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^*
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.
繊維学会誌 54(3), 134-141, 1998-03-10
The Society of Fiber Science and Technology, Japan