Immobilized Horseradish Peroxidase as a Reusable Catalyst for Emulsion Polymerization

The study on the adsorption of horseradish peroxidase (HRP) onto silicon wafers was carried out by means of in situ ellipsometry, atomic force microscopy (AFM) and contact angle measurements. A smooth HRP layer adsorbed onto Si wafers. The enzymatic activity of free or adsorbed HRP was determined by...

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Bibliographic Details
Published in:Langmuir 2007-02, Vol.23 (4), p.1981-1987
Main Authors: Naves, Alliny F, Carmona-Ribeiro, Ana M, Petri, Denise F. S
Format: Article
Language:English
Subjects:
Catalysis
Chemistry
Dimerization
Electrochemistry
Emulsions
Enzymes, Immobilized - metabolism
Exact sciences and technology
Free Radicals - chemistry
Free Radicals - metabolism
General and physical chemistry
Horseradish Peroxidase - metabolism
Hydrogen Peroxide - chemistry
Kinetics
Methacrylates - chemistry
Microscopy, Atomic Force
Molecular Structure
Polymers - chemistry
Silicon - chemistry
Surface physical chemistry
Theory of reactions, general kinetics. Catalysis. Nomenclature, chemical documentation, computer chemistry
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Summary:The study on the adsorption of horseradish peroxidase (HRP) onto silicon wafers was carried out by means of in situ ellipsometry, atomic force microscopy (AFM) and contact angle measurements. A smooth HRP layer adsorbed onto Si wafers. The enzymatic activity of free or adsorbed HRP was determined by the oxidation of 2,2‘-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and by the emulsion polymerization of ethylene glycol dimethacrylate (EGDMA). Upon adsorbing, HRP molecules might have undergone some conformational changes, which caused a small reduction of enzymatic activity in comparison to that observed for HRP solution. However, it was possible to reuse the same HRP-covered Si wafer as catalyst in the polymerization of EGDMA three times.
ISSN:0743-7463
1520-5827
DOI:10.1021/la061884o