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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).

Keywords: pyranose dehydrogenase, enzyme deglycosylation, glucose amperometric detection, Os-redox polymer