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Hydrolysis of cellulose by purified cellulase components: Synergistic effects

Conference ·
OSTI ID:6049919
;
The hydrolysis of cellulose by purified cellulase components is reported. 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 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 (50% saturation) concentrations of cellulase components alone and in combination with each other, and it was found that the greatest amount of synergism between them was observed when Avicel was incubated with non-saturating concentrations of enzyme. Synergism was observed between CBH I and CBH II, as well as between EG I and CBH I; however, inhibition of hydrolysis occurred using a combination of EG I and EG II. Synergism between cellulase components may be significant during cellulose hydrolysis only when non-saturating enzyme concentrations are used. 4 refs., 3 figs.
Research Organization:
Oak Ridge National Lab., TN (USA)
DOE Contract Number:
AC05-84OR21400
OSTI ID:
6049919
Report Number(s):
CONF-8710145-1; ON: DE87014954
Country of Publication:
United States
Language:
English

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59 BASIC BIOLOGICAL SCIENCES
ALDEHYDES
BIOCHEMICAL REACTION KINETICS
CARBOHYDRATES
CELLULASE
CHEMICAL REACTIONS
DECOMPOSITION
ENZYME ACTIVITY
ENZYMES
GLUCOSE
GLYCOSYL HYDROLASES
HEXOSES
HYDROLASES
HYDROLYSIS
IMMOBILIZED ENZYMES
KINETICS
LYSIS
MONOSACCHARIDES
O-GLYCOSYL HYDROLASES
ORGANIC COMPOUNDS
REACTION KINETICS
SACCHARIDES
SACCHARIFICATION
SOLVOLYSIS