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Arabinoxylan (Wheat Flour; Insoluble)

Arabinoxylan Wheat Flour Insoluble P-WAXYI
Product code: P-WAXYI

5 g

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Content: 5 g
Shipping Temperature: Ambient
Storage Temperature: Ambient
Physical Form: Powder
Stability: > 2 years under recommended storage conditions
CAS Number: 9040-27-1
Source: Wheat
Purity: > 90%
Monosaccharides (%): Arabinose: Xylose: Glucose: Mannose: Galactose = 33.5: 62: 1.5: 2: 1
Main Chain Glycosidic Linkage: β-1,4
Substrate For (Enzyme): endo-1,4-β-Xylanase

High purity Arabinoxylan (Wheat Flour; Insoluble) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

Carefully extracted and purified to maintain the ferulic acid crosslinks in the native arabinoxylan. Treated to remove starch, β-glucan and protein.

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Megazyme publication
Novel substrates for the automated and manual assay of endo-1,4-β-xylanase.

Mangan, D., Cornaggia, C., Liadova, A., McCormack, N., Ivory, R., McKie, V. A., Ormerod, A. & McCleary, D. V. (2017). Carbohydrate Research, 445, 14-22.

endo-1,4-β-Xylanase (EC is employed across a broad range of industries including animal feed, brewing, baking, biofuels, detergents and pulp (paper). Despite its importance, a rapid, reliable, reproducible, automatable assay for this enzyme that is based on the use of a chemically defined substrate has not been described to date. Reported herein is a new enzyme coupled assay procedure, termed the XylX6 assay, that employs a novel substrate, namely 4,6-O-(3-ketobutylidene)-4-nitrophenyl-β-45-O-glucosyl-xylopentaoside. The development of the substrate and associated assay is discussed here and the relationship between the activity values obtained with the XylX6 assay versus traditional reducing sugar assays and its specificity and reproducibility were thoroughly investigated.

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Megazyme publication
Hydrolysis of wheat flour arabinoxylan, acid-debranched wheat flour arabinoxylan and arabino-xylo-oligosaccharides by β-xylanase, α-L-arabinofuranosidase and β-xylosidase.

McCleary, B. V., McKie, V. A., Draga, A., Rooney, E., Mangan, D. & Larkin, J. (2015). Carbohydrate Research, 407, 79-96.

A range of α-L-arabinofuranosyl-(1-4)-β-D-xylo-oligosaccharides (AXOS) were produced by hydrolysis of wheat flour arabinoxylan (WAX) and acid debranched arabinoxylan (ADWAX), in the presence and absence of an AXH-d3 α-L-arabinofuranosidase, by several GH10 and GH11 β-xylanases. The structures of the oligosaccharides were characterised by GC-MS and NMR and by hydrolysis by a range of α-L-arabinofuranosidases and β-xylosidase. The AXOS were purified and used to characterise the action patterns of the specific α-L-arabinofuranosidases. These enzymes, in combination with either Cellvibrio mixtus or Neocallimastix patriciarum β -xylanase, were used to produce elevated levels of specific AXOS on hydrolysis of WAX, such as 32-α-L-Araf-(1-4)-β-D-xylobiose (A3X), 23-α-L-Araf-(1-4)-β-D-xylotriose (A2XX), 33-α-L-Araf-(1-4)-β-D-xylotriose (A3XX), 22-α-L-Araf-(1-4)-β-D-xylotriose (XA2X), 32-α-L-Araf (1-4)-β-D-xylotriose (XA3X), 23-α-L-Araf-(1-4)-β-D-xylotetraose (XA2XX), 33-α-L-Araf-(1-4)-β-D-xylotetraose (XA3XX), 23 ,33-di-α-L-Araf-(1-4)-β-D-xylotriose (A2+3XX), 23,33-di-α-L-Araf-(1-4)-β-D-xylotetraose (XA2+3XX), 24,34-di-α-L-Araf-(1-4)-β-D-xylopentaose (XA2+3XXX) and 33,34-di-α-L-Araf-(1-4)-β-D-xylopentaose (XA3A3XX), many of which have not previously been produced in sufficient quantities to allow their use as substrates in further enzymic studies. For A2,3XX, yields of approximately 16% of the starting material (wheat arabinoxylan) have been achieved. Mixtures of the α-L-arabinofuranosidases, with specific action on AXOS, have been combined with β-xylosidase and β-xylanase to obtain an optimal mixture for hydrolysis of arabinoxylan to L-arabinose and D-xylose.

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Glycoside Hydrolase family 30 harbors fungal subfamilies with distinct polysaccharide specificities.

Li, X., Kouzounis, D., Kabel, M. A., de Vries, R. P. & Dilokpimol, A. (2022). New biotechnology, 67, 32-41.

Efficient bioconversion of agro-industrial side streams requires a wide range of enzyme activities. Glycoside Hydrolase family 30 (GH30) is a diverse family that contains various catalytic functions and has so far been divided into ten subfamilies (GH30_1-10). In this study, a GH30 phylogenetic tree using over 150 amino acid sequences was contructed. The members of GH30 cluster into four subfamilies and eleven candidates from these subfamilies were selected for biochemical characterization. Novel enzyme activities were identified in GH30. GH30_3 enzymes possess β-(1→6)-glucanase activity. GH30_5 targets β-(1→6)-galactan with mainly β-(1→6)-galactobiohydrolase catalytic behavior. β-(1→4)-Xylanolytic enzymes belong to GH30_7 targeting β-(1→4)-xylan with several activities (e.g. xylobiohydrolase, endoxylanase). Additionally, a new fungal subfamily in GH30 was proposed, i.e. GH30_11, which displays β-(1→6)-galactobiohydrolase. This study confirmed that GH30 fungal subfamilies harbor distinct polysaccharide specificity and have high potential for the production of short (non-digestible) di- and oligosaccharides.

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Activity of an Endo‐1, 4‐β‐xylanase from Wheat Malt towards Water Unextractable Arabinoxylan Derived from Wheat.

Peng, Z. & Jin, Y. (2021). Journal of the Science of Food and Agriculture, In Press.

Background: Non-starch polysaccharides in wheat are dominated by arabinoxylan (AX). Endo-1,4-β-xylanase (EC is the most important enzyme for degrading AX. This paper investigated the ability of endo-1,4-β-xylanase extracted from wheat malt to degrade non-water-extractable wheat-derived arabinoxylan (WUAX). Results: The enzyme was observed to break down wheat-derived WUAX effectively, substantially increasing the concentration of water-extractable arabinoxylan (WEAX) in the system for up to 6 h. A considerable quantity of arabinose xylooligosaccharide (AXOS) was also produced, suggesting that the enzyme could produce oligosaccharides too. The molecular weight of the product WEAX was between 23 and 27 kDa and the content of oligosaccharides changed with degradation time. This suggests that endo-1,4-β-xylanase can not only degrade WUAX into WEAX and xylooligosaccharides but can also degrade the xylooligosaccharides with larger molecular weights into xylobiose and xylotriose. The viscosity of the degradation product increased significantly in the first 2 h, then decreased with longer degradation times. The concentration of WEAX in the reaction system increased throughout the reaction but at gradually lower rates, indicating that the endo-1,4-β-xylanase degraded WEAX better than it degraded WUAX. Rheological tests showed that solutions prepared from the WEAX that was produced had properties of a pseudoplastic fluid. Conclusion: The results showed that the wheat malt endo-1,4-β-xylanase, which we had previously tested on WEAX, was also effective in degrading wheat-derived WUAX. This study can therefore provide a theoretical basis for the subsequent role of the enzyme in other sources of xylan, and provide guidance for the quality control of beer in the brewing process.

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Feruloyl esterase (FAE-1) sourced from a termite hindgut and GH10 xylanases synergy improves degradation of arabinoxylan.

Mafa, M. S., Malgas, S. & Pletschke, B. I. (2021). AMB Express, 11(1), 1-9.

Cereal feedstocks have high arabinoxylan content as their main hemicellulose, which is linked to lignin by hydroxycinnamic acids such as ferulic acid. The ferulic acid is linked to arabinoxylan by ester bonds, and generally, the high substitution of ferulic acid leads to a loss of activity of xylanases targeting the arabinoxylan. In the current study, a feruloyl esterase (FAE-1) from a termite hindgut bacteria was functionally characterised and used in synergy with xylanases during xylan hydrolysis. The FAE-1 displayed temperature and pH optima of 60℃ and 7.0, respectively. FAE-1 did not release reducing sugars from beechwood xylan (BWX), wheat arabinoxylan (WAX) and oat spelt xylan (OX), however, displayed high activity of 164.74 U/mg protein on p-nitrophenyl-acetate (pNPA). In contrast, the GH10 xylanases; Xyn10 and XT6, and a GH11 xylanase, Xyn2A, showed more than two-fold increased activity on xylan substrates with low sidechain substitutions; BWX and OX, compared to the highly branched substrate, WAX. Interestingly, the FAE-1 and GH10 xylanases (Xyn10D and XT6) displayed a degree of synergy (DS) that was higher than 1 in all enzyme loading combinations during WAX hydrolysis. The 75%XT6:25%FAE-1 synergistic enzyme combination increased the release of reducing sugars by 1.34-fold from WAX compared to the control, while 25%Xyn10D:75%FAE-1 synergistic combination released about 2.1-fold of reducing sugars from WAX compared to controls. These findings suggest that FAE-1 can be used in concert with xylanases, particularly those from GH10, to efficiently degrade arabinoxylans contained in cereal feedstocks for various industrial settings such as in animal feeds and baking.

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Role of (1,3)(1,4) β-glucan in cell walls: Interaction with cellulose.

Kiemle, S. N., Zhang, X., Esker, A. R., Toriz, G., Gatenholm, P. & Cosgrove, D. J. (2014). Biomacromolecules, 15 (5), 1727-1736.

(1,3)(1,4)-β-D-Glucan (mixed-linkage glucan or MLG), a characteristic hemicellulose in primary cell walls of grasses, was investigated to determine both its role in cell walls and its interaction with cellulose and other cell wall polysaccharides in vitro. Binding isotherms showed that MLG adsorption onto microcrystalline cellulose is slow, irreversible, and temperature-dependent. Measurements using quartz crystal microbalance with dissipation monitoring showed that MLG adsorbed irreversibly onto amorphous regenerated cellulose, forming a thick hydrogel. Oligosaccharide profiling using endo-(1,3)(1,4)-β-glucanase indicated that there was no difference in the frequency and distribution of (1,3) and (1,4) links in bound and unbound MLG. The binding of MLG to cellulose was reduced if the cellulose samples were first treated with certain cell wall polysaccharides, such as xyloglucan and glucuronoarabinoxylan. The tethering function of MLG in cell walls was tested by applying endo-(1,3)(1,4)-β-glucanase to wall samples in a constant force extensometer. Cell wall extension was not induced, which indicates that enzyme-accessible MLG does not tether cellulose fibrils into a load-bearing network.

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Adsorption of β-glucosidases in two commercial preparations onto pretreated biomass and lignin.

Haven, M. Ø. & Jørgensen, H. (2013). Biotechnology for Biofuels, 6(1), 165.

Background: Enzyme recycling is a method to reduce the production costs for advanced bioethanol by lowering the overall use of enzymes. Commercial cellulase preparations consist of many different enzymes that are important for efficient and complete cellulose (and hemicellulose) hydrolysis. This abundance of different activities complicates enzyme recycling since the individual enzymes behave differently in the process. Previously, the general perception was that β-glucosidases could easily be recycled via the liquid phase, as they have mostly been observed not to adsorb to pretreated biomass or only adsorb to a minor extent. Results: The results from this study with Cellic® CTec2 revealed that the vast majority of the β-glucosidase activity was lost from the liquid phase and was adsorbed to the residual biomass during hydrolysis and fermentation. Adsorption studies with β-glucosidases in two commercial preparations (Novozym 188 and Cellic® CTec2) to substrates mimicking the components in pretreated wheat straw revealed that the Aspergillus niger β-glucosidase in Novozym 188 did not adsorb significantly to any of the components in pretreated wheat straw, whereas the β-glucosidase in Cellic® CTec2 adsorbed strongly to lignin. The extent of adsorption of β-glucosidase from Cellic® CTec2 was affected by both type of biomass and pretreatment method. With approximately 65% of the β-glucosidases from Cellic® CTec2 adsorbed onto lignin from pretreated wheat straw, the activity of the β-glucosidases in the slurry decreased by only 15%. This demonstrated that some enzyme remained active despite being bound. It was possible to reduce the adsorption of Cellic® CTec2 β-glucosidase to lignin from pretreated wheat straw by addition of bovine serum albumin or poly(ethylene glycol). Conclusions: Contrary to the β-glucosidases in Novozym 188, the β-glucosidases in Cellic® CTec2 adsorb significantly to lignin. The lignin adsorption observed for Cellic® CTec2 is usually not a problem during hydrolysis and fermentation since most of the catalytic activity is retained. However, adsorption of β-glucosidases to lignin may prove to be a problem when trying to recycle enzymes in the production of advanced bioethanol.

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A novel thermophilic xylanase from Achaetomium sp. Xz-8 with high catalytic efficiency and application potentials in the brewing and other industries.

Zhao, L., Meng, K., Shi, P., Bai, Y., Luo, H., Huang, H., Wang, Y., Yang, P. & Yao, B. (2013). Process Biochemistry, 48(12), 1879-1885.

Thermophilic xylanases are of great interest for their wide industrial application prospects. Here we identified a thermophilic xylanase (XynC01) of glycoside hydrolase (GH) family 10 in a thermophilic fungal strain Achaetomium sp. Xz-8. The deduced amino acids of XynC01 showed the highest identity of ≤52% to experimentally verified xylanases. XynC01 was functionally expressed in Pichia pastoris, showed optimal activity at pH 5.5 and 75°C with stability over a broad pH range (pH 4.0–10.0) and at temperatures of 55°C and below. XynC01 had the highest catalytic efficiency (kcat/Km, 3710 mL/s/mg) ever reported for all GH 10 xylanases, and was resistant to all tested metal ions and chemical reagents. Its hydrolysis products of various xylans were simple, mainly consisting of xylobiose and xylose. Under simulated mashing conditions, XynC01 alone had a comparable effect on filtration improvement with Ultraflo from Novozymes (20.24% vs. 20.71%), and showed better performance when combined with a commercial β-glucanase (38.50%). Combining all excellent properties described above, XynC01 may find diverse applications in industrial fields, especially in the brewing industry.

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Plant pathogens as a source of diverse enzymes for lignocellulose digestion.

Gibson, D. M., King, B. C., Hayes, M. L. & Bergstrom, G. C. (2011). Current Opinion in Microbiology, 14(3), 264-270.

The plant cell wall is a major barrier that many plant pathogens must surmount for successful invasion of their plant hosts. Full genome sequencing of a number of plant pathogens has revealed often large, complex, and redundant enzyme systems for degradation of plant cell walls. Recent surveys have noted that plant pathogenic fungi are highly competent producers of lignocellulolytic enzymes, and their enzyme activity patterns reflect host specificity. We propose that plant pathogens may contribute to biofuel production as diverse sources of accessory enzymes for more efficient conversion of lignocellulose into fermentable sugars.

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Arsenal of plant cell wall degrading enzymes reflects host preference among plant pathogenic fungi.

King, B. C., Waxman, K. D., Nenni, N. V., Walker, L. P., Bergstrom, G. C. & Gibson, D. M. (2011). Biotechnol Biofuels, 4(4).

Background: The discovery and development of novel plant cell wall degrading enzymes is a key step towards more efficient depolymerization of polysaccharides to fermentable sugars for the production of liquid transportation biofuels and other bioproducts. The industrial fungus Trichoderma reesei is known to be highly cellulolytic and is a major industrial microbial source for commercial cellulases, xylanases and other cell wall degrading enzymes. However, enzyme-prospecting research continues to identify opportunities to enhance the activity of T. reesei enzyme preparations by supplementing with enzymatic diversity from other microbes. The goal of this study was to evaluate the enzymatic potential of a broad range of plant pathogenic and non-pathogenic fungi for their ability to degrade plant biomass and isolated polysaccharides. Results: Large-scale screening identified a range of hydrolytic activities among 348 unique isolates representing 156 species of plant pathogenic and non-pathogenic fungi. Hierarchical clustering was used to identify groups of species with similar hydrolytic profiles. Among moderately and highly active species, plant pathogenic species were found to be more active than non-pathogens on six of eight substrates tested, with no significant difference seen on the other two substrates. Among the pathogenic fungi, greater hydrolysis was seen when they were tested on biomass and hemicellulose derived from their host plants (commelinoid monocot or dicot). Although T. reesei has a hydrolytic profile that is highly active on cellulose and pretreated biomass, it was less active than some natural isolates of fungi when tested on xylans and untreated biomass. Conclusions: Several highly active isolates of plant pathogenic fungi were identified, particularly when tested on xylans and untreated biomass. There were statistically significant preferences for biomass type reflecting the monocot or dicot host preference of the pathogen tested. These highly active fungi are promising targets for identification and characterization of novel cell wall degrading enzymes for industrial applications.

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