A cold-adapted and glucose-stimulated type II α-glucosidase from a deep-sea bacterium Pseudoalteromonas sp. K8

Biotechnol Lett. 2016 Feb;38(2):345-9. doi: 10.1007/s10529-015-1987-x. Epub 2015 Nov 13.

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.

Keywords: Cold adapted enzyme; Genome missing; Glucose stimulated enzyme; Pseudoaltemonas; α-Glucosidase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cold Temperature
  • Computational Biology
  • Data Mining
  • Enzyme Activators / metabolism*
  • Enzyme Stability
  • Glucose / metabolism*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Weight
  • Pseudoalteromonas / enzymology*
  • Pseudoalteromonas / isolation & purification
  • Seawater / microbiology
  • Substrate Specificity
  • alpha-Glucosidases / chemistry
  • alpha-Glucosidases / isolation & purification*
  • alpha-Glucosidases / metabolism*

Substances

  • Enzyme Activators
  • alpha-Glucosidases
  • Glucose