Papain digestion of crude Trichoderma reesei cellulase: Purification and properties of cellobiohydrolase I and II core proteins
Papain digestion of a crude Trichoderma reesei cellulose preparation followed by gel filtration on a Superdex column resulted in the separation of cellobiohydrolase (CBH) I and II core proteins (cp). They were further purified to apparent homogeneity by chromatofocusing. N-terminal protein sequencing of the CBH II cp preparation confirmed its identity. A comparison of the catalytic activity and cellulose-binding ability of these core proteins was made. The major differences between them were the findings that CBH II cp possessed a sixfold higher specific activity toward p-nitrophenylcellobioside than the native CBH II preparation and still bound to microcrystalline cellulose, unlike CBH I cp. Neither CBH I cp nor CBH II cp had activity toward carboxymethylcellulose, but both were able to hydrolyze barley b-glucan. These data suggest that removal of the cellulose-binding domain and hinge region from CBH I and II have different effects on their properties.
- Research Organization:
- Oak Ridge National Lab., TN (United States)
- Sponsoring Organization:
- USDOE; USDOE, Washington, DC (United States)
- DOE Contract Number:
- AC05-84OR21400
- OSTI ID:
- 6910310
- Report Number(s):
- CONF-9210197-1; ON: DE93002423
- Resource Relation:
- Conference: Department of Energy (DOE) ethanol from biomass annual review meeting, Golden, CO (United States), 28-29 Oct 1992
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
CELLULASE
FRACTIONATION
ENZYME ACTIVITY
GEL PERMEATION CHROMATOGRAPHY
PAPAIN
TRICHODERMA VIRIDE
CHROMATOGRAPHY
ENZYMES
EUMYCOTA
FUNGI
GLYCOSYL HYDROLASES
HYDROLASES
O-GLYCOSYL HYDROLASES
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PLANTS
PROTEINS
SEPARATION PROCESSES
SH-PROTEINASES
TRICHODERMA
090900* - Biomass Fuels- Processing- (1990-)
550200 - Biochemistry