Your browser doesn't support javascript.
loading
Enzyme Immobilization and Mediation with Osmium Redox Polymers.
VandeZande, Gaige R; Olvany, Jasmine M; Rutherford, Julia L; Rasmussen, Michelle.
Afiliación
  • VandeZande GR; Chemistry Department, Lebanon Valley College, 101 N College Avenue, Annville, PA, 17003-1400, USA.
  • Olvany JM; Chemistry Department, Lebanon Valley College, 101 N College Avenue, Annville, PA, 17003-1400, USA.
  • Rutherford JL; Chemistry Department, Lebanon Valley College, 101 N College Avenue, Annville, PA, 17003-1400, USA.
  • Rasmussen M; Chemistry Department, Lebanon Valley College, 101 N College Avenue, Annville, PA, 17003-1400, USA. rasmusse@lvc.edu.
Methods Mol Biol ; 1504: 165-179, 2017.
Article en En | MEDLINE | ID: mdl-27770421
ABSTRACT
Enzymatic electrodes are becoming increasingly common for energy production and sensing applications. Research over the past several decades has addressed a major issue that can occur when using these biocatalysts, i.e., slow heterogeneous electron transfer, by incorporation of a redox active species to act as an electron shuttle. There are several advantages to immobilizing both the enzyme and mediator at the enzyme surface, including increased electron transfer rates, decreased enzyme leaching, and minimized diffusion limitations. Redox polymers consisting of a redox active center attached to a polymer backbone are a particularly attractive option because they have high self-exchange rates for electron transfer and tunable redox potential. Osmium (Os) polymers are the most well studied of this type of polymer for bioelectrocatalysis. Here, we describe the methods to synthesize one of the most common Os redox polymers and how it can be used to fabricate glucose oxidase electrodes. Procedures are also outlined for evaluating the enzymatic electrodes.
Asunto(s)
Palabras clave
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Osmio / Polímeros / Aspergillus niger / 2,2'-Dipiridil / Enzimas Inmovilizadas / Glucosa Oxidasa Idioma: En Revista: Methods Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2017 Tipo del documento: Article País de afiliación: Estados Unidos
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Osmio / Polímeros / Aspergillus niger / 2,2'-Dipiridil / Enzimas Inmovilizadas / Glucosa Oxidasa Idioma: En Revista: Methods Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2017 Tipo del documento: Article País de afiliación: Estados Unidos