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Exoglucanase activities of the recombinant Clostridium thermocellum CelS, a major cellulosome component.
- Source :
-
Journal of bacteriology [J Bacteriol] 1995 Mar; Vol. 177 (6), pp. 1641-4. - Publication Year :
- 1995
-
Abstract
- The recombinant CelS (rCelS), the most abundant catalytic subunit of the Clostridium thermocellum cellulosome, displayed typical exoglucanase characteristics, including (i) a preference for amorphous or crystalline cellulose over carboxymethyl cellulose, (ii) an inability to reduce the viscosity of a carboxymethyl cellulose solution, and (iii) the production of few bound reducing ends on the solid substrate. The hydrolysis products from crystalline cellulose were cellobiose and cellotriose at a ratio of 5:1. The rCelS activity on amorphous cellulose was optimal at 70 degrees C and at pH 5 to 6. Its thermostability was increased by Ca2+. Sulfhydryl reagents had only a mild adverse effect on the rCelS activity. Cellotetraose was the smallest oligosaccharide substrate for rCelS, and the hydrolysis rate increased with the substrate chain length. Many of these properties were consistent with those of the cellulosome, indicating a key role for CelS.
- Subjects :
- Base Sequence
Cellulase drug effects
Cellulase genetics
Cellulose analogs & derivatives
Cellulose chemistry
Clostridium genetics
Clostridium metabolism
Dextrins metabolism
Glucan 1,3-beta-Glucosidase
Hydrolysis
Molecular Sequence Data
Multienzyme Complexes genetics
Multienzyme Complexes metabolism
Recombinant Proteins metabolism
Substrate Specificity
Sulfhydryl Reagents pharmacology
Viscosity
beta-Glucosidase drug effects
beta-Glucosidase genetics
Cellulase metabolism
Cellulose metabolism
Clostridium enzymology
beta-Glucosidase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9193
- Volume :
- 177
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Journal of bacteriology
- Publication Type :
- Academic Journal
- Accession number :
- 7883725
- Full Text :
- https://doi.org/10.1128/jb.177.6.1641-1644.1995