Enzymatic oxidation of glyoxylate by brown rot fungus Fomitopsis pinicola
| Authors | |
|---|---|
| Year of publication | 2002 |
| Type | Article in Proceedings |
| Conference | XVIII. BIOCHEMICKÝ ZJAZD |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | brown rot fungus; glyoxylate oxidase |
| Description | Two types of enzymes oxidizing glyoxylate were purified from basidiomycetes as yet. One of them was identified as glyoxylate dehydrogenase, the other as glyoxylate oxidase, both were from Tyromyces palustris. We partially purified activity responsible for enzymatic glyoxylate oxidation from brown rot fungus Fomitopsis pinicola. The purification procedure consisted of (NH4)2SO4 precipitation of cell-free extract from F. pinicola, ion-exchange chromatography on Sepharose Q and chromatofocusing on MonoP column. Results of ion-exchange chromatography indicated that two proteins contributed to this activity. One of the enzymes has very low stability, so only one of them was characterized more in detail. We determined isoelectric point of this enzyme to be about 4.8. Among the compounds tested, the best substrate was glyoxylate. Glycollate and glyoxal were slightly utilized, but none of the other used substrates, such as ethylene glycol, oxalate, formaldehyde, formate, were effective. 2,6-dichloroindophenol, ferricyanide and very slightly even cytochrome c served as electron acceptors but neither NAD+, NADP+ nor FMN was effective. Mr of native enzyme was estimated to be about 200 000 on Superose 6 gel filtration column. |
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