Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Papain digestion of crude Trichoderma reesei cellulase: Purification and properties of cellobiohydrolase I and II core proteins

Conference ·
OSTI ID:10102448
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, Washington, DC (United States)
DOE Contract Number:
AC05-84OR21400
OSTI ID:
10102448
Report Number(s):
CONF-9210197--1; ON: DE93002423
Country of Publication:
United States
Language:
English