Selective Cleavage of Lignin β-<i>O</i>-4 Aryl Ether Bond by β-Etherase of the White-Rot Fungus <i>Dichomitus squalens</i>
Mila MarinovícDivision of Microbiology and Biotechnology, Department of Food and Environmental Sciences, University of Helsinki, Viikinkaari 9, FI-00014 Helsinki, FinlandPaula NousiainenDepartment of Chemistry, Laboratory of Organic Chemistry, University of Helsinki, A.I. Virtasen aukio 1, FI-00014 Helsinki, FinlandAdiphol DilokpimolFungal Physiology, Westerdijk Fungal Biodiversity Institute & Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584 CT Utrecht, The NetherlandsJussi KontroDepartment of Chemistry, Laboratory of Organic Chemistry, University of Helsinki, A.I. Virtasen aukio 1, FI-00014 Helsinki, FinlandRobin MooreDepartment of Chemistry, Laboratory of Organic Chemistry, University of Helsinki, A.I. Virtasen aukio 1, FI-00014 Helsinki, FinlandJussi SipiläDepartment of Chemistry, Laboratory of Organic Chemistry, University of Helsinki, A.I. Virtasen aukio 1, FI-00014 Helsinki, FinlandRonald P. de VriesDivision of Microbiology and Biotechnology, Department of Food and Environmental Sciences, University of Helsinki, Viikinkaari 9, FI-00014 Helsinki, FinlandMiia MäkeläDivision of Microbiology and Biotechnology, Department of Food and Environmental Sciences, University of Helsinki, Viikinkaari 9, FI-00014 Helsinki, FinlandKristiina HildénDivision of Microbiology and Biotechnology, Department of Food and Environmental Sciences, University of Helsinki, Viikinkaari 9, FI-00014 Helsinki, Finland
2018en
ABI
Annotatsiya
4 aryl ether bond of a dimeric lignin model compound in a glutathione-dependent reaction. Ds-GST1 also demonstrated activity on polymeric synthetic lignin fractions, shown by a decrease in molecular weight distribution of the laccase-oxidized guaiacyl dehydrogenation polymer. In addition to a possible role of Ds-GST1 in intracellular catabolism of lignin-derived aromatic compounds, the cleavage of the most abundant linkages in lignin under mild reaction conditions makes this biocatalyst an attractive green alternative in biotechnological applications.
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