Degradation of lignin β-aryl ether units in Arabidopsis thaliana expressing LigD, LigF and LigG from Sphingomonas paucimobilis SYK-6
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Degradation of lignin β-aryl ether units in Arabidopsis thaliana expressing LigD, LigF and LigG from Sphingomonas paucimobilis SYK-6. / Mnich, Ewelina; Vanholme, Ruben; Oyarce, Paula; Liu, Sarah; Lu, Fachuang; Goeminne, Geert; Jørgensen, Bodil; Motawie, Mohammed Saddik; Boerjan, Wout; Ralph, John; Ulvskov, Peter; Møller, Birger Lindberg; Bjarnholt, Nanna; Harholt, Jesper.
I: Plant Biotechnology Journal, Bind 15, Nr. 5, 2017, s. 581-593.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Degradation of lignin β-aryl ether units in Arabidopsis thaliana expressing LigD, LigF and LigG from Sphingomonas paucimobilis SYK-6
AU - Mnich, Ewelina
AU - Vanholme, Ruben
AU - Oyarce, Paula
AU - Liu, Sarah
AU - Lu, Fachuang
AU - Goeminne, Geert
AU - Jørgensen, Bodil
AU - Motawie, Mohammed Saddik
AU - Boerjan, Wout
AU - Ralph, John
AU - Ulvskov, Peter
AU - Møller, Birger Lindberg
AU - Bjarnholt, Nanna
AU - Harholt, Jesper
N1 - This article is protected by copyright. All rights reserved.
PY - 2017
Y1 - 2017
N2 - Lignin is a major polymer in the secondary plant cell wall and composed of hydrophobic interlinked hydroxyphenylpropanoid units. The presence of lignin hampers conversion of plant biomass into biofuels; plants with modified lignin are therefore being investigated for increased digestibility. The bacterium Sphingomonas paucimobilis produces lignin-degrading enzymes including LigD, LigF and LigG involved in cleaving the most abundant lignin inter-unit linkage, the β-aryl ether bond. In this study, we expressed the LigD, LigF and LigG (LigDFG) genes in Arabidopsis thaliana to introduce post-lignification modifications into the lignin structure. The three enzymes were targeted to the secretory pathway. Phenolic metabolite profiling and 2D HSQC NMR of the transgenic lines showed an increase in oxidized guaiacyl and syringyl units without concomitant increase in oxidized β-aryl-ether units, showing lignin bond cleavage. Saccharification yield increased significantly in transgenic lines expressing LigDFG, showing the applicability of our approach. Additional new information on substrate specificity of the LigDFG enzymes is also provided. This article is protected by copyright. All rights reserved.
AB - Lignin is a major polymer in the secondary plant cell wall and composed of hydrophobic interlinked hydroxyphenylpropanoid units. The presence of lignin hampers conversion of plant biomass into biofuels; plants with modified lignin are therefore being investigated for increased digestibility. The bacterium Sphingomonas paucimobilis produces lignin-degrading enzymes including LigD, LigF and LigG involved in cleaving the most abundant lignin inter-unit linkage, the β-aryl ether bond. In this study, we expressed the LigD, LigF and LigG (LigDFG) genes in Arabidopsis thaliana to introduce post-lignification modifications into the lignin structure. The three enzymes were targeted to the secretory pathway. Phenolic metabolite profiling and 2D HSQC NMR of the transgenic lines showed an increase in oxidized guaiacyl and syringyl units without concomitant increase in oxidized β-aryl-ether units, showing lignin bond cleavage. Saccharification yield increased significantly in transgenic lines expressing LigDFG, showing the applicability of our approach. Additional new information on substrate specificity of the LigDFG enzymes is also provided. This article is protected by copyright. All rights reserved.
U2 - 10.1111/pbi.12655
DO - 10.1111/pbi.12655
M3 - Journal article
C2 - 27775869
VL - 15
SP - 581
EP - 593
JO - Plant Biotechnology Journal
JF - Plant Biotechnology Journal
SN - 1467-7644
IS - 5
ER -
ID: 169077792