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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Autores principales: Cortón, E., Battaglini, F.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00220728_v511_n1-2_p1_Corton
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spelling 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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