Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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A New Extremely Halophilic, Calcium-Independent and Surfactant-Resistant Alpha-Amylase from Alkalibacterium sp. SL3

  • Wang, Guozeng (College of Biological Science and Engineering, Fuzhou University) ;
  • Luo, Meng (College of Biological Science and Engineering, Fuzhou University) ;
  • Lin, Juan (College of Biological Science and Engineering, Fuzhou University) ;
  • Lin, Yun (College of Biological Science and Engineering, Fuzhou University) ;
  • Yan, Renxiang (College of Biological Science and Engineering, Fuzhou University) ;
  • Streit, Wolfgang R. (Department of Microbiology and Biotechnology, Biocenter Klein Flottbek, University of Hamburg) ;
  • Ye, Xiuyun (College of Biological Science and Engineering, Fuzhou University)
  • Received : 2019.01.17
  • Accepted : 2019.04.04
  • Published : 2019.05.28
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Abstract

A new ${\alpha}$-amylase-encoding gene (amySL3) of glycoside hydrolase (GH) family 13 was identified in soda lake isolate Alkalibacterium sp. SL3. The deduced AmySL3 shares high identities (82-98%) with putative ${\alpha}$-amylases from the genus Alkalibacterium, but has low identities (<53%) with functionally characterized counterparts. amySL3 was successfully expressed in Escherichia coli, and the recombinant enzyme (rAmySL3) was purified to electrophoretic homogeneity. The optimal temperature and pH of the activity of the purified rAmySL3 were determined to be $45^{\circ}C$ and pH 7.5, respectively. rAmySL3 was found to be extremely halophilic, showing maximal enzyme activity at a nearly saturated concentration of NaCl. Its thermostability was greatly enhanced in the presence of 4 M NaCl, and it was highly stable in 5 M NaCl. Moreover, the enzyme did not require calcium ions for activity, and was strongly resistant to a range of surfactants and hydrophobic organic solvents. The major hydrolysis products of rAmySL3 from soluble starch were maltobiose and maltotriose. The high ratio of acidic amino acids and highly negative electrostatic potential surface might account for the halophilic nature of AmySL3. The extremely halophilic, calcium-independent, and surfactant-resistant properties make AmySL3 a promising candidate enzyme for both basic research and industrial applications.

Keywords

References

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