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endo-1,4-β-Xylanase M1 (Trichoderma viride)

Product code: E-XYTR1

8,000 Units

Prices exclude VAT

This product has been discontinued

Content: 8,000 Units
Shipping Temperature: Ambient
Storage Temperature: 2-8oC
Formulation: In 3.2 M ammonium sulphate
Physical Form: Suspension
Stability: > 4 years at 4oC
Enzyme Activity: endo-1,4-β-Xylanase
EC Number:
CAZy Family: GH11
CAS Number: 9025-57-4
Synonyms: endo-1,4-beta-xylanase; 4-beta-D-xylan xylanohydrolase
Source: Trichoderma viride
Molecular Weight: 20,500,
Concentration: Supplied at ~ 1,700 U/mL
Expression: Purified from Trichoderma viride
Specificity: endo-hydrolysis of (1,4)-β-D-xylosidic linkages in xylans.
Specific Activity: ~ 230 U/mg (40oC, pH 4.5 on wheat arabinoxylan)
Unit Definition: One Unit of xylanase activity is defined as the amount of enzyme required to release one µmole of xylose reducing-sugar equivalents per minute from wheat arabinoxylan (10 mg/mL) in sodium acetate buffer (100 mM), pH 4.5 at 40oC.
Temperature Optima: 50oC
pH Optima: 4.5
Application examples: Applications in carbohydrate and biofuels research and in the food and feeds and paper pulping industries.

This product has been discontinued (read more).

High purity endo-1,4-β-Xylanase M1 (Trichoderma viride) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

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Data Sheet
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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Megazyme publication
A Comparison of Polysaccharide Substrates and Reducing Sugar Methods for the Measurement of endo-1,4-β-Xylanase.

McCleary, B. V. & McGeough, P. (2015). Appl. Biochem. Biotechnol., 177(5), 1152-1163.

The most commonly used method for the measurement of the level of endo-xylanase in commercial enzyme preparations is the 3,5-dinitrosalicylic acid (DNS) reducing sugar method with birchwood xylan as substrate. It is well known that with the DNS method, much higher enzyme activity values are obtained than with the Nelson-Somogyi (NS) reducing sugar method. In this paper, we have compared the DNS and NS reducing sugar assays using a range of xylan-type substrates and accurately compared the molar response factors for xylose and a range of xylo-oligosaccharides. Purified beechwood xylan or wheat arabinoxylan is shown to be a suitable replacement for birchwood xylan which is no longer commercially available, and it is clearly demonstrated that the DNS method grossly overestimates endo-xylanase activity. Unlike the DNS assay, the NS assay gave the equivalent colour response with equimolar amounts of xylose, xylobiose, xylotriose and xylotetraose demonstrating that it accurately measures the quantity of glycosidic bonds cleaved by the endo-xylanase. The authors strongly recommend cessation of the use of the DNS assay for measurement of endo-xylanase due to the fact that the values obtained are grossly overestimated due to secondary reactions in colour development.

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Megazyme publication
A simple procedure for the large-scale purification of β-D-xylanase from Trichoderma viride.

Gibson, T. S. & McCleary, B. V. (1987). Carbohydrate Polymers, 7(3), 225- 240.

A simple procedure is described for the purification of gram quantities of β-D-xylanase from a commercially available Trichoderma viride culture filtrate. Chromatography of the crude extract on CM-Sepharose CL-6B gave two partially separated peaks of β-D-xylanase activity, and for convenience these have been termed xylanases I and II. Each has cellulase activity. The cellulase and xylanase activities were not separated by further purification on Ultrogel AcA 54 or Phenyl Sepharose CL-4B. Each of these xylanases was purified essentially to homogeneity (by the criterion of isoelectric focusing) and was free of protease, amylase and glycosidase activities. Physical and kinetic properties of xylanases I and II were identical, indicating that the separation of CM-Sepharose CL-6B may simply have been an artefact of chromatography. However, this pattern was reproducible, being obtained on several occasions. Each enzyme separated into two protein bands on isoelectric focusing. The major band had a pI of 8•45 and a very minor component had a pI of 7•3. Optimal activity was at pH 4•5 and 50°C and the enzymes were stable over a pH range of 3•4–7•9 and at temperatures below 55°C. Apparent Kms were 3•33 mg ml-1 on rye flour arabinoxylan and 1•33 mg ml-1 on larch wood xylan. The enzymes partially hydrolysed larch wood xylan to oligosaccharides with two or three D-xylosyl residues. Rye flour arabinoxylan was hydrolysed to high molecular weight oligosaccharides which were not fractionated on Bio-Gel P-2.

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Production of xylooligosaccharides, bioethanol, and lignin from structural components of barley straw pretreated with a steam explosion.

Álvarez, C., González, A., Ballesteros, I. & Negro, M. J. (2021). Bioresource Technology, 342, 125953.

Barley straw (BS) is a potential source to obtain bioethanol and value-added products such as xylooligosaccharides (XOS) and lignin for application in diverse industries. In this study, BS was submitted to steam explosion pretreatment to valorize the main components of this lignocellulose biomass. For hemicellulose fraction valorization, different combinations of endo-β-(1,4)-D-xylanase enzyme with accessory enzymes (α-L-arabinofuranosidase, feruloy -esterase and acetylxylan-esterase) have been studied to produce XOS with a low degree of polymerization. The application of accessory enzymes combined with endo-β-(1,4)-D-xylanase enzymes turned out to be the most effective strategy for the formation of XOS. The solid fraction obtained after the pretreatment was submitted to presacharification and simultaneous saccharification and fermentation process for bioethanol production. The resulting lignin-rich residue was characterized. In this integrated process, 13.0 g XOS (DP2-DP6), 12.6 g ethanol and 16.6 g lignin were obtained from 100 g of BS, achieving the goal of valorizing this agricultural residue.

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Ozone assisted autohydrolysis of wheat bran enhances xylooligosaccharide production with low generation of inhibitor compounds: A comparative study.

Sonkar, R. M., Gade, P. S., Bokade, V., Mudliar, S. N. & Bhatt, P. (2021). Bioresource Technology, 338, 125559.

In the present study, ozone assisted autohydrolysis (OAAH) was evaluated for enhanced generation of xylooligosaccharide (XOS) from wheat bran. The total XOS yield with optimum ozone dose of 3% (OAAH-3) was found to be 8.9% (w/w biomass) at 110°C in comparison to 7.96% at 170°C by autohydrolysis (AH) alone. Although, there was no significant difference in oligomeric composition (DP 2-6), significant decrease in degradation products namely furfural (2.78-fold), HMF (3.15-fold), acrylamide (nil) and acetic acid (1.06-fold), was observed with OAAH-3 as a pretreatment option. There was 1-fold higher xylan to XOS conversion and OAAH-hydrolysate had higher DPPH radical scavenging activity than AH. PCA plots indicated clear enhancement in XOS production and lower generation of inhibitors with decrease in treatment temperature. Results of the study therefore suggest OAAH can be an effective pretreatment option that can further be integrated with downstream processing for concentration and purification of XOS.

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Imaging Study by Mass Spectrometry of the Spatial Variation of Cellulose and Hemicellulose Structures in Corn Stalks.

Arnaud, B., Durand, S., Fanuel, M., Guillon, F., Méchin, V. & Rogniaux, H. (2020). Journal of Agricultural and Food Chemistry, 68(13), 4042-4050.

The study used mass spectrometry imaging (MSI) to map the distribution of enzymatically degraded cell wall polysaccharides in maize stems for two genotypes and at several stages of development. The context was the production of biofuels, and the overall objective was to better describe the structural determinants of recalcitrance of grasses in bioconversion. The selected genotypes showed contrasting characteristics in bioconversion assays as well as in their lignin deposition pattern. We compared the pattern of cell wall polysaccharide degradation observed by MSI following the enzymatic degradation of tissues with that of lignin deposition. Several enzymes targeting the main families of wall polysaccharides were used. In the early stages of development, cellulose and mixed-linked β-glucans appeared as the main polysaccharides degraded from the walls, while heteroxylan products were barely detected, suggesting subsequent deposition of heteroxylans in the walls. At all stages and for both genotypes, enzymatic degradation occurred preferentially in nonlignified walls for all structural families of polysaccharides studied here. However, our results showed heterogeneity in the distribution of heteroxylan products according to their chemical structure: arabinosylated products were mostly represented in the pith center, while glucuronylated products were found at the pith periphery. The conclusions of our work are in agreement with those of previous studies. The MSI approach presented here is unique and attractive for addressing the histological and biochemical aspects of biomass recalcitrance to conversion, as it allows for a simultaneous interpretation of cell wall degradation and lignification patterns at the scale of an entire stem section.

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Hemicellulose based biorefinery from pineapple peel waste: Xylan extraction and its conversion into xylooligosaccharides.

Banerjee, S., Patti, A. F., Ranganathan, V. & Arora, A. (2019). Food and Bioproducts Processing, 117, 38-50.

Pineapple peel waste was utilized as an unexplored source of hemicellulose (31.8 ± 1.9%) for value addition. Hemicellulose was extracted by an alkali-based method, where the peels were incubated at different alkali concentrations (5%, 10% and 15% w/v) at temperatures ranging from 35°C to a maximum of 65°C for a fixed period of 16 h. A maximum recovery of hemicellulose (95.9 ± 2.0%) was observed after incubating extractive-free pineapple peels in 15% (w/v) alkali solution for 16 h at 45°C. Higher incubation temperatures (65°C) for 16 h, resulted in a lower yield of hemicellulose (81.7 ± 3.7%) which can be attributed to the disintegration of the hemicellulose structure due to large severity factor (temperature–time combination). With low severity factor, it was noted that higher yields (96.6 ± 0.3%) were obtained 65°C, 4 h). Hydrothermal-assisted alkali extraction was also evaluated for maximizing the recovery of pineapple peel hemicellulose. The maximum relative recovery of ˜87.6% was obtained with 10% (w/v) alkali at the end of 1.5 h of hydrothermal pretreatment (121°C and 15 psi pressure). The hemicellulose extracted by hydrothermal-assisted alkali pretreatment was enzymatically hydrolyzed to produce XOS and the process was optimized in terms of enzyme dose (U), temperature (°C), pH and time (h). Direct hydrolysis of pineapple peels with dilute nitric acid produced xylose-rich liquor (˜91% xylose yield) at 0.5% nitric acid, reaction time of 1 h and solid-liquid ratio of 1:20. The xylose-rich liquor could be converted to potential chemicals such as xylitol.

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Characterization of hemicelluloses in Phyllostachys edulis (Moso bamboo) culm during xylogenesis.

Wang, K. L., Wang, B., Hu, R., Zhao, X., Li, H., Zhou, G., Song, L. & Wu, A. M. (2019). Carbohydrate Polymers, 221, 127-136.

Hemicelluloses are β-(1→4)-linked backbone polysaccharides found in plant cell walls that include xyloglucans, xylans, mannans and glucomannans, and play important roles in plant tissue configuration. In this study, hemicelluloses were isolated from the apical, middle and basal segments of 6 m Phyllostachys edulis culm using KOH and DMSO extraction procedures, respectively. Chemical composition and structural characterization of hemicellulosic fractions were comparatively investigated by a combination of HPLC, GPC, FT-IR, 1H-, 13C-, HSQC NMR and TGA techniques. Our results show that the main chain of hemicellulose in P. edulis consists of glucuronoarabinoxylans (GAXs) with backbone 1, 4-β-d-Xyl, and side chain arabinose, glucuronic acid and acetylation. Hemicellulose content and molecular weight increased with culm xylogenesis in P. edulis. Our results provide new insights on the dynamics of hemicellulose structure in culm xylogenesis in P. edulis.

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Insight into the role of α-arabinofuranosidase in biomass hydrolysis: cellulose digestibility and inhibition by xylooligomers.

Xin, D., Chen, X., Wen, P. & Zhang, J. (2019). Biotechnology for Biofuels, 12(1), 64.

Background: α-L-Arabinofuranosidase (ARA), a debranching enzyme that can remove arabinose substituents from arabinoxylan and arabinoxylooligomers (AXOS), promotes the hydrolysis of the arabinoxylan fraction of biomass; however, the impact of ARA on the overall digestibility of cellulose is controversial. In this study, we investigated the effects of the addition of ARA on cellulase hydrolytic action. Results: We found that approximately 15% of the xylan was converted into AXOS during the hydrolysis of aqueous ammonia-pretreated corn stover and that this AXOS fraction was approximately 12% substituted with arabinose. The addition of ARA removes a portion of the arabinose decoration, but the resulting less-substituted AXOS inhibited cellulase action much more effectively; showing an increase of 45.7%. Kinetic experiments revealed that AXOS with a lower degree of arabinose substitution showed stronger affinity for the active site of cellobiohydrolase, which could be the mechanism of increased inhibition. Conclusions: Our findings strongly suggest that the ratio of ARA and other xylanases should be carefully selected to avoid the strong inhibition caused by the less-substituted AXOS during the hydrolysis of arabinoxylan-containing biomass. This study advances our understanding of the inhibitory mechanism of xylooligomers and provides critical new insights into the relationship of ARA addition and cellulose digestibility.

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