Tandem mass spectrometric analysis of Aspergillus niger pectin methylesterase: mode of action on fully methyl-esterified oligogalacturonates

Kester, H.C.M.; Benen, J.A.E.; Visser, Jaap; Warren, Maria; Orlando, Ron; Bergmann, Carl; Magaud, Didier; Anker, D.; Doutheau, Alain

doi:10.1042/0264-6021:3460469

Cited by 12 publications

(11 citation statements)

References 10 publications

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“…The genome of T. reesei encodes one CE family 15 glucuronoyl esterase [JGI:123940], also known as CIP2, which contains a cellulose binding module (CBM1) and which plays an important role in dissociating lignin from hemicelluloses through targeting the ester bonds between the aromatic alcohols of lignin and the glucuronic acid residues from the xylose backbone in hemicelluloses [29]. CE families 8 and 12 are present in A. niger but not in T. reesei [18,25] and the genome of A. niger encodes 3 CE family 8 pectin methylesterases involved in the de-esterification of pectin [30], and two CE family 12 rhamnogalacturonan acetylesterases involved in the deconstruction of plant cell wall pectin [31]. …”

Section: Resultsmentioning

confidence: 99%

Genome-wide transcriptional response of Trichoderma reesei to lignocellulose using RNA sequencing and comparison with Aspergillus niger

et al. 2013

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BackgroundA major part of second generation biofuel production is the enzymatic saccharification of lignocellulosic biomass into fermentable sugars. Many fungi produce enzymes that can saccarify lignocellulose and cocktails from several fungi, including well-studied species such as Trichoderma reesei and Aspergillus niger, are available commercially for this process. Such commercially-available enzyme cocktails are not necessarily representative of the array of enzymes used by the fungi themselves when faced with a complex lignocellulosic material. The global induction of genes in response to exposure of T. reesei to wheat straw was explored using RNA-seq and compared to published RNA-seq data and model of how A. niger senses and responds to wheat straw.ResultsIn T. reesei, levels of transcript that encode known and predicted cell-wall degrading enzymes were very high after 24 h exposure to straw (approximately 13% of the total mRNA) but were less than recorded in A. niger (approximately 19% of the total mRNA). Closer analysis revealed that enzymes from the same glycoside hydrolase families but different carbohydrate esterase and polysaccharide lyase families were up-regulated in both organisms. Accessory proteins which have been hypothesised to possibly have a role in enhancing carbohydrate deconstruction in A. niger were also uncovered in T. reesei and categories of enzymes induced were in general similar to those in A. niger. Similarly to A. niger, antisense transcripts are present in T. reesei and their expression is regulated by the growth condition.ConclusionsT. reesei uses a similar array of enzymes, for the deconstruction of a solid lignocellulosic substrate, to A. niger. This suggests a conserved strategy towards lignocellulose degradation in both saprobic fungi. This study provides a basis for further analysis and characterisation of genes shown to be highly induced in the presence of a lignocellulosic substrate. The data will help to elucidate the mechanism of solid substrate recognition and subsequent degradation by T. reesei and provide information which could prove useful for efficient production of second generation biofuels.

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Section: Resultsmentioning

confidence: 99%

Genome-wide transcriptional response of Trichoderma reesei to lignocellulose using RNA sequencing and comparison with Aspergillus niger

et al. 2013

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“…whereas plant PMEs and the Erwinia PME remove blocks of methyl groups on a single chain [13][14][15][16][17]. However, PME action on (highly) methylated pectins does not result in complete deesterification [6].…”

Section: Introductionmentioning

confidence: 99%

Partially esterified oligogalacturonides are the preferred substrates for pectin methylesterase of Aspergillus niger

Alebeek

Scherpenzeel

Beldman

et al. 2003

Biochemical Journal

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Investigations on the mode of action of Aspergillus niger pectin methylesterase (PME) towards differently C(6)- and C(1)-substituted oligogalacturonides (oligoGal p A) are described. De-esterification of methyl-esterified (un)saturated oligoGal p A proceeds via a specific pattern, depending on the degree of polymerization. Initially, a first methyl ester of the oligomer is hydrolysed, resulting in one free carboxyl group. Subsequently, this first product is preferred as a substrate and is de-esterified for a second time. This product is then accumulated and hereafter de-esterified further to the final product, i.e. oligoGal p A containing one methyl ester located at the non-reducing end residue for both saturated and unsaturated oligoGal p A, as found by post-source decay matrix-assisted laser-desorption/ionization-time-of-flight MS. The saturated hexamer is an exception to this: three methyl esters are removed very rapidly, instead of two methyl esters. When unsaturated oligoGal p A were used, the formation of the end product differed slightly, suggesting that the unsaturated bond at the non-reducing end influences the de-esterification process. In vivo, PME prefers methyl esters, but the enzyme appeared to be tolerant for other C(6)- and C(1)-substituents. Changing the type of ester (ethyl esterification) or addition of a methyl glycoside (C(1)) only reduced the activity or had no effect respectively. The specific product pattern was identical for all methyl- and ethyl-esterified oligoGal p A and methyl-glycosidated oligoGal p A, which strongly indicates that one or perhaps two non-esterified oligoGal p A are preferred in the active-site cleft.

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“…In general, most fungal PMEs have optimal pH values between 4 and 6. PMEs randomly attack the methyl groups on the pectin molecules resulting in a random distribution of the nonmethylated GalpA (D-galacturonic acid) residues (Dongowski & Bock 1984;Kester et al 2000;Benen et al 2002).…”

Section: Introductionmentioning

confidence: 98%

Purification and partial characterisation of pectin methylesterase produced by Fusarium asiaticum

Glinka

Liao

2011

Fungal Biology

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Tandem mass spectrometric analysis of Aspergillus niger pectin methylesterase: mode of action on fully methyl-esterified oligogalacturonates

Cited by 12 publications

References 10 publications

Genome-wide transcriptional response of Trichoderma reesei to lignocellulose using RNA sequencing and comparison with Aspergillus niger

Genome-wide transcriptional response of Trichoderma reesei to lignocellulose using RNA sequencing and comparison with Aspergillus niger

Partially esterified oligogalacturonides are the preferred substrates for pectin methylesterase of Aspergillus niger

Purification and partial characterisation of pectin methylesterase produced by Fusarium asiaticum

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