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Abstract
The adsorption of purified cellobiohydrolases (CBH I and II) and endoglucanases (EG I and II) from Trichoderma reesei strain L27 to microcrystalline cellulose (Avicel) has been studied. Scatchard analysis of the adsorption data indicated that Avicel possessed high– and low–affinity binding sites for the cellulase components and gave the maximum amount of each component that bound to Avicel at saturation. Hydrolysis of Avicel was thus carried out by saturating and non–saturating concentrations of purified cellulase components alone and in combination with each other. Synergism between them was greatest when Avicel was incubated with non–saturating concentrations of EG I or EG II with CBH I and CBH II. This finding could lead to a dramatic reduction in the enzyme requirement for cellulose utilization.Cite this article
Woodward, J., Hayes, M. & Lee, N. Hydrolysis of Cellulose by Saturating and Non–Saturating Concentrations of Cellulase: Implications for Synergism. Nat Biotechnol 6, 301–304 (1988). https://doi.org/10.1038/nbt0388-301 