Effect of milk proteins on the behavior of a biosensor based on poly(allylamine) containing an osmium complex wired to redox enzymes: Part 1. Monoenzymatic configuration
The characterization of a biosensor based on poly(allylamine) containing an osmium complex (OsPAA) in a matrix of industrial relevance, like milk, is presented. The biosensor is constructed by crosslinking an oxidase and the redox polymer (OsPAA) with poly(ethylene diglycidyl) ether (PEG). Parameter...
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todo:paper_00220728_v511_n1-2_p1_Corton2023-10-03T14:25:49Z Effect of milk proteins on the behavior of a biosensor based on poly(allylamine) containing an osmium complex wired to redox enzymes: Part 1. Monoenzymatic configuration Cortón, E. Battaglini, F. Biosensors Chronoamperometry Cyclic voltammetry Flow injection analysis Redox enzymes Crosslinking Cyclic voltammetry Electrochemical electrodes Enzymes Ionic strength Osmium compounds pH effects Polyethers Proteins Redox reactions Thermal effects Buffer solutions Biosensors The characterization of a biosensor based on poly(allylamine) containing an osmium complex (OsPAA) in a matrix of industrial relevance, like milk, is presented. The biosensor is constructed by crosslinking an oxidase and the redox polymer (OsPAA) with poly(ethylene diglycidyl) ether (PEG). Parameters such as the optimum crosslinker concentration, working pH and temperature, and the effect of ionic strength were examined. When the electrode was immersed in milk spiked with substrate, an important decrease in the amperometric signal was observed compared with the one observed in a buffer solution at pH 7.0. The effects of different components of the milk are presented. The decay in the catalytic current is mainly due to the caseins, which insulate the osmium complex from the redox center of the oxidase. © 2001 Elsevier Science B.V. Fil:Cortón, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Battaglini, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00220728_v511_n1-2_p1_Corton |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Biosensors Chronoamperometry Cyclic voltammetry Flow injection analysis Redox enzymes Crosslinking Cyclic voltammetry Electrochemical electrodes Enzymes Ionic strength Osmium compounds pH effects Polyethers Proteins Redox reactions Thermal effects Buffer solutions Biosensors |
spellingShingle |
Biosensors Chronoamperometry Cyclic voltammetry Flow injection analysis Redox enzymes Crosslinking Cyclic voltammetry Electrochemical electrodes Enzymes Ionic strength Osmium compounds pH effects Polyethers Proteins Redox reactions Thermal effects Buffer solutions Biosensors Cortón, E. Battaglini, F. Effect of milk proteins on the behavior of a biosensor based on poly(allylamine) containing an osmium complex wired to redox enzymes: Part 1. Monoenzymatic configuration |
topic_facet |
Biosensors Chronoamperometry Cyclic voltammetry Flow injection analysis Redox enzymes Crosslinking Cyclic voltammetry Electrochemical electrodes Enzymes Ionic strength Osmium compounds pH effects Polyethers Proteins Redox reactions Thermal effects Buffer solutions Biosensors |
description |
The characterization of a biosensor based on poly(allylamine) containing an osmium complex (OsPAA) in a matrix of industrial relevance, like milk, is presented. The biosensor is constructed by crosslinking an oxidase and the redox polymer (OsPAA) with poly(ethylene diglycidyl) ether (PEG). Parameters such as the optimum crosslinker concentration, working pH and temperature, and the effect of ionic strength were examined. When the electrode was immersed in milk spiked with substrate, an important decrease in the amperometric signal was observed compared with the one observed in a buffer solution at pH 7.0. The effects of different components of the milk are presented. The decay in the catalytic current is mainly due to the caseins, which insulate the osmium complex from the redox center of the oxidase. © 2001 Elsevier Science B.V. |
format |
JOUR |
author |
Cortón, E. Battaglini, F. |
author_facet |
Cortón, E. Battaglini, F. |
author_sort |
Cortón, E. |
title |
Effect of milk proteins on the behavior of a biosensor based on poly(allylamine) containing an osmium complex wired to redox enzymes: Part 1. Monoenzymatic configuration |
title_short |
Effect of milk proteins on the behavior of a biosensor based on poly(allylamine) containing an osmium complex wired to redox enzymes: Part 1. Monoenzymatic configuration |
title_full |
Effect of milk proteins on the behavior of a biosensor based on poly(allylamine) containing an osmium complex wired to redox enzymes: Part 1. Monoenzymatic configuration |
title_fullStr |
Effect of milk proteins on the behavior of a biosensor based on poly(allylamine) containing an osmium complex wired to redox enzymes: Part 1. Monoenzymatic configuration |
title_full_unstemmed |
Effect of milk proteins on the behavior of a biosensor based on poly(allylamine) containing an osmium complex wired to redox enzymes: Part 1. Monoenzymatic configuration |
title_sort |
effect of milk proteins on the behavior of a biosensor based on poly(allylamine) containing an osmium complex wired to redox enzymes: part 1. monoenzymatic configuration |
url |
http://hdl.handle.net/20.500.12110/paper_00220728_v511_n1-2_p1_Corton |
work_keys_str_mv |
AT cortone effectofmilkproteinsonthebehaviorofabiosensorbasedonpolyallylaminecontaininganosmiumcomplexwiredtoredoxenzymespart1monoenzymaticconfiguration AT battaglinif effectofmilkproteinsonthebehaviorofabiosensorbasedonpolyallylaminecontaininganosmiumcomplexwiredtoredoxenzymespart1monoenzymaticconfiguration |
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1807322152637038592 |