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. Ca2+, Mn2+, Zn2+, Ba2+, Pb2+, Sr2+ 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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This work was supported by grants from the National Natural Science Foundation of China (NO.u1170303) and the open project of state key laboratory of Huazhong Agricultrual University (ALM0810).
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Xiaoluo Huang and Yan Zhao contribute equally to the work.
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Huang, X., Zhao, Y., Dai, Y. et al. Cloning and biochemical characterization of a glucosidase from a marine bacterium Aeromonas sp. HC11e-3. World J Microbiol Biotechnol 28, 3337–3344 (2012). https://doi.org/10.1007/s11274-012-1145-8
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DOI: https://doi.org/10.1007/s11274-012-1145-8