Purification and Characterization of a New Alginate Lyase from Marine Bacterium Vibrio sp. SY08

Mar Drugs. 2016 Dec 23;15(1):1. doi: 10.3390/md15010001.

Abstract

Unsaturated alginate disaccharides (UADs), enzymatically derived from the degradation of alginate polymers, are considered powerful antioxidants. In this study, a new high UAD-producing alginate lyase, AlySY08, has been purified from the marine bacterium Vibrio sp. SY08. AlySY08, with a molecular weight of about 33 kDa and a specific activity of 1070.2 U/mg, showed the highest activity at 40 °C in phosphate buffer at pH 7.6. The enzyme was stable over a broad pH range (6.0-9.0) and retained about 75% activity after incubation at 40 °C for 2 h. Moreover, the enzyme was active in the absence of salt ions and its activity was enhanced by the addition of NaCl and KCl. AlySY08 resulted in an endo-type alginate lyase that degrades both polyM and polyG blocks, yielding UADs as the main product (81.4% of total products). All these features made AlySY08 a promising candidate for industrial applications in the production of antioxidants from alginate polysaccharides.

Keywords: Vibrio sp.; alginate lyase; thermostability; unsaturated alginate disaccharides.

MeSH terms

  • Alginates / chemistry*
  • Aquatic Organisms / chemistry*
  • Enzyme Stability
  • Glucuronic Acid / chemistry
  • Hexuronic Acids / chemistry
  • Hydrogen-Ion Concentration
  • Molecular Weight
  • Polysaccharide-Lyases / chemistry*
  • Sodium Chloride / chemistry
  • Substrate Specificity
  • Temperature
  • Vibrio / chemistry*

Substances

  • Alginates
  • Hexuronic Acids
  • Sodium Chloride
  • Glucuronic Acid
  • Polysaccharide-Lyases
  • poly(beta-D-mannuronate) lyase