To express and characterize a putative alpha-glucosidase, Pagl, from Pseudoalteromonas sp. K8 obtained via genome mining approach. Pagl was expressed and purified to homogeneity, with a molecular mass of 60 kDa. It was optimally active at pH 8.5 and 30 A degrees C, and showed cold-adapted activity. Pagl exhibited specific activity towards substrates with alpha-1,4-linkage, with the highest specific activity of 19.4 U/mg for maltose, followed by pNP alpha G and maltodextrins, suggesting that Pagl belongs to the type II alpha-glucosidase. Interestingly, the activity of Pagl is significantly enhanced (2.7 times) in the presence of 200 mM glucose. The unique catalytic properties of Pagl make it an attractive candidate for several industrial applications.