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Cloning and expression of a β-1,4-endoglucanase gene fromCellulomonassp. CelB7 inEscherichia coli; purification and characterization of the recombinant enzyme
- Source :
- FEMS Microbiology Letters. 145:355-360
- Publication Year :
- 1996
- Publisher :
- Oxford University Press (OUP), 1996.
-
Abstract
- A gene library of a newly isolated Cellulomonas sp. strain was constructed in Escherichia coli and clones were screened for endoglucanase activity using dye-labelled carboxymethylcellulose. Seventeen clones were isolated that carried DNA inserts coding for endoglucanase enzymes. Of the 17 clones, one carrying the gene cegA, was further characterized. The recombinant endoglucanase was purified by FPLC. The endoglucanase was active against carboxymethylcellulose, lichenin and also degraded crystalline cellulose and birchwood xylan. The molecular mass of the enzyme (36 kDa), and its pH (7.4) and temperature (35 degrees C) optima were determined.
- Subjects :
- Restriction Mapping
Lichenin
Cellulase
medicine.disease_cause
Microbiology
Gene Expression Regulation, Enzymologic
Substrate Specificity
law.invention
chemistry.chemical_compound
law
Actinomycetales
Escherichia coli
Genetics
medicine
Genomic library
Cellulomonas
Cloning, Molecular
Molecular Biology
Chromatography, High Pressure Liquid
Gene Library
biology
Molecular mass
beta-Glucosidase
Temperature
Fast protein liquid chromatography
Gene Expression Regulation, Bacterial
Hydrogen-Ion Concentration
biology.organism_classification
Molecular biology
Recombinant Proteins
Molecular Weight
chemistry
Genes, Bacterial
Recombinant DNA
biology.protein
Electrophoresis, Polyacrylamide Gel
Subjects
Details
- ISSN :
- 15746968 and 03781097
- Volume :
- 145
- Database :
- OpenAIRE
- Journal :
- FEMS Microbiology Letters
- Accession number :
- edsair.doi.dedup.....d6bc12950b0e5f21fe63af6e97828c03