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.
Copyright © 2011 Elsevier B.V. All rights reserved.
MeSH terms
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Arecaceae / chemistry
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Arecaceae / enzymology*
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Benzothiazoles / metabolism
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Biotechnology / methods*
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Chromatography
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Dianisidine / metabolism
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Electrophoresis, Polyacrylamide Gel
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Guaiacol / metabolism
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Hydrogen Peroxide / adverse effects*
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Hydrogen-Ion Concentration
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Kinetics
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Models, Chemical
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Oxidation-Reduction / drug effects
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Peroxidase / antagonists & inhibitors*
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Peroxidase / isolation & purification
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Peroxidase / metabolism
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Phenylenediamines / metabolism
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Plant Leaves / chemistry
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Plant Leaves / enzymology*
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Plant Proteins / antagonists & inhibitors*
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Plant Proteins / isolation & purification
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Plant Proteins / metabolism
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Solutions
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Substrate Specificity
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Sulfonic Acids / metabolism
Substances
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Benzothiazoles
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Phenylenediamines
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Plant Proteins
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Solutions
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Sulfonic Acids
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2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid
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Guaiacol
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1,2-diaminobenzene
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Hydrogen Peroxide
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Peroxidase
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Dianisidine