Action of Cellulase on .BETA.-1,4-Glucosidic Bonds in Acetylcellulose Molecules.

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  • Sonq Zheng
    Department of Applied Chemistry & Biotechnology, Faculty of Engineering, Fukui University
  • Hisada Kenji
    Department of Applied Chemistry & Biotechnology, Faculty of Engineering, Fukui University
  • Hori Teruo
    Department of Applied Chemistry & Biotechnology, Faculty of Engineering, Fukui University

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Other Title
  • Action of Cellulase on β-1,4-Glucosidic Bonds in Acetylcellulose Molecules
  • Action of Cellulase on ベータ 1 4 Glucosid

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Abstract

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.

Journal

  • Sen'i Gakkaishi

    Sen'i Gakkaishi 54 (3), 134-141, 1998

    The Society of Fiber Science and Technology, Japan

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