Back to Search
Start Over
Hyperthermostable endoglucanase from Pyrococcus horikoshii.
- Source :
-
Applied and environmental microbiology [Appl Environ Microbiol] 2002 Jan; Vol. 68 (1), pp. 430-3. - Publication Year :
- 2002
-
Abstract
- An endoglucanase homolog from the hyperthermophilic archaeon Pyrococcus horikoshii was expressed in Escherichia coli, and its enzymatic characteristics were examined. The expressed protein was a hyperthermostable endoglucanase which hydrolyzes celluloses, including Avicel and carboxymethyl cellulose, as well as beta-glucose oligomers. This enzyme is the first endoglucanase belonging to glycosidase family 5 found from Pyrococcus species and is also the first hyperthermostable endoglucanase to which celluloses are the best substrates. This enzyme is expected to be useful for industrial hydrolysis of cellulose at high temperatures, particularly in biopolishing of cotton products.
- Subjects :
- Amino Acid Sequence
Cellulase genetics
Cellulose metabolism
Enzyme Stability
Escherichia coli enzymology
Escherichia coli genetics
Hot Temperature
Molecular Sequence Data
Pyrococcus genetics
Recombinant Proteins genetics
Recombinant Proteins metabolism
Sequence Analysis, DNA
Cellulase metabolism
Pyrococcus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0099-2240
- Volume :
- 68
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Applied and environmental microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 11772658
- Full Text :
- https://doi.org/10.1128/AEM.68.1.430-433.2002