hymecromone and guaiacylglycerol-beta-guaiacyl-ether

Cleavage of the arylglycerol beta-aryl ether linkage is the most important process in the biological degradation of lignin. The bacterial beta-etherase was described previously and shown to be tightly associated with the cellular membrane. In this study, we aimed to detect and isolate a new extracellular function that catalyses the beta-aryl ether linkage cleavage of high-molecular lignin in the soil fungi. We screened and isolated 2BW-1 cells by using a highly sensitive fluorescence assay system. The beta-aryl ether cleavage enzyme was produced by a newly isolated fungus, 2BW-1, and is secreted into the extracellular fraction. The beta-aryl ether cleavage enzyme converts the guaiacylglycerol beta-O-guaiacyl ether (GOG) to guaiacylglycerol and guaiacol. It requires the C alpha alcohol structure and p-hydroxyl group and specifically attacks the beta-aryl ether linkage of high-molecular mass lignins with addition of two water molecules at the C alpha and C beta positions.

Topics: Catalysis; Cell Death; Cell Membrane; Classification; DNA, Ribosomal; Electrophoresis, Polyacrylamide Gel; Fungi; Guaifenesin; Hydrolysis; Hymecromone; Indicators and Reagents; Lignin; Mass Spectrometry; Microscopy, Fluorescence; Models, Chemical; Phylogeny; Substrate Specificity; Time Factors