Characterization of an Alkaline Alginate Lyase with pH-Stable and Thermo-Tolerance Property

Mar Drugs. 2019 May 24;17(5):308. doi: 10.3390/md17050308.

Abstract

Alginate oligosaccharides (AOS) show versatile bioactivities. Although various alginate lyases have been characterized, enzymes with special characteristics are still rare. In this study, a polysaccharide lyase family 7 (PL7) alginate lyase-encoding gene, aly08, was cloned from the marine bacterium Vibrio sp. SY01 and expressed in Escherichia coli. The purified alginate lyase Aly08, with a molecular weight of 35 kDa, showed a specific activity of 841 U/mg at its optimal pH (pH 8.35) and temperature (45 °C). Aly08 showed good pH-stability, as it remained more than 80% of its initial activity in a wide pH range (4.0-10.0). Aly08 was also a thermo-tolerant enzyme that recovered 70.8% of its initial activity following heat shock treatment for 5 min. This study also demonstrated that Aly08 is a polyG-preferred enzyme. Furthermore, Aly08 degraded alginates into disaccharides and trisaccharides in an endo-manner. Its thermo-tolerance and pH-stable properties make Aly08 a good candidate for further applications.

Keywords: Alginate lyase; Endo-manner; Thermo-tolerant; Vibrio sp. SY01; pH-stability.

MeSH terms

  • Aquatic Organisms / enzymology*
  • Aquatic Organisms / genetics
  • Enzyme Stability
  • Escherichia coli / genetics
  • Hydrogen-Ion Concentration
  • Polysaccharide-Lyases / chemistry
  • Polysaccharide-Lyases / genetics
  • Polysaccharide-Lyases / isolation & purification
  • Polysaccharide-Lyases / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Temperature*
  • Vibrio / enzymology*
  • Vibrio / genetics

Substances

  • Recombinant Proteins
  • Polysaccharide-Lyases
  • poly(beta-D-mannuronate) lyase