Journal
EUROPEAN JOURNAL OF BIOCHEMISTRY
Volume 270, Issue 11, Pages 2353-2362Publisher
WILEY
DOI: 10.1046/j.1432-1033.2003.03545.x
Keywords
lignin biodegradaion; beta-aryl ether linkage; fungi; guaiacylglycerol beta-O-guaiacyl ether; extracellular enzyme
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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 Calpha 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 Calpha and Cbeta positions.
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