2019 ; Vol.29-5: 765~775
|Author||Guozeng Wang, Meng Luo, Juan Lin, Yun Lin, Renxiang Yan, Wolfgang R. Streit, Xiuyun Ye|
|Place of duty||College of Biological Science and Engineering, Fuzhou University, P. R. China,Department of Microbiology and Biotechnology, Biocenter Klein Flottbek, University of Hamburg,Germany|
|Title||A New Extremely Halophilic, Calcium-Independent and Surfactant-Resistant Alpha-Amylase from Alkalibacterium sp. SL3|
J. Microbiol. Biotechnol.2019 ;
|Abstract||A new α-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 α-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°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.|
|Key_word||α-Amylase, glycoside hydrolase family 13, halophilic, surfactant-resistant, calcium-independent, alkalibacterium|
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