A beta-1,4-endoglucanase-encoding gene from Cellulomonas pachnodae.
Appl Microbiol Biotechnol
; 52(2): 232-9, 1999 Aug.
Article
in En
| MEDLINE
| ID: mdl-10499263
ABSTRACT
A gene library of Cellulomonas pachnodae was constructed in Escherichia coli and was screened for endoglucanase activity. Five endoglucanase-positive clones were isolated that carried identical DNA fragments. The gene, designated cel6A, encoding an endoglucanase enzyme, belongs to the glycosyl hydrolase family 6 (cellulase family B). The recombinant Cel6A had a molecular mass of 53 kDa, a pH optimum of 5.5, and a temperature optimum of 50-55 degrees C. The recombinant endoglucanase Cel6A bound to crystalline cellulose and beech litter. Based on amino acid sequence similarity, a clear cellulose-binding domain was not distinguished. However, the regions in the Cel6A amino acid sequence at the positions 262-319 and 448-473, which did not show similarity to any of the known family-6 glycosyl hydrolases, may be involved in substrate binding.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Cellulase
/
Gram-Positive Asporogenous Rods, Irregular
/
Genes, Bacterial
Limits:
Animals
Language:
En
Journal:
Appl Microbiol Biotechnol
Year:
1999
Document type:
Article
Affiliation country:
Netherlands