抄録
○The hydrolysis reaction of cellulose substrates by Trichoderma viride cellulases were
investigated by analyzing the substrate binding of cellulase activities, the amount of sugar
produced, and the degree of polymerization of substrates using untreated, NaOH-treated,
and CADOXEN reagent treated substrates. Avicelase and CMCase adsorbed heavily on the
cellulose surface in the early stages of the reaction and then partially desorbed, but
cellobiase did not adsorb to cellulose. Cellobiose was first produced as the product sugar,
then converted to glucose, and finally most of it became glucose. The degree of
polymerization of cellulose changed little during the reaction. In summary, it was found
that Avicelase and CMCase bind to the cellulose surface to change it to an amorphous state,
CMCase cleaves the amorphous region in the endo type, Avicelase cleaves the cleaved end
in the exo type to release cellobiose, and cellobiase converts its cellobiose to glucose. The
findings of this study will provide useful guidelines for establishing optimal conditions for
practical glucose production using cellulase from cellulosic feedstocks.
