Analysis of Structural Properties and Formation of Sericin Fiber by Infrared Spectroscopy

• Teramoto Hidetoshi

  New Silk Materials Laboratory, National Institute of Agrobiological Sciences

• Miyazawa Mitsuhiro

  Biomaterial Development Laboratory, National Institute of Agrobiological Sciences

抄録

Attenuated total reflection-Fourier transform infrared (ATR-FTIR) spectroscopy was applied to sericin fiber spun by Sericin-hope silkworms, developed to produce silk protein sericin in large amounts, and to a native sericin solution before spinning. Polarized ATR-FTIR measurement showed little orientation of sericin molecules in sericin fiber. Secondary structures of sericin fiber and native sericin were analyzed by Fourier self-deconvolution and curve fitting. The drying process of the native sericin solution was also followed to determine the effect of dehydration on sericin conformation. These analyses showed that β-sheets in native sericin increased with drying and that the secondary structure of air-dried sericin was similar to that of sericin fiber. These observations suggest that drying is a significant factor in the structural transition of sericin during fiber formation and that sericin undergoes only modest structural changes by spinning compared with fibroin.

収録刊行物

• Ｊｏｕｒｎａｌ　ｏｆ　Ｉｎｓｅｃｔ　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ　ａｎｄ　Ｓｅｒｉｃｏｌｏｇｙ

  Ｊｏｕｒｎａｌ　ｏｆ　Ｉｎｓｅｃｔ　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ　ａｎｄ　Ｓｅｒｉｃｏｌｏｇｙ 72 (3), 157-162, 2003

  社団法人 日本蚕糸学会

キーワード

• Sericin
• fiber formation
• ATR-FTIR
• orientation
• secondary structure

詳細情報

• CRID: 1390001205196465408
• NII論文ID: 10012453369
• NII書誌ID: AA11558849
• DOI: 10.11416/jibs.72.157
• ISSN: 18847978
• ISSN: 13468073
• NDL書誌ID: 6730766
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I6730766
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可