Effect of enzyme deglycosylation on the amperometric detection of glucose at PDH-modified electrode

Anikó Killyéni; Maria E. Yakovleva; Clemens K. Peterbauer; Dónal Leech; Lo Gorton; Ionel Catalin Popescu

Effect of enzyme deglycosylation on the amperometric detection of glucose at PDH-modified electrode

Anikó Killyéni
, Maria E. Yakovleva
, Clemens K. Peterbauer
, Dónal Leech
, Lo Gorton
, Ionel Catalin Popescu

Cellular & Molecular Medicine

Babes-Bolyai University
Lund University
BOKU-University of Natural Resources and Life Sciences

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

3 Citations (Scopus)

Abstract

The effect of deglycosylation of pyranose dehydrogenase (PDH), obtained from Agaricus meleagris and recombinantly expressed in Pichia pastoris, on the amperometric detection of glucose was investigated. Glycosylated (gPDH) and deglycosylated (dgPDH) PDH were immobilized on spectrographic graphite (G) simultaneously with an Os redox polymer (Os-RP). The amperometric response of G/Os-RP/gPDH and G/Os-RP/dgPDH to glucose was recorded using flow injection measurements and cyclic voltammetry. A significant increase in the maximum catalytic current density was observed for G/Os-RP/dgPDH [(148.7 ± 0.14) μA/cm²) compared with G/Os-RP/gPDH [(81.4 ± 1.4) μA/cm²]. Additionally, the deglycosylation of the enzyme resulted in a higher substrate-enzyme affinity (K_M^app = 2.44 ± 0.10 mM), compared with glycosylated PDH (K_M^app = 7.52 ± 0.34 mM).

Original language	English
Pages (from-to)	87-99
Number of pages	13
Journal	Studia Universitatis Babes-Bolyai Chemia
Issue number	4
Publication status	Published - 2012

Keywords

Enzyme deglycosylation
Glucose amperometric detection
Os-redox polymer
Pyranose dehydrogenase

Cite this

@article{b605a825b94c4a3c8f8f60dd7176e4bf,

title = "Effect of enzyme deglycosylation on the amperometric detection of glucose at PDH-modified electrode",

abstract = "The effect of deglycosylation of pyranose dehydrogenase (PDH), obtained from Agaricus meleagris and recombinantly expressed in Pichia pastoris, on the amperometric detection of glucose was investigated. Glycosylated (gPDH) and deglycosylated (dgPDH) PDH were immobilized on spectrographic graphite (G) simultaneously with an Os redox polymer (Os-RP). The amperometric response of G/Os-RP/gPDH and G/Os-RP/dgPDH to glucose was recorded using flow injection measurements and cyclic voltammetry. A significant increase in the maximum catalytic current density was observed for G/Os-RP/dgPDH [(148.7 ± 0.14) μA/cm2) compared with G/Os-RP/gPDH [(81.4 ± 1.4) μA/cm2]. Additionally, the deglycosylation of the enzyme resulted in a higher substrate-enzyme affinity (KMapp = 2.44 ± 0.10 mM), compared with glycosylated PDH (KMapp = 7.52 ± 0.34 mM).",

keywords = "Enzyme deglycosylation, Glucose amperometric detection, Os-redox polymer, Pyranose dehydrogenase",

author = "Anik{\'o} Killy{\'e}ni and Yakovleva, \{Maria E.\} and Peterbauer, \{Clemens K.\} and D{\'o}nal Leech and Lo Gorton and Popescu, \{Ionel Catalin\}",

year = "2012",

language = "English",

pages = "87--99",

journal = "Studia Universitatis Babes-Bolyai Chemia",

issn = "1224-7154",

publisher = "Babes-Bolyai University",

number = "4",

}

TY - JOUR

T1 - Effect of enzyme deglycosylation on the amperometric detection of glucose at PDH-modified electrode

AU - Killyéni, Anikó

AU - Yakovleva, Maria E.

AU - Peterbauer, Clemens K.

AU - Leech, Dónal

AU - Gorton, Lo

AU - Popescu, Ionel Catalin

PY - 2012

Y1 - 2012

N2 - The effect of deglycosylation of pyranose dehydrogenase (PDH), obtained from Agaricus meleagris and recombinantly expressed in Pichia pastoris, on the amperometric detection of glucose was investigated. Glycosylated (gPDH) and deglycosylated (dgPDH) PDH were immobilized on spectrographic graphite (G) simultaneously with an Os redox polymer (Os-RP). The amperometric response of G/Os-RP/gPDH and G/Os-RP/dgPDH to glucose was recorded using flow injection measurements and cyclic voltammetry. A significant increase in the maximum catalytic current density was observed for G/Os-RP/dgPDH [(148.7 ± 0.14) μA/cm2) compared with G/Os-RP/gPDH [(81.4 ± 1.4) μA/cm2]. Additionally, the deglycosylation of the enzyme resulted in a higher substrate-enzyme affinity (KMapp = 2.44 ± 0.10 mM), compared with glycosylated PDH (KMapp = 7.52 ± 0.34 mM).

AB - The effect of deglycosylation of pyranose dehydrogenase (PDH), obtained from Agaricus meleagris and recombinantly expressed in Pichia pastoris, on the amperometric detection of glucose was investigated. Glycosylated (gPDH) and deglycosylated (dgPDH) PDH were immobilized on spectrographic graphite (G) simultaneously with an Os redox polymer (Os-RP). The amperometric response of G/Os-RP/gPDH and G/Os-RP/dgPDH to glucose was recorded using flow injection measurements and cyclic voltammetry. A significant increase in the maximum catalytic current density was observed for G/Os-RP/dgPDH [(148.7 ± 0.14) μA/cm2) compared with G/Os-RP/gPDH [(81.4 ± 1.4) μA/cm2]. Additionally, the deglycosylation of the enzyme resulted in a higher substrate-enzyme affinity (KMapp = 2.44 ± 0.10 mM), compared with glycosylated PDH (KMapp = 7.52 ± 0.34 mM).

KW - Enzyme deglycosylation

KW - Glucose amperometric detection

KW - Os-redox polymer

KW - Pyranose dehydrogenase

UR - https://www.scopus.com/pages/publications/84875890821

M3 - Article

SN - 1224-7154

SP - 87

EP - 99

JO - Studia Universitatis Babes-Bolyai Chemia

JF - Studia Universitatis Babes-Bolyai Chemia

IS - 4

ER -

Effect of enzyme deglycosylation on the amperometric detection of glucose at PDH-modified electrode

Abstract

Keywords

Other files and links

Fingerprint

Cite this