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Xyloglucanase (GH5) (Paenibacillus sp.)

Product code: E-XEGP
€191.00

3,000 Units

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Content: 3,000 Units
Shipping Temperature: Ambient
Storage Temperature: 2-8oC
Formulation: In 3.2 M ammonium sulphate
Physical Form: Suspension
Stability: > 1 year under recommended storage conditions
Enzyme Activity: Xyloglucanase
EC Number: 3.2.1.151
CAZy Family: GH5
CAS Number: 76901-10-5
Synonyms: xyloglucan-specific endo-beta-1,4-glucanase; [(1→6)-alpha-D-xylo]-(1→4)-beta-D-glucan glucanohydrolase
Source: Paenibacillus sp.
Molecular Weight: 42,300
Concentration: Supplied at ~ 1,000 U/mL
Expression: Recombinant from Paenibacillus sp.
Specificity: endo-hydrolysis of 1,4-β-D-glucosidic linkages in xyloglucan.
Specific Activity: ~ 78 U/mg (40oC, pH 5.5 on tamarind xyloglucan)
Unit Definition: One Unit of xyloglucanase activity is defined as the amount of enzyme required to release one µmole of glucose reducing-sugar equivalents per minute from xyloglucan (5 mg/mL) in sodium acetate buffer (100 mM), pH 5.5 at 40oC.
Temperature Optima: 50oC
pH Optima: 5.5
Application examples: Applications in carbohydrate and biofuels research.

High purity recombinant Xyloglucanase (GH5) (Paenibacillus sp.) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

See other related CAZy enzymes.

Documents
Certificate of Analysis
Safety Data Sheet
Data Sheet
Publications
Publication

Transcellular progression of infection threads in Medicago truncatula roots is controlled by locally confined cell wall modifications.

Su, C., Zhang, G., Rodriguez-Franco, M., Wietschorke, J., Liang, P., Yang, W., Uhler, L., Li, X. & Ott, T. (2022). BioRxiv, 2022-07.

The root nodule symbiosis with its global impact on nitrogen fertilization of soils is characterized by an intracellular colonization of legume roots by rhizobia. Although the symbionts are initially taken up by morphologically adapted root hairs, rhizobia persistently progress within a membrane-confined infection thread through several root cortical and later nodular cell layers. Throughout this transcellular passaging, rhizobia have to repeatedly pass host plasma membranes and cell walls. Here, we investigated this essential process and describe the concerted action of one of the symbiosis-specific pectin methyl esterases (SyPME1) and the nodulation pectate lyase (NPL) at the infection thread and transcellular passage sites. Their coordinated function mediates spatially confined pectin alterations in the cell-cell interface that result in the establishment of an apoplastic compartment where bacteria are temporarily released into and taken up from the subjacent cell. This process allows successful intracellular progression of infection threads through the entire root cortical tissue.

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Publication

Structures of the xyloglucans in the monocotyledon family Araceae (aroids).

Hsiung, S. Y., Li, J., Imre, B., Kao, M. R., Liao, H. C., Wang, D., Chen, C. C., Liang, P. H., Harris, P. J. & Hsieh, Y. S. (2023). Planta, 257(2), 39.

The aquatic Araceae species Lemna minor was earlier shown to have xyloglucans with a different structure from the fucogalactoxyloglucans of other non-commelinid monocotyledons. We investigated 26 Araceae species (including L. minor), from five of the seven subfamilies. All seven aquatic species examined had xyloglucans that were unusual in having one or two of three features: < 77% XXXG core motif [L. minor (Lemnoideae) and Orontium aquaticum (Orontioideae)]; no fucosylation [L. minor (Lemnoideae), Cryptocoryne aponogetonifolia, and Lagenandra ovata (Aroideae, Rheophytes clade)]; and > 14% oligosaccharide units with S or D side chains [Spirodela polyrhiza and Landoltia punctata (Lemnoideae) and Pistia stratiotes (Aroideae, Dracunculus clade)]. Orontioideae and Lemnoideae are the two most basal subfamilies, with all species being aquatic, and Aroideae is the most derived. Two terrestrial species [Dieffenbachia seguine and Spathicarpa hastifolia (Aroideae, Zantedeschia clade)] also had xyloglucans without fucose indicating this feature was not unique to aquatic species.

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Publication

Conservation of endo-glucanase 16 (EG16) activity across highly divergent plant lineages.

Behar, H., Tamura, K., Wagner, E. R., Cosgrove, D. J., & Brumer, H. (2021). Biochemical Journal, 478(16), 3063-3078.

Plant cell walls are highly dynamic structures that are composed predominately of polysaccharides. As such, endogenous carbohydrate active enzymes (CAZymes) are central to the synthesis and subsequent modification of plant cells during morphogenesis. The endo-glucanase 16 (EG16) members constitute a distinct group of plant CAZymes, angiosperm orthologs of which were recently shown to have dual β-glucan/xyloglucan hydrolase activity. Molecular phylogeny indicates that EG16 members comprise a sister clade with a deep evolutionary relationship to the widely studied apoplastic xyloglucan endo-transglycosylases/hydrolases (XTH). A cross-genome survey indicated that EG16 members occur as a single ortholog across species and are widespread in early diverging plants, including the non-vascular bryophytes, for which functional data were previously lacking. Remarkably, enzymological characterization of an EG16 ortholog from the model moss Physcomitrella patens (PpEG16) revealed that EG16 activity and sequence/structure are highly conserved across 500 million years of plant evolution, vis-à-vis orthologs from grapevine and poplar. Ex vivo biomechanical assays demonstrated that the application of EG16 gene products caused abrupt breakage of etiolated hypocotyls rather than slow extension, thereby indicating a mode-of-action distinct from endogenous expansins and microbial endo-glucanases. The biochemical data presented here will inform future genomic, genetic, and physiological studies of EG16 enzymes.

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Publication

Ancient origin of fucosylated xyloglucan in charophycean green algae.

Mikkelsen, M. D., Harholt, J., Westereng, B., Domozych, D., Fry, S. C., Johansen, I. E., Fangel, J. U., Lęzyk, M., Tao Feng, T., Nancke, L., Mikkelsen, J. D., William G. T. Willats, W. G. T. & Ulvskov , P. (2021). Communications Biology, 4(1), 1-12.

The charophycean green algae (CGA or basal streptophytes) are of particular evolutionary significance because their ancestors gave rise to land plants. One outstanding feature of these algae is that their cell walls exhibit remarkable similarities to those of land plants. Xyloglucan (XyG) is a major structural component of the cell walls of most land plants and was originally thought to be absent in CGA. This study presents evidence that XyG evolved in the CGA. This is based on a) the identification of orthologs of the genetic machinery to produce XyG, b) the identification of XyG in a range of CGA and, c) the structural elucidation of XyG, including uronic acid-containing XyG, in selected CGA. Most notably, XyG fucosylation, a feature considered as a late evolutionary elaboration of the basic XyG structure and orthologs to the corresponding biosynthetic enzymes are shown to be present in Mesotaenium caldariorum.

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Publication

Configuration of active site segments in lytic polysaccharide monooxygenases steers oxidative xyloglucan degradation.

Sun, P., Laurent, C. V., Scheiblbrandner, S., Frommhagen, M., Kouzounis, D., Sanders, M. G., van Berkel, W. J. H., Ludwig, R. & Kabel, M. A. (2020). Biotechnology for Biofuels, 13, 1-19.

This study investigated pilot-scale production of xylo-oligosaccharides (XOS) and fermentable sugars from Miscanthus using steam explosion (SE) pretreatment. SE conditions (200°C; 15 bar; 10 min) led to XOS yields up to 52 % (w/w of initial xylan) in the hydrolysate. Liquid chromatography-mass spectrometry demonstrated that the solubilised XOS contained bound acetyl- and hydroxycinnamate residues, physicochemical properties known for high prebiotic effects and anti-oxidant activity in nutraceutical foods. Enzymatic hydrolysis of XOS-rich hydrolysate with commercial endo-xylanases resulted in xylobiose yields of 380 to 500 g/kg of initial xylan in the biomass after only 4 h, equivalent to ~74 to 90 % conversion of XOS into xylobiose. Fermentable glucose yields from enzymatic hydrolysis of solid residues were 8 to 9-fold higher than for untreated material. In view of an integrated biorefinery, we demonstrate the potential for efficient utilisation of Miscanthus for the production of renewable sources, including biochemicals and biofuels.

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Publication

An amendment to the fine structure of galactoxyloglucan from Tamarind (Tamarindus indica L.) seed.

Zhang, H., Zhao, T., Wang, J., Xia, Y., Song, Z. & Ai, L. (2020). International Journal of Biological Macromolecules, 149, 1189-1197.

A polysaccharide from tamarind seeds (TSP) was characterized in terms of backbone and side chain structural features, as well as conformational property using methylation and GC–MS analysis, 2D NMR, MALDI-TOF MS, and high performance size exclusion chromatography (HPSEC). Results showed that TSP was a galactoxyloglucan (GXG) consisting of glucose, xylose, and galactose in a molar ratio of 3.1: 1.7: 1.0. The Mw was determined to be 524.0 kDa with radius of gyration (Rg) of 55.6 nm. The chemical structure was confirmed as a classical β-(1 → 4)-glucan with short side chains of T-β-Galp-(1 → 2)-α-Xylp-(1 → and T-α-Xylp-(1 → attached to O-6 position of glucose. MALDI-TOF MS analysis indicated that TSP mainly composed of nonasaccharide (XLLG) and octasaccharide (XLXG or XXLG) blocks in periodic or interrupted sequence in a ratio of 3: 2, occasionally interrupted by heptasaccharide (XXXG), hexasaccharide (XLG or XXGG), or even hendesaccharide blocks. Conformational study indicated that TSP was in a random-coil shape with relative extended stiff chain in aqueous solution. This study provided more evidences to make an amendment to the fine structure of tamarind GXG.

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Publication
Xyloglucan Fucosylation Modulates Arabidopsis Cell Wall Hemicellulose Aluminium binding Capacity.

Wan, J. X., Zhu, X. F., Wang, Y. Q., Liu, L. Y., Zhang, B. C., Li, G. X., Zhou, Y. H. & Zheng, S. J. (2018). Scientific Reports, 8(1), 428.

Although xyloglucan (XyG) is reported to bind Aluminium (Al), the influence of XyG fucosylation on the cell wall Al binding capacity and plant Al stress responses is unclear. We show that Arabidopsis T-DNA insertion mutants with reduced AXY3 (XYLOSIDASE1) function and consequent reduced levels of fucosylated XyG are more sensitive to Al than wild-type Col-0 (WT). In contrast, T-DNA insertion mutants with reduced AXY8 (FUC95A) function and consequent increased levels of fucosylated XyG are more Al resistant. AXY3 transcript levels are strongly down regulated in response to 30 min Al treatment, whilst AXY8 transcript levels also repressed until 6 h following treatment onset. Mutants lacking AXY3 or AXY8 function exhibit opposing effects on Al contents of root cell wall and cell wall hemicellulose components. However, there was no difference in the amount of Al retained in the pectin components between mutants and WT. Finally, whilst the total sugar content of the hemicellulose fraction did not change, the altered hemicellulose Al content of the mutants is shown to be a likely consequence of their different XyG fucosylation levels. We conclude that variation in XyG fucosylation levels influences the Al sensitivity of Arabidopsis by affecting the Al-binding capacity of hemicellulose.

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Publication
Methods for Xyloglucan Structure Analysis in Brachypodium distachyon.

Liu, L. (2017). Brachypodium Genomics, Humana Press, New York, NY, 65-71.

Matrix-assisted laser desorption-ionization time-of-flight mass spectrometry (MALDI-TOF MS) has become an important tool for the analysis of biomolecules, such as DNA, peptides, and oligosaccharides. This technique has been developed as a rapid, sensitive, and accurate means for analyzing cell wall polysaccharide structures. Here, we describe a method using mass spectrometry to provide xyloglucan composition and structure information of Brachypodium plants which will be useful for functional characterization of xyloglucan biosynthesis pathway in Brachypodium distachyon.

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Publication
Recognition of xyloglucan by the crystalline cellulose‐binding site of a family 3a carbohydrate‐binding module.

Hernandez-Gomez, M. C., Rydahl, M. G., Rogowski, A., Morland, C., Cartmell, A., Crouch, L., Labourel, A., Fontes, C. M. G. A., Willats, W. G. T., Gilbert, H. J. & Knox, J. P. (2015). FEBS Letters, 589(18), 2297-2303.

Type A non-catalytic carbohydrate-binding modules (CBMs), exemplified by CtCBM3acipA, are widely believed to specifically target crystalline cellulose through entropic forces. Here we have tested the hypothesis that type A CBMs can also bind to xyloglucan (XG), a soluble β-1,4-glucan containing α-1,6-xylose side chains. CtCBM3acipA bound to xyloglucan in cell walls and arrayed on solid surfaces. Xyloglucan and cellulose were shown to bind to the same planar surface on CBM3acipA. A range of type A CBMs from different families were shown to bind to xyloglucan in solution with ligand binding driven by enthalpic changes. The nature of CBM-polysaccharide interactions is discussed.

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Publication
The synergistic action of accessory enzymes enhances the hydrolytic potential of a “cellulase mixture” but is highly substrate specific.

Hu, J., Arantes, V., Pribowo, A. & Saddler, J. N. (2013). Biotechnology for Biofuels, 6(1), 112.

Background: Currently, the amount of protein/enzyme required to achieve effective cellulose hydrolysis is still too high. One way to reduce the amount of protein/enzyme required is to formulate a more efficient enzyme cocktail by adding so-called accessory enzymes such as xylanase, lytic polysaccharide monooxygenase (AA9, formerly known as GH61), etc., to the cellulase mixture. Previous work has shown the strong synergism that can occur between cellulase and xylanase mixtures during the hydrolysis of steam pretreated corn stover, requiring lower protein loading to achieve effective hydrolysis. However, relatively high loadings of xylanases were required. When family 10 and 11 endo-xylanases and family 5 xyloglucanase were supplemented to a commercial cellulase mixture varying degrees of improved hydrolysis over a range of pretreated, lignocellulosic substrates were observed. Results: The potential synergistic interactions between cellulase monocomponents and hemicellulases from family 10 and 11 endo-xylanases (GH10 EX and GH11 EX) and family 5 xyloglucanase (GH5 XG), during hydrolysis of various steam pretreated lignocellulosic substrates, were assessed. It was apparent that the hydrolytic activity of cellulase monocomponents was enhanced by the addition of accessory enzymes although the “boosting” effect was highly substrate specific. The GH10 EX and GH5 XG both exhibited broad substrate specificity and showed strong synergistic interaction with the cellulases when added individually. The GH10 EX was more effective on steam pretreated agriculture residues and hardwood substrates whereas GH5 XG addition was more effective on softwood substrates. The synergistic interaction between GH10 EX and GH5 XG when added together further enhanced the hydrolytic activity of the cellulase enzymes over a range of pretreated lignocellulosic substrates. GH10 EX addition could also stimulate further cellulose hydrolysis when added to the hydrolysis reactions when the rate of hydrolysis had levelled off. Conclusions: Endo-xylanases and xyloglucanases interacted synergistically with cellulases to improve the hydrolysis of a range of pretreated lignocellulosic substrates. However, the extent of improved hydrolysis was highly substrate dependent. It appears that those accessory enzymes, such as GH10 EX and GH5 XG, with broader substrate specificities promoted the greatest improvements in the hydrolytic performance of the cellulase mixture on all of the pretreated biomass substrates.

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Safety Data Sheet
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