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Identification of a halophilic α-amylase gene from Escherichia coli JM109 and characterization of the recombinant enzyme

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Abstract

A halophilic α-amylase (EAMY) gene from Escherichia coli JM109 was overexpressed in E. coli XL10-Gold and the recombinant protein was purified and characterized. The activity of the EAMY depended on the presence of both Na+ and Cl−, and had maximum activity in 2 M NaCl at 55 °C and pH 7.0. When 2 % (w/v) soluble starch was used as substrate, the specific activity was about 1,090 U mg−1 protein. This is the first report on identifying a halophilic α-amylase with high specific activity from non-halophilic bacteria.

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Acknowledgments

This work was supported by the National Natural Science Foundation of China (Grant no. 31160311), Science and Technology Development Project of Guangxi (Contract no. 11107008-3) and the Natural Science Foundation of Guangxi (Contract no. 2012GXNSFAA053051).

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Authors and Affiliations

  1. State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, Guangxi University, 100 Daxue Road, Nanning, 530004, Guangxi, China

    Yutuo Wei, Xiaobo Wang, Jiayuan Liang, Xue Li, Liqin Du & Ribo Huang

  2. National Engineering Research Center for Non-Food Biorefinery, Guangxi Academy of Sciences, 98 Daling Road, Nanning, 530007, Guangxi, China

    Ribo Huang

  3. Guangxi Biotechnology Research Center, Guangxi Academy of Sciences, 98 Daling Road, Nanning, 530007, Guangxi, China

    Ribo Huang

Authors
  1. Yutuo Wei
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  2. Xiaobo Wang
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  3. Jiayuan Liang
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  4. Xue Li
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  5. Liqin Du
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  6. Ribo Huang
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Corresponding author

Correspondence to Ribo Huang.

Additional information

Yutuo Wei and Xiaobo Wang contributed equally to this study.

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Wei, Y., Wang, X., Liang, J. et al. Identification of a halophilic α-amylase gene from Escherichia coli JM109 and characterization of the recombinant enzyme. Biotechnol Lett 35, 1061–1065 (2013). https://doi.org/10.1007/s10529-013-1175-9

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  • DOI: https://doi.org/10.1007/s10529-013-1175-9

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