Abstract
In order to understand the reaction of cellulose saccharification by Trichoderma
viride cellulase at a more practical level, we tested the effects of the coexistence of
cellobiose and glucose as product sugars, lignin present in cellulosic substrate materials, or
proteins capable of stabilizing the enzyme, in the saccharification system of cellulose. When
the product sugar (cellobiose or glucose) was present at a concentration of 20 mg/mL,
cellulose saccharification was reduced to 60-65%. At a concentration of 50 mg/mL of glucose,
the saccharification reaction apparently ceased to proceed. When lignin was present at a
concentration of 25 mg/mL, cellobiase activity was adsorbed by the lignin and reduced to
about 50%. Thus, glucose production was suppressed to about 20%. On the other hand,
when protein was present at a concentration of 1 mg/mL in addition to cellulase, the
production of soluble sugars increased by about 50%. This effect of the coexisting protein
may be the result of increased stability of Avicelase activity to shaking and heat. The
findings of this study will provide useful guidelines for establishing suitable conditions for
practical glucose production from cellulosic materials using cellulase.