Milk lactate determination with a rotating bioreactor based on an electron transfer mediated by osmium complexes incorporating a continuous-flow/stopped-flow system Torriero, Angel A. J., Salinas, Eloy, Battaglini, Fernando and Raba, Julio 2003, Milk lactate determination with a rotating bioreactor based on an electron transfer mediated by osmium complexes incorporating a continuous-flow/stopped-flow system, Analytica chimica acta, vol. 498, no. 1-2, pp. 155-163, doi: 10.1016/S0003-2670(03)00897-3. Attached Files Name Description MIMEType Size Downloads Title Milk lactate determination with a rotating bioreactor based on an electron transfer mediated by osmium complexes incorporating a continuous-flow/stopped-flow system Author(s) Torriero, Angel A. J. orcid.org/0000-0001-8616-365X Salinas, Eloy Battaglini, Fernando Raba, Julio Journal name Analytica chimica acta Volume number 498 Issue number 1-2 Start page 155 End page 163 Total pages 9 Publisher Elsevier BV Place of publication Amsterdam, The Netherlands Publication date 2003-11-28 ISSN 0003-2670 1873-4324 0924-2031 Keyword(s) milk lactate lactate oxidase horseradish peroxidase osmium bioreactor flow system iosensors Summary The high sensitivity that can be attained using a bienzymatic system and mediated by the redox polymer [Os(bpy)2ClPyCH2NHpoly(allylamine)] (Os-PAA), has been verified by on-line interfacing of a rotating bioreactor and continuous-flow/stopped-flow/continuous-flow processing. When the hydrogen peroxide formed by LOx layer reaches the inner layer, the electronic flow between the immobilized peroxidase and the electrode surface produces a current, proportional to lactate concentration. The determination of lactate was possible with a limit of detection of 5 nmol l−1 in the processing of as many as 30 samples per hour. This arrangement allows working in undiluted milk samples with a good stability and reproducibility. Horseradish peroxidase [EC 1.11.1.7] and Os-PAA were covalently immobilized on the glassy carbon electrode surface (upper cell body), lactate oxidase [EC 1.1.3.x] was immobilized on a disk that can be rotated. Language eng DOI 10.1016/S0003-2670(03)00897-3 Field of Research 030107 Sensor Technology (Chemical aspects) 030102 Electroanalytical Chemistry Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences HERDC Research category C1.1 Refereed article in a scholarly journal Copyright notice ©2003, Elsevier B.V. Persistent URL http://hdl.handle.net/10536/DRO/DU:30038940 Document type: Journal Article Collections: Centre for Material and Fibre Innovation GTP Research Related Links Link Description Connect to published version (restricted access) Go to link with your DU access privileges     Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved. Versions Version Filter Type Mon, 24 Oct 2011, 07:52:41 EST Mon, 23 Jul 2012, 10:34:24 EST Mon, 23 Jul 2012, 10:36:39 EST Filtered Full Citation counts:   Cited 17 times in TR Web of Science Cited 17 times in Scopus Search Google Scholar Access Statistics: 434 Abstract Views, 0 File Downloads  -  Detailed Statistics Created: Mon, 24 Oct 2011, 07:52:41 EST

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