Citation

Cuadrado NH, Zhadan GG, Roig MG, Shnyrov VL. Int. J. Biol. Macromol. 2011; 49(5): 1078-1082.

Copyright

(Copyright © 2011, Elsevier Publishing)

DOI

10.1016/j.ijbiomac.2011.09.001

PMID

21925205

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.

Language: en

Keywords

Hydrogen-Ion Concentration; Chromatography; Kinetics; Biotechnology; Oxidation-Reduction; Substrate Specificity; Hydrogen Peroxide; Plant Leaves; Solutions; Electrophoresis, Polyacrylamide Gel; Plant Proteins; Peroxidase; Models, Chemical; Phenylenediamines; Guaiacol; Benzothiazoles; Arecaceae; Dianisidine; Sulfonic Acids