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

Source: Proc. Natl. Acad. Sci. USA, Vol. 81, pp. 2936-2940, April 1990

Author(s)Kersten, Philip J.

Publication Year: 1990  View PDF »

Category: Journal Articles

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, glycol-aldehyde, acetaldehyde, glyoxal, glyoxylic acid, and formal-dehyde, were determined by using a lignin peroxidase coupled-assay at pH 4.5.

Keywords: Hydrogen peroxide, methylglyoxal, white-rot fungus, wood decay

File size: 266 kb(s)

Date posted: 05/19/2010
Current FPL Scientist associated with this product
Kersten, Philip J.
Research Microbiologist

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