Selective cleavage of lignin β-O-4 aryl ether bond by β-etherase of the white-rot fungus Dichomitus squalens.

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Marinovic , M , Nousiainen , P , Dilokpimol , A , Kontro , J , Moore , R , Sipilä , J , de Vries , R P , Mäkelä , M R & Hilden , K 2018 , ' Selective cleavage of lignin β-O-4 aryl ether bond by β-etherase of the white-rot fungus Dichomitus squalens. ' , ACS Sustainable Chemistry & Engineering , vol. 6 , no. 3 , pp. 2878-2882 . https://doi.org/10.1021/acssuschemeng.7b03619

Title: Selective cleavage of lignin β-O-4 aryl ether bond by β-etherase of the white-rot fungus Dichomitus squalens.
Author: Marinovic, Mila; Nousiainen, Paula; Dilokpimol, Adiphol; Kontro, Jussi; Moore, Robin; Sipilä, Jussi; de Vries, Ronald P.; Mäkelä, Miia R.; Hilden, Kristiina
Contributor: University of Helsinki, Department of Food and Nutrition
University of Helsinki, Department of Chemistry
University of Helsinki, Department of Chemistry
University of Helsinki, Department of Chemistry
University of Helsinki, Jussi Sipilä / Principal Investigator
University of Helsinki, Department of Food and Nutrition
University of Helsinki, Department of Microbiology
University of Helsinki, Department of Microbiology
Date: 2018-03
Language: eng
Number of pages: 9
Belongs to series: ACS Sustainable Chemistry & Engineering
ISSN: 2168-0485
URI: http://hdl.handle.net/10138/298677
Abstract: Production of value-added compounds from a renewable aromatic polymer, lignin, has proven to be challenging. Chemical procedures, involving harsh reaction conditions, are costly and often result in nonselective degradation of lignin linkages. Therefore, enzymatic catalysis with selective cleavage of lignin bonds provides a sustainable option for lignin valorization. In this study, we describe the first functionally characterized fungal intracellular beta-etherase from the wood-degrading white-rot basidiomycete Dichomitus squalens. This enzyme, Ds-GST1, from the glutathione-Stransferase superfamily selectively cleaved the beta-O-4 aryl ether bond of a dimeric lignin model compound in a glutathionedependent reaction. Ds-GST1 also demonstrated activity on polymeric synthetic lignin fractions, shown by a decrease in molecular weight distribution of the lactase -oxidized guaiacyl dehydrogenation polymer. In addition to a possible role of DsGST1 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.
Subject: Dichomitus squalens
White-rot fungi
Glutathione-S-transferase
beta-Etherase
Lignin
beta-O-4 linkage
SP STRAIN SYK-6
ENZYMATIC CLEAVAGE
PAUCIMOBILIS SYK-6
ENZYMES
VALORIZATION
GENE
WOOD
TRANSFERASES
SUPERFAMILY
DEGRADATION
116 Chemical sciences
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