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Updated: Mar 30, 2026

Determination of the Glycogen Content in Cyanobacteria
Published on: July 17, 2017
A cold-adapted and glucose-stimulated type II α-glucosidase from a deep-sea bacterium Pseudoalteromonas sp. K8
Wei Li1,2, Yi Xue1,2, Jingjing Li1,2
1School of Life Sciences, Anhui University, Hefei, 230601, Anhui, China.
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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