Glucuronoyl esterases are active on the polymeric substrate methyl esterified glucuronoxylan

Biely, Peter; Malovı́ková, Anna; Uhliariková, Iveta; Li, Xin Liang; Wong, Dominic W. S.

doi:10.1016/j.febslet.2015.07.019

Cited by 28 publications

(24 citation statements)

References 33 publications

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“…Most studies of GEs to date have been conducted using synthetic substrates obtained through organic synthesis (Biely et al 2015; D’Errico et al 2015; Ďuranová et al 2009a; Katsimpouras et al 2014; Li et al 2007; Špániková et al 2007). The production of these compounds is laborious and requires expertise in organic chemistry, and the compounds often do not allow for high-throughput screening due to their requirement for HPLC or NMR analyses.…”

Section: Discussionmentioning

confidence: 99%

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Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds

Hüttner

Klaubauf

Vries

et al. 2017

Appl Microbiol Biotechnol

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The glucuronoyl esterases (GEs) that have been identified so far belong to family 15 of the carbohydrate esterases in the CAZy classification system and are presumed to target ester bonds between lignin alcohols and (4-O-methyl-)d-glucuronic acid residues of xylan. Few GEs have been cloned, expressed and characterised to date. Characterisation has been done on a variety of synthetic substrates; however, the number of commercially available substrates is very limited. We identified novel putative GEs from a wide taxonomic range of fungi and expressed the enzymes originating from Acremonium alcalophilum and Wolfiporia cocos as well as the previously described PcGE1 from Phanerochaete chrysosporium. All three fungal GEs were active on the commercially available compounds benzyl glucuronic acid (BnGlcA), allyl glucuronic acid (allylGlcA) and to a lower degree on methyl glucuronic acid (MeGlcA). The enzymes showed pH stability over a wide pH range and tolerated 6-h incubations of up to 50 °C. Kinetic parameters were determined for BnGlcA. This study shows the suitability of the commercially available model compounds BnGlcA, MeGlcA and allylGlcA in GE activity screening and characterisation experiments. We enriched the spectrum of characterised GEs with two new members of a relatively young enzyme family. Due to its biotechnological significance, this family deserves to be more extensively studied. The presented enzymes are promising candidates as auxiliary enzymes to improve saccharification of plant biomass.Electronic supplementary materialThe online version of this article (doi:10.1007/s00253-017-8266-9) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

“…GEs have been characterised on a variety of synthetic substrates that mimic the structure of lignin-carbohydrate complexes (LCCs) (Biely et al 2015; D’Errico et al 2015, 2016; Nylander et al 2015; Ďuranová et al 2009a, b; Katsimpouras et al 2014; Li et al 2007). Variations of the overall structure of these substrates (Fig.…”

Section: Introductionmentioning

confidence: 99%

Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds

Hüttner

Klaubauf

Vries

et al. 2017

Appl Microbiol Biotechnol

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“…Recently, Biely et al . confirmed GE activity on the polymeric substrate glucuronoxylan‐methyl‐ester using 1 H NMR analysis. Improved corn fibre degradation has been observed when fungal GEs were added to commercial enzyme cocktails, thus demonstrating the auxiliary function of GEs in lignocellulose saccharification .…”

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confidence: 72%

“…The first characterized GE was produced by the wood‐rotting fungus Schizophyllum commune and at the present time nine GEs have been characterized for their activity and kinetics on different model substrates .…”

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confidence: 99%

A glucuronoyl esterase from Acremonium alcalophilum cleaves native lignin‐carbohydrate ester bonds

et al. 2016

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Edited by Ulf-Ingo Fl€ uggeThe Glucuronoyl esterases (GE) have been proposed to target lignin-carbohydrate (LC) ester bonds between lignin moieties and glucuronic acid side groups of xylan, but to date, no direct observations of enzymatic cleavage on native LC ester bonds have been demonstrated. In the present investigation, LCC fractions from spruce and birch were treated with a recombinantly produced GE originating from Acremonium alcalophilum (AaGE1). A combination of size exclusion chromatography and 31 P NMR analyses of phosphitylated LCC samples, before and after AaGE1 treatment provided the first evidence for cleavage of the LC ester linkages existing in wood.Keywords: 31 P NMR; carbohydrate esterase; lignin-carbohydrate complexes; size exclusion chromatography; spruce and birch An obstacle to intact and efficient extraction of the wood polymers cellulose, hemicelluloses and lignin may be the proposed chemical linkages connecting lignin with hemicelluloses, the so-called lignin-carbohydrate complexes (LCCs). In a lignocellulose-based biorefinery context it is therefore of interest to find mild methods, for example, enzymatic treatment, that specifically would break these lignin-carbohydrate (LC) linkages. Three types of existing covalent LC bonds have been suggested, namely benzyl ether-, ester-and phenyl glycosidic linkages [1]. The first described and most studied LC ester bond is the benzyl a-ester bond [2]. However, several more recent studies have also shown the presence of c-esters [3,4], suggested to arise due to uronosyl migrations of the linkage from the a-to the c-position [5,6].It has been proposed that glucuronoyl esterases (GE), members of the recently discovered carbohydrate esterase 15 family (CE15), could be used to target the LC ester bond between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid residues of glucuronoxylans ( Fig. 1) [7,8].The first characterized GE was produced by the wood-rotting fungus Schizophyllum commune [7] and at the present time nine GEs have been characterized for their activity and kinetics on different model substrates [7][8][9][10][11][12][13][14][15][16][17][18][19][20].Cleavage of model substrates mimicking LC ester bonds has been investigated for a wide range of esters. Studies have covered simple glucuronic acid (GlcA) esters with the 'lignin moiety' being single arylalkyl units at the c-position [8,10] or at the a-position [14].

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“…2) (22). The de-esterification of this substrate by GEs can easily be followed by 1 H-nuclear magnetic resonance ( 1 H-NMR) spectroscopy (22). The GE-catalyzed hydrolysis of synthetic sub-…”

Section: Structure and Proposed Mode Of Actionmentioning

confidence: 99%

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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Glucuronoyl esterases are active on the polymeric substrate methyl esterified glucuronoxylan

Cited by 28 publications

References 33 publications

Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds

Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds

A glucuronoyl esterase from Acremonium alcalophilum cleaves native lignin‐carbohydrate ester bonds

Microbial Glucuronoyl Esterases: 10 Years after Discovery

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