features. The DSC curves exhibited a clear and relatively large endothermic peak at about 110-160 degrees C in the wet condition. A considerable decrease in transition temperature with urea and its helical structure content estimated by Fourier transform infrared spectroscopy (FT-IR), and the disappearance of one of the diffraction peaks with heating at 160 degrees C for 30 min, indicated that DSC could be used to evaluate the thermal behavior of keratin. Barbs showed a lower denaturation temperature than rachis and calamus. The pulverized samples showed a slightly higher denaturation temperature than the native samples. In the dry condition, thermal transition occurred in a markedly higher temperature region close to 170-200 degrees C. It is hence concluded that fowl feather keratins have very high thermal stability, and that the elimination of water brings about even greater thermal stability.
authors.affiliation: Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Japan. k-taka@cc.tuat.ac.jp
authors.forename: Koji
authors.initials: K
authors.lastname: Takahashi
authors.forename: Hirosaburo
authors.initials: H
authors.lastname: Yamamoto
authors.forename: Yoshiko
authors.initials: Y
authors.lastname: Yokote
authors.forename: Makoto
authors.initials: M
authors.lastname: Hattori
mesh_terms: D000818:Animals; D002152:Calorimetry, Differential Scanning; D002645:Chickens; D005241:Feathers / Q000737:chemistry*; D007633:Keratins / Q000737:chemistry*; D044367:Phase Transition; D011489:Protein Denaturation; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature; D014867:Water / Q000737:chemistry
chemical_list: D014867:Water; D007633:Keratins