[Isolation and purification of Mn-peroxidase from Azospirillum brasilense Sp245]

Prikl Biokhim Mikrobiol. 2012 Jan-Feb;48(1):23-6.
[Article in Russian]

Abstract

Homogenous Mn-peroxidase of a 26-fold purity grade was isolated from a culture of Azospirillum brasilense Sp245 cultivated on a medium containing 0.1 mM pyrocatechol. The molecular weight of the enzyme is 43 kD as revealed by electrophoresis in SDS-PAAG. It was shown that the use of pyrocatechol and 2,2'-azino-bis(3-ethylbenzotiazoline-6-sulfonate) at concentrations of 0.1 and I mM as inductors increased the Mn-peroxidase activity by a factor of 3.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Azospirillum brasilense* / drug effects
  • Azospirillum brasilense* / enzymology
  • Azospirillum brasilense* / isolation & purification
  • Bacterial Proteins / biosynthesis*
  • Bacterial Proteins / isolation & purification
  • Benzothiazoles / pharmacology
  • Catechols / pharmacology
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Culture Media
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Induction
  • Kinetics
  • Molecular Weight
  • Peroxidases / biosynthesis*
  • Peroxidases / isolation & purification
  • Soil Microbiology*
  • Sulfonic Acids / pharmacology

Substances

  • Bacterial Proteins
  • Benzothiazoles
  • Catechols
  • Culture Media
  • Sulfonic Acids
  • 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid
  • Peroxidases
  • manganese peroxidase
  • catechol