Open AccessDetection and characterization of a novel extracellular fungal enzyme that catalyzes the specific and hydrolytic cleavage of lignin guaiacylglycerol β‐aryl ether linkages
Author(s) -
Otsuka Yuichiro,
Sonoki Tomonori,
Ikeda Seiichiro,
Kajita Shinya,
Nakamura Masaya,
Katayama Yoshihiro
Publication year - 2003
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2003.03545.x
Subject(s) - ether , ether cleavage , lignin , chemistry , cleavage (geology) , aryl , extracellular , guaiacol , hydrolysis , enzyme , organic chemistry , biochemistry , biology , paleontology , alkyl , fracture (geology)
Cleavage of the arylglycerol β‐aryl ether linkage is the most important process in the biological degradation of lignin. The bacterial β‐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 β‐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 β‐aryl ether cleavage enzyme was produced by a newly isolated fungus, 2BW‐1, and is secreted into the extracellular fraction. The β‐aryl ether cleavage enzyme converts the guaiacylglycerol β‐ O ‐guaiacyl ether (GOG) to guaiacylglycerol and guaiacol. It requires the Cα alcohol structure and p‐hydroxyl group and specifically attacks the β‐aryl ether linkage of high‐molecular mass lignins with addition of two water molecules at the Cα and Cβ positions.