
doi: 10.1271/bbb.68.1875
pmid: 15388962
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.
Protein Denaturation, Calorimetry, Differential Scanning, differential scanning calorimetry (DSC), Temperature, Water, Feathers, Fourier transform infrared spectroscopy (FT-IR), thermal stability, Phase Transition, X-ray diffraction, Spectroscopy, Fourier Transform Infrared, Animals, Keratins, keratin, Chickens
Protein Denaturation, Calorimetry, Differential Scanning, differential scanning calorimetry (DSC), Temperature, Water, Feathers, Fourier transform infrared spectroscopy (FT-IR), thermal stability, Phase Transition, X-ray diffraction, Spectroscopy, Fourier Transform Infrared, Animals, Keratins, keratin, Chickens
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