Peroxidase-mediated transformation of hydroxy-9,10-anthraquinones

Daniel Arrieta-Baez, Rosa Roman, Rafael Vazquez-Duhalt, Manuel Jiménez-Estrada

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

A peroxidase (EC 1.11.1.7) has been isolated and purified from Senna angustifolia. The enzyme was purified by ion-exchange chromatography on high Q and high S columns. SDS-PAGE electrophoresis showed that the protein has a molecular mass of approximately 70 kDa. Hydroxy-anthraquinones and hydroxy-anthracenones were evaluated as substrate of S. angustifolia and horseradish peroxidases. Both peroxidases catalyzed the oxidation of alizarin and purpurin anthraquinones to the corresponding 3,3′-bializarin and the new compound 3,3′-bipurpurin, respectively, as well as the formation of 2,2′-biquinizarin from quinizarin anthracenone. The KMapp and Vmax values for alizarin and purpurin were 97 and 95 μM and 1.5 and 2.1 μM min-1 mg prot-1, respectively. The results suggest that peroxidase may participate in the biogenesis of anthraquinones.

Original languageEnglish
Pages (from-to)567-572
Number of pages6
JournalPhytochemistry
Volume60
Issue number6
DOIs
StatePublished - 2002
Externally publishedYes

Keywords

  • Anthracenones
  • Bianthraquinones
  • Horseradish peroxidase
  • Kinetic properties
  • Leguminosae
  • Phenolic oxidation
  • Senna angustifolia

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