Abstract
Objectives
To express and characterize a putative α-glucosidase, Pagl, from Pseudoalteromonas sp. K8 obtained via genome mining approach.
Results
Pagl was expressed and purified to homogeneity, with a molecular mass of 60 kDa. It was optimally active at pH 8.5 and 30 °C, and showed cold-adapted activity. Pagl exhibited specific activity towards substrates with α-1,4-linkage, with the highest specific activity of 19.4 U/mg for maltose, followed by pNPαG and maltodextrins, suggesting that Pagl belongs to the type II α-glucosidase. Interestingly, the activity of Pagl is significantly enhanced (2.7 times) in the presence of 200 mM glucose.
Conclusion
The unique catalytic properties of Pagl make it an attractive candidate for several industrial applications.
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Acknowledgments
This work was supported by Grants from the National Natural Science Foundation of China (31570064); the Natural Science Foundation of the Department of Education of Anhui Province (KJ2015A038); the Key Scientific and Technological project of Anhui Province (1301032154); the Introduction Project of Academic and Technology Leaders in Anhui University (32030066) and the Innovative Research Team Program of 211 Project in Anhui University.
Supporting information
Supplementary Table 1—Primers used in cloning pagl from Pseudoalteromonas sp. K8.
Supplementary Table 2—Effects of cations on Pagl activitya.
Supplementary Fig. 1—Kinetic profile of Pagl under concentrations of glucose.
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Li, W., Xue, Y., Li, J. et al. A cold-adapted and glucose-stimulated type II α-glucosidase from a deep-sea bacterium Pseudoalteromonas sp. K8. Biotechnol Lett 38, 345–349 (2016). https://doi.org/10.1007/s10529-015-1987-x
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DOI: https://doi.org/10.1007/s10529-015-1987-x