Milk lactate determination with a rotating bioreactor based on an electron transfer mediated by osmium complexes incorporating a continuous-flow/stopped- flow system
The high sensitivity that can be attained using a bienzymatic system and mediated by the redox polymer [Os(bpy)2 ClPyCH2NHpoly(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 perox...
| Authors: | , , , |
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| Format: | article |
| Status: | Published version |
| Publication Date: | 2003 |
| Country: | Argentina |
| Institution: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repository: | CONICET Digital (CONICET) |
| Language: | English |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/97973 |
| Online Access: | http://hdl.handle.net/11336/97973 |
| Access Level: | Open access |
| Keyword: | BIOREACTOR BIOSENSORS FLOW SYSTEM HORSERADISH PEROXIDASE LACTATE LACTATE OXIDASE MILK OSMIUM https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
| Summary: | The high sensitivity that can be attained using a bienzymatic system and mediated by the redox polymer [Os(bpy)2 ClPyCH2NHpoly(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 5nmoll -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. |
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