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Substrate Preference Pattern of Agaricus meleagris Pyranose Dehydrogenase Evaluated through Bioelectrochemical Flow Injection Amperometry

Rafighi, Parvin ; Bollella, Paolo ; Pankratova, Galina LU ; Peterbauer, Clemens K. ; Conghaile, Peter ; Leech, Dónal ; Haghighi, Behzad LU and Gorton, Lo LU (2019) In ChemElectroChem 6(3). p.801-809
Abstract

Pyranose dehydrogenase (PDH) is a quinone-dependent extracellular flavoglycoprotein mainly produced by litter-decomposing fungi and contributes to the degradation of lignocellulose. PDH in terms of structure and catalytic features pertains to the glucose methanol-choline oxidoreductase family and oxidizes a wide substrate range of aldopyranoses including hexoses, pentoses, disaccharides and oligosaccharides with a high degree of regioselectivity. The purpose of this study was to rationalize the preference of PDH immobilized on an electrode with the structural features of various substrates and thus the kinetic constants were measured for various sugars. PDH was co-immobilized on the electrode with an osmium redox polymer. Response... (More)

Pyranose dehydrogenase (PDH) is a quinone-dependent extracellular flavoglycoprotein mainly produced by litter-decomposing fungi and contributes to the degradation of lignocellulose. PDH in terms of structure and catalytic features pertains to the glucose methanol-choline oxidoreductase family and oxidizes a wide substrate range of aldopyranoses including hexoses, pentoses, disaccharides and oligosaccharides with a high degree of regioselectivity. The purpose of this study was to rationalize the preference of PDH immobilized on an electrode with the structural features of various substrates and thus the kinetic constants were measured for various sugars. PDH was co-immobilized on the electrode with an osmium redox polymer. Response currents for different sugars were measured using flow injection amperometry at +0.3 V vs. Ag|AgCl, KCl (0.1 M). The Michaelis-Menten constants, the turnover numbers and the catalytic efficiency were calculated and revealed that type, orientation and configuration of the substituent play a major role on substrate preference. An OH-group at C-1 and C-6 are not essential and substrate specificities are little affected by the substitution at C-1. The presence and orientation of OH− at C-2 and C-3 are relevant for reactivity. Orientation of OH− at the C-4 position has little effect, and sugars with a substitution below the plane at C-5 are not suitable as substrate. Highest activity for oxidation of glucose, mannose and sucrose was detected at pH 8.5.

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author
; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
amperometry, enzyme modified electrode, osmium redox polymer, pyranose dehydrogenase, sugar oxidation
in
ChemElectroChem
volume
6
issue
3
pages
801 - 809
publisher
Wiley-Blackwell
external identifiers
  • scopus:85055590154
ISSN
2196-0216
DOI
10.1002/celc.201801194
language
English
LU publication?
yes
id
5d3b2b0f-3927-43dc-a077-9396b687ed1c
date added to LUP
2018-11-26 15:27:23
date last changed
2022-04-10 03:55:53
@article{5d3b2b0f-3927-43dc-a077-9396b687ed1c,
  abstract     = {{<p>Pyranose dehydrogenase (PDH) is a quinone-dependent extracellular flavoglycoprotein mainly produced by litter-decomposing fungi and contributes to the degradation of lignocellulose. PDH in terms of structure and catalytic features pertains to the glucose methanol-choline oxidoreductase family and oxidizes a wide substrate range of aldopyranoses including hexoses, pentoses, disaccharides and oligosaccharides with a high degree of regioselectivity. The purpose of this study was to rationalize the preference of PDH immobilized on an electrode with the structural features of various substrates and thus the kinetic constants were measured for various sugars. PDH was co-immobilized on the electrode with an osmium redox polymer. Response currents for different sugars were measured using flow injection amperometry at +0.3 V vs. Ag|AgCl, KCl (0.1 M). The Michaelis-Menten constants, the turnover numbers and the catalytic efficiency were calculated and revealed that type, orientation and configuration of the substituent play a major role on substrate preference. An OH-group at C-1 and C-6 are not essential and substrate specificities are little affected by the substitution at C-1. The presence and orientation of OH− at C-2 and C-3 are relevant for reactivity. Orientation of OH− at the C-4 position has little effect, and sugars with a substitution below the plane at C-5 are not suitable as substrate. Highest activity for oxidation of glucose, mannose and sucrose was detected at pH 8.5.</p>}},
  author       = {{Rafighi, Parvin and Bollella, Paolo and Pankratova, Galina and Peterbauer, Clemens K. and Conghaile, Peter and Leech, Dónal and Haghighi, Behzad and Gorton, Lo}},
  issn         = {{2196-0216}},
  keywords     = {{amperometry; enzyme modified electrode; osmium redox polymer; pyranose dehydrogenase; sugar oxidation}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{801--809}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{ChemElectroChem}},
  title        = {{Substrate Preference Pattern of Agaricus meleagris Pyranose Dehydrogenase Evaluated through Bioelectrochemical Flow Injection Amperometry}},
  url          = {{http://dx.doi.org/10.1002/celc.201801194}},
  doi          = {{10.1002/celc.201801194}},
  volume       = {{6}},
  year         = {{2019}},
}