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EFFECT OF ENZYME DEGLYCOSYLATION ON THE AMPEROMETRIC DETECTION OF GLUCOSE AT PDH-MODIFIED ELECTRODE

Killyeni, Aniko; Yakovleva, Maria LU ; Peterbauer, Clemens K.; Leech, Donal; Gorton, Lo LU and Popescu, Ionel Catalin (2012) In Studia Universitatis Babes-Bolyai, Chemia 57(4). p.87-99
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) mu A/cm(2)) compared with G/Os-RP/gPDH [(81.4 +/- 1.4) mu A/cm(2)]. Additionally, the deglycosylation of the enzyme resulted in a higher... (More)
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) mu A/cm(2)) compared with G/Os-RP/gPDH [(81.4 +/- 1.4) mu A/cm(2)]. 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). (Less)
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author
organization
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Contribution to journal
publication status
published
subject
keywords
pyranose dehydrogenase, enzyme deglycosylation, glucose amperometric, detection, Os-redox polymer
in
Studia Universitatis Babes-Bolyai, Chemia
volume
57
issue
4
pages
87 - 99
publisher
Univ Babes-Bolyai
external identifiers
  • wos:000318593300009
  • scopus:84875890821
ISSN
2065-9520
language
English
LU publication?
yes
id
84ea3a54-e591-4e94-82dc-f391a12e17b7 (old id 3821387)
date added to LUP
2013-06-25 13:05:33
date last changed
2017-01-01 03:27:32
@article{84ea3a54-e591-4e94-82dc-f391a12e17b7,
  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) mu A/cm(2)) compared with G/Os-RP/gPDH [(81.4 +/- 1.4) mu A/cm(2)]. 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).},
  author       = {Killyeni, Aniko and Yakovleva, Maria and Peterbauer, Clemens K. and Leech, Donal and Gorton, Lo and Popescu, Ionel Catalin},
  issn         = {2065-9520},
  keyword      = {pyranose dehydrogenase,enzyme deglycosylation,glucose amperometric,detection,Os-redox polymer},
  language     = {eng},
  number       = {4},
  pages        = {87--99},
  publisher    = {Univ Babes-Bolyai},
  series       = {Studia Universitatis Babes-Bolyai, Chemia},
  title        = {EFFECT OF ENZYME DEGLYCOSYLATION ON THE AMPEROMETRIC DETECTION OF GLUCOSE AT PDH-MODIFIED ELECTRODE},
  volume       = {57},
  year         = {2012},
}