Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans

Biotechnol Lett. 2012 Jun;34(6):1087-92. doi: 10.1007/s10529-012-0876-9. Epub 2012 Mar 4.

Abstract

A gene, alg7D, from Saccharophagus degradans, coding for a putative alginate lyase belonging to the family of polysaccharide lyase-7, was overexpressed in Escherichia coli. The properties of the recombinant Alg7D were characterized. The enzyme endolytically depolymerized alginate by β-elimination into oligo-alginates with degrees of polymerization of 2-5. Its activity was maximal at 50°C and pH 7 and was slightly increased in the presence of Na(+). The K(M), V(max), k(cat), and k(cat)/K(M) values were: 3 mg ml(-1), 6.2 U mg(-1), 1.9 × 10(-2) s(-1), and 6.3 × 10(-3) mg(-1 )ml s(-1), respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alginates / metabolism
  • Alteromonadaceae / enzymology*
  • Alteromonadaceae / genetics
  • Enzyme Stability
  • Escherichia coli / genetics
  • Gene Expression
  • Glucuronic Acid / metabolism
  • Hexuronic Acids / metabolism
  • Hydrogen-Ion Concentration
  • Kinetics
  • Oligosaccharides / metabolism
  • Polysaccharide-Lyases / chemistry
  • Polysaccharide-Lyases / genetics*
  • Polysaccharide-Lyases / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Temperature

Substances

  • Alginates
  • Hexuronic Acids
  • Oligosaccharides
  • Recombinant Proteins
  • Glucuronic Acid
  • Polysaccharide-Lyases
  • poly(beta-D-mannuronate) lyase