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Numrering	Referens	Omslagsbild	Hitta
1.	Alpeeva, IS, et al. (författare) Bi-enzyme alcohol biosensors based on genetically engineered alcohol oxidase and different peroxidases 2005 Ingår i: Microchimica Acta. - : Springer Science and Business Media LLC. - 1436-5073 .- 0026-3672. ; 152:1-2, s. 21-27 Tidskriftsartikel (refereegranskat)abstract We report on the development of a bi-layer bi-enzyme biosensor architecture using different peroxidases and alcohol oxidase from Hansenula polymorpha C-105 as biological recognition elements. The sensor architecture comprises a first layer containing either horseradish peroxidase or royal palm tree peroxidase crosslinked with an Osmium complex-modified redox hydrogel. On top, a second layer was formed by electrochemically induced precipitation of a cathodic electrodeposition paint simultaneously entrapping alcohol oxidase isolated from a genetically modified strain of Hansenula polymorpha C-105. The sensor architecture was optimized with respect to effective electron transfer and stability of the enzyme. The main characteristics of the biosensors are an apparent maximal current I-max(app) of 572-940 nA, an apparent Michaelis constant K-M(app) of 9.5 mM, a sensitivity of 60-98 nA mM(-1) and an improved operational stability represented by a deactivation constant of 1.5-2.0 x 10(-4) min(-1).

Alpeeva, IS, et al. (författare)
Bi-enzyme alcohol biosensors based on genetically engineered alcohol oxidase and different peroxidases
2005
Ingår i: Microchimica Acta. - : Springer Science and Business Media LLC. - 1436-5073 .- 0026-3672. ; 152:1-2, s. 21-27
Tidskriftsartikel (refereegranskat)abstract
- We report on the development of a bi-layer bi-enzyme biosensor architecture using different peroxidases and alcohol oxidase from Hansenula polymorpha C-105 as biological recognition elements. The sensor architecture comprises a first layer containing either horseradish peroxidase or royal palm tree peroxidase crosslinked with an Osmium complex-modified redox hydrogel. On top, a second layer was formed by electrochemically induced precipitation of a cathodic electrodeposition paint simultaneously entrapping alcohol oxidase isolated from a genetically modified strain of Hansenula polymorpha C-105. The sensor architecture was optimized with respect to effective electron transfer and stability of the enzyme. The main characteristics of the biosensors are an apparent maximal current I-max(app) of 572-940 nA, an apparent Michaelis constant K-M(app) of 9.5 mM, a sensitivity of 60-98 nA mM(-1) and an improved operational stability represented by a deactivation constant of 1.5-2.0 x 10(-4) min(-1).

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