Recombinant pyranose dehydrogenase-A versatile enzyme possessing both mediated and direct electron transfer

Maria Yakovleva; Aniko Killyeni; Roberto Ortiz; Christopher Schulz; Domhnall MacAodha; Peter O. Conghaile; Donal Leech; Ionel Catalin Popescu; Christoph Gonaus; Clemens K. Peterbauer; Lo Gorton

doi:10.1016/j.elecom.2012.08.029

Recombinant pyranose dehydrogenase-A versatile enzyme possessing both mediated and direct electron transfer

Maria Yakovleva, Aniko Killyeni, Roberto Ortiz, Christopher Schulz, Domhnall MacAodha, Peter O. Conghaile, Donal Leech, Ionel Catalin Popescu, Christoph Gonaus, Clemens K. Peterbauer, Lo Gorton

Research output: Contribution to journal › Article › peer-review

Abstract

The catalytical properties of glycosylated pyranose dehydrogenase (gPDH) and deglycosylated PDH (dgPDH) from Agaricus meleagris recombinantly expressed in Pichia pastoris were studied. Both gPDH and dgPDH were "wired" to an osmium redox polymer on graphite electrodes mounted in a flow-injection system. The current from oxidation of glucose by immobilised gPDH and dgPDH was compared using flow injection amperometry and cyclic voltammetry. An increase in the current density was observed for dgPDH (190 mu A cm(-2)) compared with that for gPDH (90 mu A cm(-2)) due to the improved electron transfer between the active site and the electrode. Additionally, the ability of dgPDH for direct electron transfer (DET) was discovered, which is rather unique among FAD-containing enzymes. The ability to oxidise a variety of sugars at a rather low potential makes dgPDH attractive for construction of biofuel cells with high power output. (C) 2012 Elsevier B.V. All rights reserved.

Original language	English
Pages (from-to)	120-122
Journal	Electrochemistry Communications
Volume	24
DOIs	https://doi.org/10.1016/j.elecom.2012.08.029
Publication status	Published - 2012

Subject classification (UKÄ)

Biological Sciences

Free keywords

Pyranose dehydrogenase
Deglycosylation
Osmium polymer
Direct electron
transfer
Biosensor

Access to Document

10.1016/j.elecom.2012.08.029

1 Doctoral Thesis (compilation)

Improving the biocatalyst. Engineering of fungal oxidoreductases and thin-film electrodes for improvement of membraneless biofuel cells and carbohydrate biosensors.
Ortiz, R., 2013, Department of Chemistry, Lund University. 262 p.
Research output: Thesis › Doctoral Thesis (compilation)

Cite this

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title = "Recombinant pyranose dehydrogenase-A versatile enzyme possessing both mediated and direct electron transfer",

abstract = "The catalytical properties of glycosylated pyranose dehydrogenase (gPDH) and deglycosylated PDH (dgPDH) from Agaricus meleagris recombinantly expressed in Pichia pastoris were studied. Both gPDH and dgPDH were {"}wired{"} to an osmium redox polymer on graphite electrodes mounted in a flow-injection system. The current from oxidation of glucose by immobilised gPDH and dgPDH was compared using flow injection amperometry and cyclic voltammetry. An increase in the current density was observed for dgPDH (190 mu A cm(-2)) compared with that for gPDH (90 mu A cm(-2)) due to the improved electron transfer between the active site and the electrode. Additionally, the ability of dgPDH for direct electron transfer (DET) was discovered, which is rather unique among FAD-containing enzymes. The ability to oxidise a variety of sugars at a rather low potential makes dgPDH attractive for construction of biofuel cells with high power output. (C) 2012 Elsevier B.V. All rights reserved.",

keywords = "Pyranose dehydrogenase, Deglycosylation, Osmium polymer, Direct electron, transfer, Biosensor",

author = "Maria Yakovleva and Aniko Killyeni and Roberto Ortiz and Christopher Schulz and Domhnall MacAodha and Conghaile, {Peter O.} and Donal Leech and Popescu, {Ionel Catalin} and Christoph Gonaus and Peterbauer, {Clemens K.} and Lo Gorton",

year = "2012",

doi = "10.1016/j.elecom.2012.08.029",

language = "English",

volume = "24",

pages = "120--122",

journal = "Electrochemistry Communications",

issn = "1388-2481",

publisher = "Elsevier",

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TY - JOUR

T1 - Recombinant pyranose dehydrogenase-A versatile enzyme possessing both mediated and direct electron transfer

AU - Yakovleva, Maria

AU - Killyeni, Aniko

AU - Ortiz, Roberto

AU - Schulz, Christopher

AU - MacAodha, Domhnall

AU - Conghaile, Peter O.

AU - Leech, Donal

AU - Popescu, Ionel Catalin

AU - Gonaus, Christoph

AU - Peterbauer, Clemens K.

AU - Gorton, Lo

PY - 2012

Y1 - 2012

N2 - The catalytical properties of glycosylated pyranose dehydrogenase (gPDH) and deglycosylated PDH (dgPDH) from Agaricus meleagris recombinantly expressed in Pichia pastoris were studied. Both gPDH and dgPDH were "wired" to an osmium redox polymer on graphite electrodes mounted in a flow-injection system. The current from oxidation of glucose by immobilised gPDH and dgPDH was compared using flow injection amperometry and cyclic voltammetry. An increase in the current density was observed for dgPDH (190 mu A cm(-2)) compared with that for gPDH (90 mu A cm(-2)) due to the improved electron transfer between the active site and the electrode. Additionally, the ability of dgPDH for direct electron transfer (DET) was discovered, which is rather unique among FAD-containing enzymes. The ability to oxidise a variety of sugars at a rather low potential makes dgPDH attractive for construction of biofuel cells with high power output. (C) 2012 Elsevier B.V. All rights reserved.

AB - The catalytical properties of glycosylated pyranose dehydrogenase (gPDH) and deglycosylated PDH (dgPDH) from Agaricus meleagris recombinantly expressed in Pichia pastoris were studied. Both gPDH and dgPDH were "wired" to an osmium redox polymer on graphite electrodes mounted in a flow-injection system. The current from oxidation of glucose by immobilised gPDH and dgPDH was compared using flow injection amperometry and cyclic voltammetry. An increase in the current density was observed for dgPDH (190 mu A cm(-2)) compared with that for gPDH (90 mu A cm(-2)) due to the improved electron transfer between the active site and the electrode. Additionally, the ability of dgPDH for direct electron transfer (DET) was discovered, which is rather unique among FAD-containing enzymes. The ability to oxidise a variety of sugars at a rather low potential makes dgPDH attractive for construction of biofuel cells with high power output. (C) 2012 Elsevier B.V. All rights reserved.

KW - Pyranose dehydrogenase

KW - Deglycosylation

KW - Osmium polymer

KW - Direct electron

KW - transfer

KW - Biosensor

U2 - 10.1016/j.elecom.2012.08.029

DO - 10.1016/j.elecom.2012.08.029

M3 - Article

SN - 1388-2481

VL - 24

SP - 120

EP - 122

JO - Electrochemistry Communications

JF - Electrochemistry Communications

ER -

Recombinant pyranose dehydrogenase-A versatile enzyme possessing both mediated and direct electron transfer

Abstract

Subject classification (UKÄ)

Free keywords

Access to Document

Fingerprint

Research output

Improving the biocatalyst. Engineering of fungal oxidoreductases and thin-film electrodes for improvement of membraneless biofuel cells and carbohydrate biosensors.

Cite this