Characterization of a new oligoalginate lyase from marine bacterium Vibrio sp

Int J Biol Macromol. 2018 Jun:112:937-942. doi: 10.1016/j.ijbiomac.2018.02.046. Epub 2018 Feb 9.

Abstract

A new oligoalginate lyase encoding gene, designed oal17A, was cloned from marine bacterium Vibrio sp. W13, and then expressed in Escherichia coli. The recombinant Oal17A was purified by NTA-Ni resin with maximal activity at 30°C and pH7.0. Oal17A exhibited broad substrate specificity, and preferred to degrade alginate than polyM or polyG into monosaccharide acid. The specific activity of Oal17A toward alginate, polyM and polyG was 21.14U/mg, 12.31U/mg and 7.43U/mg, respectively. With features of high-level expression and broad substrate specificity, Oal17A would be a potential tool for alginate monomer production process of alginate utilizing for biofuels and bioethanol production.

Keywords: Alginate; Monosaccharide; Oligoalginate lyase.

MeSH terms

  • Amino Acid Sequence
  • Aquatic Organisms / enzymology*
  • Computer Simulation
  • Ions
  • Metals / pharmacology
  • Polysaccharide-Lyases / chemistry
  • Polysaccharide-Lyases / genetics
  • Polysaccharide-Lyases / isolation & purification
  • Polysaccharide-Lyases / metabolism*
  • Protein Structure, Tertiary
  • Proteolysis / drug effects
  • Recombinant Proteins / metabolism
  • Substrate Specificity
  • Vibrio / enzymology*
  • Vibrio / genetics

Substances

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