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Specific degradation ofβ-aryl ether linkage in synthetic lignin (dehydrogenative polymerizate) by bacterial enzymes ofSphingomonas paucimobilis SYK-6 produced in recombinantEscherichia coli
Journal of Wood Science volume 48, pages 429–433 (2002)
Abstract
Sphingomonas paucimobilis SYK-6 produces unique and specific enzymes, such asβ-etherases,O-demethylases, and ring fission dioxygenases, for lignin degradation. Cleavage of arylglycerol-β-aryl ether linkage is the most important process in the lignin metabolic pathway ofS. paucimobilis SYK-6. We reported the genes (ligD, ligE, ligF) for enzymes that cleavedβ-aryl ether linkage of dimeric compounds in previous studies. In this study we synthesized the fluorescent high-molecular-weight lignin (UBE-DHP) by dehydrogenative polymerization. We investigated theβ-aryl ether cleavage ability of these enzymes produced in recombinantEscherichia coli. When UBE-DHP was incubated with LigF, 4-methylumbeliferone was released as a result ofβ-aryl ether cleavage of αO-methylumbelliferyl-β-hydroxypropiovanillone (compound III) incorporated in UBE-DHP. Here, we report thatβ-etherase ofS. paucimobilis SYK-6 can be expressed inE. coli and is able to cleave theβ-aryl ether linkage in synthetic high-molecular-weight lignin.
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Sonoki, T., Iimura, Y., Masai, E. et al. Specific degradation ofβ-aryl ether linkage in synthetic lignin (dehydrogenative polymerizate) by bacterial enzymes ofSphingomonas paucimobilis SYK-6 produced in recombinantEscherichia coli . J Wood Sci 48, 429–433 (2002). https://doi.org/10.1007/BF00770705
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DOI: https://doi.org/10.1007/BF00770705