kappa-Carrageenase from Pseudomonas carrageenovora

Eur J Biochem. 1979 Feb 1;93(3):553-8. doi: 10.1111/j.1432-1033.1979.tb12854.x.

Abstract

A kappa-carrageenase was isolated from the cell-free medium of cultured Pseudomonas carrageenovora. From dodecylsulphate/polyacrylamide gel electrophoresis, a single protein (identified as the kappa-carrageenase) was detected in the medium. Activity against nominal carrageenan types and inspection of the products indicate the enzyme to be a kappa-carrageenase. Purification is described here by ammonium sulphate precipitation and subsequent CM-Sepharose CL-6B ion-exchange chromatography. Molecular weight was estimated as 35,000 by dodecylsulphate/polyacrylamide gel electrophoresis. Products of degradation were analysed by gel filtration, spectrophotometric assays and 13C nuclear magnetic resonance. These results are consistent with the product of limit digest being neocarrabiose 4-O-sulphate.

MeSH terms

  • Carrageenan / metabolism
  • Glycoside Hydrolases / isolation & purification
  • Glycoside Hydrolases / metabolism*
  • Hydrogen-Ion Concentration
  • Molecular Weight
  • Pseudomonas / enzymology*
  • Temperature

Substances

  • Carrageenan
  • Glycoside Hydrolases