Cloning and biochemical characterization of a glucosidase from a marine bacterium Aeromonas sp. HC11e-3.
World J Microbiol Biotechnol
; 28(12): 3337-44, 2012 Dec.
Article
em En
| MEDLINE
| ID: mdl-22914897
ABSTRACT
By constructing the genomic library, a ß-glucosidase gene, with a length of 2,382 bp, encoding 793 amino acids, designated bgla, is cloned from a marine bacterium Aeromonas sp. HC11e-3. The enzyme is expressed successfully in the recombinant host Escherichia coli BL21 (DE3) and purified using glutathione affinity purification system. It shows the optimal activity at pH 6, 55 °C and hydrolyzes aryl-glucoside specially. Ca(2+), Mn(2+), Zn(2+), Ba(2+), Pb(2+), Sr(2+) can activate the enzyme activity, whereas SDS, EDTA, DTT show slight inhibition to the enzyme activity. Homologous comparing shows that the enzyme belongs to glycosyl hydrolase family 3, exhibiting 46 % identity with a fully characterized glucosidase from Thermotoga neapolitana DSM 4359. Such results provide useful references for investigating other glucosidases in the glycosyl family 3 as well as developing glucosidases using in suitable industrial area.
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1
Base de dados:
MEDLINE
Assunto principal:
Aeromonas
/
Glucosidases
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article