Synthesis and enzymatic hydrolysis of a diaryl benzyl ester model of a lignin-carbohydrate complex (LCC)

Nylander, Filip; Sunner, Hampus; Olsson, Lisbeth; Christakopoulos, Paul; Westman, Gunnar

doi:10.1515/hf-2014-0347

Cited by 18 publications

(13 citation statements)

References 40 publications

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“…The influence of the lignin moiety of the ester linkage on Cu GE’s activity is not evaluated here but the lignin structure in LRP is expected to be optimal for Cu GE activity because the substrate closely resembles the naturally occurring structure. In previous studies, the ester linkages have been synthesized by esterification to simpler alcohols [ 20 ] with little resemblance to lignin. We observe a synergistic activity between Cu GE and GH10 endo-xylanase because Cu GE releases oligomeric products that serve as new substrate for GH10 endo-xylanase.…”

Section: Discussionmentioning

confidence: 99%

The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch

Mosbech

Holck

Meyer

et al. 2018

Biotechnol Biofuels

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BackgroundGlucuronoyl esterases belong to carbohydrate esterase family 15 and catalyze de-esterification. Their natural function is presumed to be cleavage of ester linkages in lignin–carbohydrate complexes particularly those linking lignin and glucuronoyl residues in xylans in hardwood.ResultsHere, we show for the first time a detailed product profile of aldouronic acids released from birchwood lignin by a glucuronoyl esterase from the white-rot fungus Cerrena unicolor (CuGE). CuGE releases substrate for GH10 endo-xylanase which results in significantly increased product release compared to the action of endo-xylanase alone. CuGE also releases neutral xylo-oligosaccharides that can be ascribed to the enzymes feruloyl esterase side activity as demonstrated by release of ferulic acid from insoluble wheat arabinoxylan.ConclusionThe data verify the enzyme’s unique ability to catalyze removal of all glucuronoxylan associated with lignin and we propose that this is a direct result of enzymatic cleavage of the ester bonds connecting glucuronoxylan to lignin via 4-O-methyl glucuronoyl-ester linkages. This function appears important for the fungal organism’s ability to effectively utilize all available carbohydrates in lignocellulosic substrates. In bioprocess perspectives, this enzyme is a clear candidate for polishing lignin for residual carbohydrates to achieve pure, native lignin fractions after minimal pretreatment.Electronic supplementary materialThe online version of this article (10.1186/s13068-018-1075-2) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch

Mosbech

Holck

Meyer

et al. 2018

Biotechnol Biofuels

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“…Up until now, a variety of different synthetic substrates has been used to study the activity of glucuronoyl esterases ( Katsimpouras et al, 2014 ; d’Errico et al, 2015 ; Nylander et al, 2015 ; Sunner et al, 2015 ) besides the methyl ester of 4- O -methyl- D -glucuronic acid. Very recently, glucuronoyl esterase activity on naturally derived substrates was suggested by Arnling Bååth et al (2016) and d’Errico et al (2016) but there is still no understanding of how the glucuronoyl esterases function together with other carbohydrate acting enzymes in lignocellulose deconstruction.…”

Section: Introductionmentioning

confidence: 99%

A New Functional Classification of Glucuronoyl Esterases by Peptide Pattern Recognition

et al. 2017

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Glucuronoyl esterases are a novel type of enzymes believed to catalyze the hydrolysis of ester linkages between lignin and glucuronoxylan in lignocellulosic biomass, linkages known as lignin carbohydrate complexes. These complexes contribute to the recalcitrance of lignocellulose. Glucuronoyl esterases are a part of the microbial machinery for lignocellulose degradation and coupling their role to the occurrence of lignin carbohydrate complexes in biomass is a desired research goal. Glucuronoyl esterases have been assigned to CAZymes family 15 of carbohydrate esterases, but only few examples of characterized enzymes exist and the exact activity is still uncertain. Here peptide pattern recognition is used as a bioinformatic tool to identify and group new CE15 proteins that are likely to have glucuronoyl esterase activity. 1024 CE15-like sequences were drawn from GenBank and grouped into 24 groups. Phylogenetic analysis of these groups made it possible to pinpoint groups of putative fungal and bacterial glucuronoyl esterases and their sequence variation. Moreover, a number of groups included previously undescribed CE15-like sequences that are distinct from the glucuronoyl esterases and may possibly have different esterase activity. Hence, the CE15 family is likely to comprise other enzyme functions than glucuronoyl esterase alone. Gene annotation in a variety of fungal and bacterial microorganisms showed that coprophilic fungi are rich and diverse sources of CE15 proteins. Combined with the lifestyle and habitat of coprophilic fungi, they are predicted to be excellent candidates for finding new glucuronoyl esterase genes.

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“…3 demonstrates the tolerance of GEs for larger aryl propane structures on the side of lignin alcohols (Fig. 4) (23)(24)(25). It is worth noting that the esterification of glucuronoxylan with methanol reduces its solubility.…”

Section: Fig 2 3d Structures Of the Catalytic Domain Of Ge From T Rementioning

confidence: 97%

Microbial Glucuronoyl Esterases: 10 Years after Discovery

Biely

2016

Appl Environ Microbiol

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A carbohydrate esterase called glucuronoyl esterase (GE) was discovered 10 years ago in a cellulolytic system of the wood-rotting fungus Schizophyllum commune. Genes coding for GEs were subsequently found in a number of microbial genomes, and a new family of carbohydrate esterases (CE15) has been established. The multidomain structures of GEs, together with their catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass, led to the view that the esterases evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. This idea of the function of GEs is further supported by the effects of cloning of fungal GEs in plants and by very recently reported evidence for changes in the size of isolated lignin-carbohydrate complexes due to uronic acid de-esterification. These facts make GEs interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants. This article is a brief summary of current knowledge of these relatively recent and unexplored esterases.

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Synthesis and enzymatic hydrolysis of a diaryl benzyl ester model of a lignin-carbohydrate complex (LCC)

Cited by 18 publications

References 40 publications

The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch

The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin–carbohydrate complexes from birch

A New Functional Classification of Glucuronoyl Esterases by Peptide Pattern Recognition

Microbial Glucuronoyl Esterases: 10 Years after Discovery

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