Amperometric detection of peroxides using peroxidase and porphyrin biomimetic modified electrodes
Biosensors designed with crosslinked redox hydrogel and horseradish peroxidase have been evaluated in aqueous and nonaqueous media. Electrodes made of a single layer of active material were prepared with Os(byp)2ClPyCH2 NHPoly(allylamine) polymer, (PAA-Os), attached to the enzyme by PEG-400 bifuncti...
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2002
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10400397_v14_n17_p1157_Baldini http://hdl.handle.net/20.500.12110/paper_10400397_v14_n17_p1157_Baldini |
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paper:paper_10400397_v14_n17_p1157_Baldini2025-07-30T18:36:36Z Amperometric detection of peroxides using peroxidase and porphyrin biomimetic modified electrodes Biomimetic Biosensor Enzyme HRP Peroxide Porphyrin lauric acid osmium peroxide polymer porphyrin amperometric biosensor aqueous solution article biomimetics chemical modification cross linking electrode hydrogen bond molecular stability oxidation reduction reaction polymerization quantitative analysis Biosensors designed with crosslinked redox hydrogel and horseradish peroxidase have been evaluated in aqueous and nonaqueous media. Electrodes made of a single layer of active material were prepared with Os(byp)2ClPyCH2 NHPoly(allylamine) polymer, (PAA-Os), attached to the enzyme by PEG-400 bifunctional reagent with the Os sites acting as electron wires. The electrodes proved to be stable in the presence of organic solvent considering the time evolution of the redox charge and the catalytic current. However, a reasonable decrease in the enzyme response is apparent while increasing solvent content in solution for detection of hydrogen and lauroyl peroxide. As an alternative biomimetic strategy, electrodes were modified with consecutive layers of PAA-Os and electropolymerized Fe-protoporphyrin IX. The electrochemical detection of peroxides was also possible with this system, proving that the poly[Fe-protoporphyrin IX]/Osmium complex system can mimic the peroxidase activity towards hydrogen and organic peroxides. The replacement of Fe-protoporphyrin by Ni-protoporphyrin IX and PAA-Os by PAA in different experiments demonstrates that the mechanism for peroxide reduction involves both Os and Fe-protoporphyrin IX sites. The enzymatic electrodes were applied to benzoyl peroxide quantitation in a pharmaceutical product. The method validation demonstrates that a simple and rapid FIA detection can be applied. 2002 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10400397_v14_n17_p1157_Baldini http://hdl.handle.net/20.500.12110/paper_10400397_v14_n17_p1157_Baldini |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Biomimetic Biosensor Enzyme HRP Peroxide Porphyrin lauric acid osmium peroxide polymer porphyrin amperometric biosensor aqueous solution article biomimetics chemical modification cross linking electrode hydrogen bond molecular stability oxidation reduction reaction polymerization quantitative analysis |
| spellingShingle |
Biomimetic Biosensor Enzyme HRP Peroxide Porphyrin lauric acid osmium peroxide polymer porphyrin amperometric biosensor aqueous solution article biomimetics chemical modification cross linking electrode hydrogen bond molecular stability oxidation reduction reaction polymerization quantitative analysis Amperometric detection of peroxides using peroxidase and porphyrin biomimetic modified electrodes |
| topic_facet |
Biomimetic Biosensor Enzyme HRP Peroxide Porphyrin lauric acid osmium peroxide polymer porphyrin amperometric biosensor aqueous solution article biomimetics chemical modification cross linking electrode hydrogen bond molecular stability oxidation reduction reaction polymerization quantitative analysis |
| description |
Biosensors designed with crosslinked redox hydrogel and horseradish peroxidase have been evaluated in aqueous and nonaqueous media. Electrodes made of a single layer of active material were prepared with Os(byp)2ClPyCH2 NHPoly(allylamine) polymer, (PAA-Os), attached to the enzyme by PEG-400 bifunctional reagent with the Os sites acting as electron wires. The electrodes proved to be stable in the presence of organic solvent considering the time evolution of the redox charge and the catalytic current. However, a reasonable decrease in the enzyme response is apparent while increasing solvent content in solution for detection of hydrogen and lauroyl peroxide. As an alternative biomimetic strategy, electrodes were modified with consecutive layers of PAA-Os and electropolymerized Fe-protoporphyrin IX. The electrochemical detection of peroxides was also possible with this system, proving that the poly[Fe-protoporphyrin IX]/Osmium complex system can mimic the peroxidase activity towards hydrogen and organic peroxides. The replacement of Fe-protoporphyrin by Ni-protoporphyrin IX and PAA-Os by PAA in different experiments demonstrates that the mechanism for peroxide reduction involves both Os and Fe-protoporphyrin IX sites. The enzymatic electrodes were applied to benzoyl peroxide quantitation in a pharmaceutical product. The method validation demonstrates that a simple and rapid FIA detection can be applied. |
| title |
Amperometric detection of peroxides using peroxidase and porphyrin biomimetic modified electrodes |
| title_short |
Amperometric detection of peroxides using peroxidase and porphyrin biomimetic modified electrodes |
| title_full |
Amperometric detection of peroxides using peroxidase and porphyrin biomimetic modified electrodes |
| title_fullStr |
Amperometric detection of peroxides using peroxidase and porphyrin biomimetic modified electrodes |
| title_full_unstemmed |
Amperometric detection of peroxides using peroxidase and porphyrin biomimetic modified electrodes |
| title_sort |
amperometric detection of peroxides using peroxidase and porphyrin biomimetic modified electrodes |
| publishDate |
2002 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10400397_v14_n17_p1157_Baldini http://hdl.handle.net/20.500.12110/paper_10400397_v14_n17_p1157_Baldini |
| _version_ |
1840322043542765568 |