Reaction Kinetics, Mechanisms and Catalysis
Volume/Issue:
Volume 105: Issue 1
Oxidation activity of horseradish peroxidase hosted in molecular sieves: spectroscopic investigations show hindering of the enzyme activity
Authors:
Viorel Chihaia
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,
Karl Sohlberg
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Ligia Frunza National Institute of Materials Physics, Magurele, Romania

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Nicoleta Gheorghe National Institute of Materials Physics, Magurele, Romania

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Constantin Paul Ganea National Institute of Materials Physics, Magurele, Romania

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Reinhard Eckelt Leibniz Institute for Catalysis, University of Rostock, Rostock, Germany

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, and
Hendrik Kosslick Leibniz Institute for Catalysis, University of Rostock, Rostock, Germany

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Pages:
195–205
Online Publication Date:
03 Dec 2011
Publication Date:
01 Feb 2012
Article Category:
Research Article
DOI:
https://doi.org/10.1007/s11144-011-0408-y
Keywords:
Horseradish peroxidase; SBA-15; Aerosil; Alizarin Red S; Oxidation by hydrogen peroxide; Support functionalization
Restricted access

Abstract

Horseradish peroxidase immobilization inside molecular sieves with pores hexagonally structured as such or functionalized with copper ions is presented in comparison with the bidimensional immobilization onto aerosil A380 particles. Immobilization was performed under mild conditions that do not lead to enzyme denaturation. Guest–host interactions were pursued spectrophotometrically and by thermal analysis measurements. FTIR spectroscopy showed no major secondary structural change for the entrapped enzyme despite some influence of the support functionalization that can be supposed. The activity of the immobilized enzyme was tested in the oxidation of Alizarin Red S (ARS) with hydrogen peroxide. It was found that the dye oxidation is catalyzed by the enzyme in homogeneous reaction but the rate becomes much slower in heterogeneous catalytic processes with prepared catalysts. It seems that horseradish peroxidase immobilization in simple porous silica or alumino-silica post synthesis blocks the enzyme activity. In addition, copper ions make a stable complex with ARS hindering its oxidation as well.

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Cover Reaction Kinetics, Mechanisms and Catalysis
Reaction Kinetics, Mechanisms and Catalysis
Print ISSN:
1878-5190
Online ISSN:
1878-5204

Reaction Kinetics, Mechanisms and Catalysis
Language English
Size B5
Year of
Foundation		 1974
Volumes
per Year		 1
Issues
per Year		 6
Founder Akadémiai Kiadó
Founder's
Address		 H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address		 H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher		 Chief Executive Officer, Akadémiai Kiadó
ISSN 1878-5190 (Print)
ISSN 1878-5204 (Online)

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