Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8335522 | International Journal of Biological Macromolecules | 2011 | 5 Pages |
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 (2,2â²-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), guaiacol, o-dianisidine and o-phenylenediamine). The turnover number (r) of H2O2 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.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Nazaret Hidalgo Cuadrado, Galina G. Zhadan, Manuel G. Roig, Valery L. Shnyrov,