Purification and characterization of a novel alpha-agarase from a Thalassomonas sp

Curr Microbiol. 2005 Apr;50(4):212-6. doi: 10.1007/s00284-004-4435-z. Epub 2005 Mar 15.


An agar-degrading Thalassomonas bacterium, strain JAMB-A33, was isolated from the sediment off Noma Point, Japan, at a depth of 230 m. A novel alpha-agarase from the isolate was purified to homogeneity from cultures containing agar as a carbon source. The molecular mass of the purified enzyme, designated as agaraseA33, was 85 kDa on both SDS-PAGE and gel-filtration chromatography, suggesting that it is a monomer. The optimal pH and temperature for activity were about 8.5 and 45 degrees C, respectively. The enzyme had a specific activity of 40.7 U/mg protein. The pattern of agarose hydrolysis showed that the enzyme is an endo-type alpha-agarase, and the final main product was agarotetraose. The enzyme degraded not only agarose but also agarohexaose, neoagarohexaose, and porphyran.

MeSH terms

  • Gammaproteobacteria / classification
  • Gammaproteobacteria / enzymology*
  • Gammaproteobacteria / growth & development
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / isolation & purification*
  • Glycoside Hydrolases / metabolism
  • Phylogeny


  • Glycoside Hydrolases
  • agarase