Suicide inactivation of peroxidase from Chamaerops excelsa palm tree leaves

Int J Biol Macromol. 2011 Dec 1;49(5):1078-82. doi: 10.1016/j.ijbiomac.2011.09.001. Epub 2011 Sep 8.

Abstract

The concentration and time-dependences and the mechanism of the inactivation of Chamaerops excelsa peroxidase (CEP) by hydrogen peroxide were studied kinetically with four co-substrates (2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), guaiacol, o-dianisidine and o-phenylenediamine). The turnover number (r) of H(2)O(2) required to complete the inactivation of the enzyme varied for the different substrates, the enzyme most resistant to inactivation (r=4844) with ABTS being the most useful substrate for biotechnological applications, opening a new avenue of enquiry with this peroxidase.

MeSH terms

  • Arecaceae / chemistry
  • Arecaceae / enzymology*
  • Benzothiazoles / metabolism
  • Biotechnology / methods*
  • Chromatography
  • Dianisidine / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Guaiacol / metabolism
  • Hydrogen Peroxide / adverse effects*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Models, Chemical
  • Oxidation-Reduction / drug effects
  • Peroxidase / antagonists & inhibitors*
  • Peroxidase / isolation & purification
  • Peroxidase / metabolism
  • Phenylenediamines / metabolism
  • Plant Leaves / chemistry
  • Plant Leaves / enzymology*
  • Plant Proteins / antagonists & inhibitors*
  • Plant Proteins / isolation & purification
  • Plant Proteins / metabolism
  • Solutions
  • Substrate Specificity
  • Sulfonic Acids / metabolism

Substances

  • Benzothiazoles
  • Phenylenediamines
  • Plant Proteins
  • Solutions
  • Sulfonic Acids
  • 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid
  • Guaiacol
  • 1,2-diaminobenzene
  • Hydrogen Peroxide
  • Peroxidase
  • Dianisidine