Purification and spectroscopic studies on catechol oxidase from lemon balm (Melissa officinalis)

Annette Rompel (Korresp. Autor*in), Klaudia Bueldt-Karentzopoulos, Christian Molitor, Bernt Krebs

Veröffentlichungen: Beitrag in FachzeitschriftArtikelPeer Reviewed

Abstract

A catechol oxidase from lemon balm (Melissa officinalis) moCO which only catalyzes the oxidation of catechols to quinones without hydroxylating tyrosine was purified. The molecular mass of the M. officinalis enzyme of 39,370 Da was obtained by MALDI mass spectrometry and the isoelectric point was determined to be 3.4. Addition of 2 eq. H2O2 to the enzyme leads to oxy catechol oxidase. In the UV/Vis spectrum two new absorption bands occur at 343 nm (epsilon = 8510 M-1 cm(-1)) and 580 nm (epsilon = 580 M-1 cm(-1)) due to O-2(2-) Cu (II) charge transfer transitions in accordance with the oxy forms of other type 3 copper proteins. The N-terminal sequence has been determined by Edman degradation to NPVQAPELDKCGTAT, exhibiting a proline at the second and sixth position conserved in other polyphenol oxidases.
OriginalspracheEnglisch
Seiten (von - bis)19-23
Seitenumfang5
FachzeitschriftPhytochemistry
Jahrgang81
DOIs
PublikationsstatusVeröffentlicht - 2012

ÖFOS 2012

  • 106034 Phytochemie

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