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

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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, 2003-10-31

    社団法人 日本蚕糸学会

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各種コード

  • NII論文ID(NAID)
    10012453369
  • NII書誌ID(NCID)
    AA11558849
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    13468073
  • NDL 記事登録ID
    6730766
  • NDL 雑誌分類
    ZR7(科学技術--農林水産--農産)
  • NDL 請求記号
    Z54-J696
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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