A novel, thermostable manganese-containing superoxide dismutase from Bacillus licheniformis

Biotechnol Lett. 2010 Dec;32(12):1893-6. doi: 10.1007/s10529-010-0368-8. Epub 2010 Aug 12.

Abstract

A new, thermostable superoxide dismutase (SOD) from Bacillus licheniformis M20, isolated from Bulgarian mineral springs, was purified 11-fold with 11% recovery of activity. From native PAGE and SDS-PAGE, the enzyme was composed of two subunits of 21.5 kDa each. The SOD was inhibited only by NaN(3), which suggested that this SOD is of the manganese superoxide dismutase type. The purified enzyme had maximum activity at pH 8 and 55°C. The half-life of the SOD was 10 min at 95°C.

MeSH terms

  • Bacillus / enzymology*
  • Bacillus / isolation & purification
  • Bulgaria
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Inhibitors / metabolism
  • Enzyme Stability
  • Half-Life
  • Hot Springs / microbiology*
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Molecular Weight
  • Protein Subunits / chemistry
  • Protein Subunits / isolation & purification
  • Sodium Azide / metabolism
  • Superoxide Dismutase / chemistry
  • Superoxide Dismutase / isolation & purification*
  • Superoxide Dismutase / metabolism*

Substances

  • Enzyme Inhibitors
  • Protein Subunits
  • Sodium Azide
  • Superoxide Dismutase