EFFECT OF ENZYME DEGLYCOSYLATION ON THE AMPEROMETRIC DETECTION OF GLUCOSE AT PDH-MODIFIED ELECTRODE
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3821387
- author
- Killyeni, Aniko ; Yakovleva, Maria LU ; Peterbauer, Clemens K. ; Leech, Donal ; Gorton, Lo LU and Popescu, Ionel Catalin
- organization
- publishing date
- 2012
- type
- 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
- Universitatea 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
- 2016-04-01 10:18:02
- date last changed
- 2022-01-25 21:56:05
@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}}, keywords = {{pyranose dehydrogenase; enzyme deglycosylation; glucose amperometric; detection; Os-redox polymer}}, language = {{eng}}, number = {{4}}, pages = {{87--99}}, publisher = {{Universitatea 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}}, }