Purification and partial characterization of multiple bromoperoxidases from Streptomyces griseus

J Gen Microbiol. 1988 Dec;134(12):3141-9. doi: 10.1099/00221287-134-12-3141.


The presence of multiple bromoperoxidases in extracts of Streptomyces griseus Tü 6 was detected. The enzyme pattern varied with the age of the culture. A haem-type bromoperoxidase (BPO 2) was always present. Additionally three nonhaem-type bromoperoxidases (BPO 1a, 1b and 3) were detected and purified to homogeneity. The Mr of non-denatured BPO 1a was 70,000 +/- 10,000 and those of BPO 1b and 3 were 90,000 +/- 5000. BPO 1a and 1b were dimers with subunit Mr values of 34,000 and 43,000, respectively. BPO 3 was a trimer with a subunit Mr of 31,000. The enzymes differed in their isoelectric points, heat stability, and Km values. In immunodiffusion experiments BPO 1a and 3 showed partial identity with the nonhaem-type bromoperoxidase from Streptomyces aureofaciens. The nonhaem-type BPO 1a, 1b and 3 had neither peroxidase nor catalase activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Chromatography, Ion Exchange
  • Electrophoresis, Polyacrylamide Gel
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Weight
  • Peptide Hydrolases / pharmacology
  • Peroxidases / isolation & purification*
  • Streptomyces griseus / enzymology*
  • Temperature


  • Peroxidases
  • bromide peroxidase
  • Peptide Hydrolases