Direct detection, cloning and characterization of a glucoside hydrolase from forest soil.
Biotechnol Lett
; 37(6): 1227-32, 2015 Jun.
Article
em En
| MEDLINE
| ID: mdl-25700816
ABSTRACT
A glucoside hydrolase gene, egl01, was cloned from the soil DNA of Changbai Mountain forest by homologous PCR amplification. The deduced sequence of 517 amino acids included a catalytic domain of glycoside hydrolase family 5 and was homologous to a putative cellulase from Bacillus licheniformis. The recombinant enzyme, Egl01, was maximally active at pH 5 and 50 °C and it was stable at pH 3-9, 4-50 °C, and also stable in the presence of metal ions, organic solvents, surfactants and salt. Its activity was above 120 % in 2-3 M NaCl/KCl and over 70 % was retained in 1-4 M NaCl/KCl for 6d. Egl01 hydrolyzed carboxymethyl cellulose, beechwood xylan, crop stalk, laminarin, filter paper, and avicel but not pNPG, indicating its broad substrate specificity. These properties make this recombinant enzyme a promising candidate for industrial applications.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Solo
/
Celulase
/
Metagenoma
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Revista:
Biotechnol Lett
Ano de publicação:
2015
Tipo de documento:
Article