アセチルセルロース分子中のβ-1, 4-グルコシド結合に対するセルラーゼの作用 Action of Cellulase on β-1, 4-Glucosidic Bonds in Acetylcellulose Molecules^*

この論文にアクセスする

この論文をさがす

著者

抄録

After sufficient degradation of acetylcelluloses with degree of substitution (DS) from 0.58 to 1.08 by cellulase, glucose as well as monomers, dimers, trimers, and oligomers of acetylated saccharides were detected in their hydrolysates. The amount of liberated glucose was rather close to the number of unsubstituted glucose units in the molecular chains, estimated theoretically by Timel's method. The extent of enzymatic hydrolysis of the substrates was decided by the number of unsubstituted glucose units in their molecules. In the case of the acetylcellulose with DS=1.56, no chain cleavage was observed. Consequently it was found that cellulase can interact with unsubstituted glucose units in the acetylcellulose and cleaves β-1, 4-glucosidic bond attached to unsubstituted glucose unit.

収録刊行物

  • 繊維学会誌  

    繊維学会誌 54(3), 134-141, 1998-03-10 

    The Society of Fiber Science and Technology, Japan

参考文献:  13件

参考文献を見るにはログインが必要です。ユーザIDをお持ちでない方は新規登録してください。

各種コード

  • NII論文ID(NAID)
    10002059102
  • NII書誌ID(NCID)
    AN00131651
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    00379875
  • NDL 記事登録ID
    4424528
  • NDL 雑誌分類
    ZP33(科学技術--繊維工学・工業)
  • NDL 請求記号
    Z17-189
  • データ提供元
    CJP書誌  NDL  J-STAGE 
ページトップへ