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POL-88, a mutant of the white-rot fungusPhanerochaete chrysosporium , was selected for diminished phenol-oxidizing enzyme activity. A wide variety of phenolic compounds were degraded by ligninolytic cultures of this mutant. With severalo -diphenolic substrates, degradation intermediates were produced that had UV spectra consistent with muconic acids. Extensive spectrophotometric and polarographic assays failed to detect classical ring-cleaving dioxygenases in cell homogenates or in extracts from ligninolytic cultures. Even so, a sensitive carrier-trapping assay showed that intact cultures degraded [U -14 C]catechol to [14 C]muconic acid, establishing the presence of a system capable of 1,2-intradiol fission. Significant accumulation of [14 C]muconic acid into carrier occurred only when evolution of14 CO2 from [14 C]catechol was inhibited by treating cultures with excess nutrient nitrogen (e.g.,l -glutamic acid) or with cycloheximide.l -Glutamic acid is known from past work to repress the ligninolytic system inP. chrysosporium and to mimic the effect of cycloheximide. The results here indicate, therefore, that the enzyme system responsible for degrading ring-cleavage products to CO2 turns over faster than does the system responsible for ring cleavage.

Degradation of Phenolic Compounds and Ring Cleavage of Catechol by Phanerochaete chrysosporium