Transformation of 2-hydroxydibenzofuran by laccases of the white rot fungi Trametes versicolor and Pycnoporus cinnabarinus and characterization of oligomerization products

Laccase, a ligninolytic enzyme, was secreted by each of the white rot fungi Trametes versicolor and Pycnoporus cinnabarinus during growth in a nitrogen-rich medium under agitated conditions. After addition of 2-hydroxydibenzofuran to cell-free supernatants of the cultures, yellow precipitates were formed. These precipitates were poorly soluble in water and therefore readily separated from the supernatant. The products formed were more hydrophobic than the substrate, as indicated by their longer retention times on a reverse phase high-performance liquid chromatography column. Mass spectrometric analysis of the purified products indicated the formation of oligomers. Analysis of the mixture of products by gas chromatography and mass spectrometry after derivatization with diazomethane suggested the formation of at least three dimeric and nine trimeric products. Carbon-carbon and carbon-oxygen bonds were identified in the dimers and trimers, respectively. The nuclear magnetic resonance spectrum of the main dimer suggested coupling of the two monomers at the carbon one position.