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World J Microbiol Biotechnol. 2012 Dec;28(12):3337-44. doi: 10.1007/s11274-012-1145-8. Epub 2012 Aug 23.

Cloning and biochemical characterization of a glucosidase from a marine bacterium Aeromonas sp. HC11e-3.

Author information

1
State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, 430070, People's Republic of China.

Abstract

By constructing the genomic library, a β-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.

PMID:
22914897
DOI:
10.1007/s11274-012-1145-8
[Indexed for MEDLINE]

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