PMID: 11607073Apr 1, 1990Paper

Glyoxal oxidase of Phanerochaete chrysosporium: its characterization and activation by lignin peroxidase

Proceedings of the National Academy of Sciences of the United States of America
P J Kersten

Abstract

Glyoxal oxidase (GLOX) is an extracellular H2O2-generating enzyme produced by ligninolytic cultures of Phanerochaete chrysosporium. The production, purification, and partial characterization of GLOX from agitated cultures are described here. High-oxygen levels are critical for GLOX production as for lignin peroxidase. GLOX purified by anion-exchange chromatography appears homogeneous by NaDod-SO4/PAGE (molecular mass = 68 kDa). However, analysis by isoelectric focusing indicates two major bands (pI 4.7 and 4.9) that stain as glycoproteins as well as for H2O2-producing activity in the presence of methylglyoxal. Purified GLOX shows a marked stimulation in activity when incubated with Cu2+; full activation takes more than 1 hr with 1 mM CuSO4 at pH 6. The steady-state kinetic parameters for the GLOX oxidation of methylglyoxal, glyceraldehyde, dihydroxyacetone, glycolaldehyde, acetaldehyde, glyoxal, glyoxylic acid, and formaldehyde, were determined by using a lignin peroxidase coupled-assay at pH 4.5. Of these substrates, the best is the extracellular metabolite methylglyoxal with a Km of 0.64 mM an apparent rate of catalysis, kcat, of 198 s1 under air-saturated conditions. The Km for oxygen is greater than the concentration of oxy...Continue Reading

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Citations

Jul 26, 2008·Applied Microbiology and Biotechnology·Holy RavalasonIsabelle Herpoël-Gimbert
Sep 24, 2008·Applied Microbiology and Biotechnology·Deepak Singh, Shulin Chen
Jan 18, 2012·Applied Microbiology and Biotechnology·Aitor Hernández-OrtegaAngel T Martínez
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