Content: 50 mg
Shipping Temperature: Ambient
Storage Temperature: Ambient
Physical Form: Powder
Stability: > 2 years under recommended storage conditions
CAS Number: 47592-59-6
Molecular Formula: C15H26O13
Molecular Weight: 414.4
Purity: > 90%
Substrate For (Enzyme): endo-1,4-β-Xylanase

High purity Xylotriose for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

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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

Versatile high resolution oligosaccharide microarrays for plant glycobiology and cell wall research.

Pedersen, H. L., Fangel, J. U., McCleary, B., Ruzanski, C., Rydahl, M. G., Ralet, M. C., Farkas, V., Von Schantz, L., Marcus, S. E., Andersen, M.C. F., Field, R., Ohlin, M., Knox, J. P., Clausen, M. H. & Willats, W. G. T. (2012). Journal of Biological Chemistry, 287(47), 39429-39438.

Microarrays are powerful tools for high throughput analysis, and hundreds or thousands of molecular interactions can be assessed simultaneously using very small amounts of analytes. Nucleotide microarrays are well established in plant research, but carbohydrate microarrays are much less established, and one reason for this is a lack of suitable glycans with which to populate arrays. Polysaccharide microarrays are relatively easy to produce because of the ease of immobilizing large polymers noncovalently onto a variety of microarray surfaces, but they lack analytical resolution because polysaccharides often contain multiple distinct carbohydrate substructures. Microarrays of defined oligosaccharides potentially overcome this problem but are harder to produce because oligosaccharides usually require coupling prior to immobilization. We have assembled a library of well characterized plant oligosaccharides produced either by partial hydrolysis from polysaccharides or by de novo chemical synthesis. Once coupled to protein, these neoglycoconjugates are versatile reagents that can be printed as microarrays onto a variety of slide types and membranes. We show that these microarrays are suitable for the high throughput characterization of the recognition capabilities of monoclonal antibodies, carbohydrate-binding modules, and other oligosaccharide-binding proteins of biological significance and also that they have potential for the characterization of carbohydrate-active enzymes.

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Identification of inulin-responsive bacteria in the gut microbiota via multi-modal activity-based sorting.

Riva, A., Rasoulimehrabani, H., Cruz-Rubio, J. M., Schnorr, S. L., von Baeckmann, C., Inan, D., et al. (2023). Nature Communications, 14(1), 8210.

Prebiotics are defined as non-digestible dietary components that promote the growth of beneficial gut microorganisms. In many cases, however, this capability is not systematically evaluated. Here, we develop a methodology for determining prebiotic-responsive bacteria using the popular dietary supplement inulin. We first identify microbes with a capacity to bind inulin using mesoporous silica nanoparticles functionalized with inulin. 16S rRNA gene amplicon sequencing of sorted cells revealed that the ability to bind inulin was widespread in the microbiota. We further evaluate which taxa are metabolically stimulated by inulin and find that diverse taxa from the phyla Firmicutes and Actinobacteria respond to inulin, and several isolates of these taxa can degrade inulin. Incubation with another prebiotic, xylooligosaccharides (XOS), in contrast, shows a more robust bifidogenic effect. Interestingly, the Coriobacteriia Eggerthella lenta and Gordonibacter urolithinfaciens are indirectly stimulated by the inulin degradation process, expanding our knowledge of inulin-responsive bacteria.

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Effects of cellulose and lignin on xylooligosaccharides production from xylan: The superiority of acetic acid/sodium acetate hydrolysis.

Liao, H., Chen, Z., Wen, P., Ying, W. & Zhang, J. (2023). Industrial Crops and Products, 205, 117497.

Xylooligosaccharides (XOS) are high-value products derived from xylan in lignocellulose and have a variety of prebiotic applications. The intertwining of xylan, cellulose, and lignin in lignocelluloses may affect XOS production. In order to investigate those impacts, the comparative analysis of XOS production was conducted using corncob, poplar and xylan as substrates through the hydrolysis using acetic acid/sodium acetate (AC/SA), acetic acid (AC), and pure water. The results revealed that the hydrolysis of different feedstocks using AC/SA generated the highest XOS yield and the least by-products compared to AC hydrolysis and hydrothermal (HT) treatment. The presence of cellulose led to the reductions of XOS production from xylan by AC/SA hydrolysis, AC hydrolysis, and HT treatment by 6.6%, 6.3%, and 4.3%, respectively. The presence of cellulose and lignin largely decreased XOS yields by 22.2%, 22.0%, and 88.5%, respectively. Obviously, the cellulose slightly inhibited xylan hydrolysis, while lignin had a strong negative effect on xylan hydrolysis. Besides, the adverse effect of lignin on xylan hydrolysis was the greatest in HT treatment. Despite the presence of cellulose and lignin, AC/SA hydrolysis exhibited the superior ability in XOS production and reduced the formation of by-products compared to AC hydrolysis and HT treatment.

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Valorization of rice husk by hydrothermal processing to obtain valuable bioproducts: Xylooligosaccharides and Monascus biopigment.

Centeno, A. C., Muñoz, S. S., Gonçalves, I. S., Vera, F. P. S., Forte, M. B. S., da Silva, S. S., dos Santos, J. C. & Hilares, R. T. (2023). Carbohydrate Polymer Technologies and Applications, 6, 100358.

Rice husk is a readily available residue which can be used for producing bioproducts in a biorefinery context. In this study, the hemicellulose fraction was hydrolyzed in a hydrothermal process to produce xylooligosaccharides (XOS), whereas the cellulosic hydrolysate was used for red pigment production by Monascus ruber Tieghem IOC 2225. The highest XOS (X2-X4) production (24 g per 1 kg of rice husk) was achieved at 180°C for 68 min in a non-stirred Parr reactor (50 mL). Subsequently, using a stirred parr reactor (1 L) at 180 °C for 60 min, 40 g of XOS (42% of xylobiose, 35% of xylobiose, 13% of xylotriose, 7% of xylotetraose, and 3% of xylopentaose) per 1 kg of rice husk were obtained. The XOS was then purified by using ultrafiltration (UF) with two diafiltration membranes at 6.5 pH, recovering approximately 92% of total XOS. Further purification was conducted with nanofiltration (NF) at 3.8 pH, recovering approximately 86.4% of XOS in the retentate. This process yielded XOS with a purity of 77%. Additionally, the enzymatic process yielded 132 g/kg of sugar, and the hydrolysate was used to produce 2.1 UA490nm of red pigment by fungi after 7 days.

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Enzymatic valorization of cellulosic and hemicellulosic-based biomasses via the production of antioxidant water-soluble hydrolyzate of maize stalks and the green bio-deinking of mixed office waste paper.

Hassan, A. A., Hasanin, M. S. & Ismail, S. A. (2023). Biomass Conversion and Biorefinery, 1-16.

Bio-valorization of various biomasses provides a sustainable promising approach for the eco-friendly production of variable value-added products. Herein, the current study devoted to the enzymatic valorization of two widely available biomasses, namely, maize stalks and waste paper. The cellulytic and hemicellulytic-rich cocktail was produced through the fermentation of rice straw by a locally isolated fungal strain Aspergillus terreus. The potential applicability of the produced cocktail for the enzymatic hydrolysis of the polysaccharide constituents of maize stalks was evaluated under various strategies. The reported results indicated that the microwave pretreatment of the biomass yielding a water-soluble hydrolyzate rich in cellobiose and xylobiose, sustained by thin layer (TLC) and high-performance liquid chromatographic (HPLC) measurements, in addition to phenolic compounds. Moreover, the enzymatic hydrolysis of the extracted hemicellulosic fraction from maize stalks was rich in xylooligosaccharides and phenolic compounds higher than that released from the hydrolysis of commercial xylan. The estimated antioxidant activity of the resulted hydrolyzate was also monitored by the scavenging of 1,1-diphenyl-2-picrylhydrazyl free radical spectrophotometrically at 515 nm. Moreover, the potential applicability of the produced enzymatic cocktail was examined for the bio-deinking of waste paper. The physical, chemical, and surface morphological characteristics of the treated paper sample was compared to a blank one regarding the whiteness index, ash content, scanning electron microscopy (SEM), energy dispersive X-ray (EDX), and Fourier transform infrared spectroscopy (FTIR). On the base of the estimated results, the produced enzymatic cocktail possessed efficient dislodgement ability for the printed ink from the paper surface.

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A combined liquid chromatography–trapped ion mobility–tandem high-resolution mass spectrometry and multivariate analysis approach for the determination of enzymatic reactivity descriptors in biomass hydrolysates.

Ramtanon, I., Berlioz-Barbier, A., Remy, S., Renault, J. H. & Le Masle, A. (2023). Journal of Chromatography A, 1706, 464277.

Intermediate products such as oxygenated compounds may interfere with bioconversion kinetics of lignocellulosic biomass into bioethanol. This work presents a multidimensional approach, based on liquid chromatography (LC), trapped ion mobility spectrometry (TIMS), tandem high-resolution mass spectrometry (HRMS/MS), and multivariate analysis, for the identification of enzymatic reactivity descriptors in 22 industrial biomass samples, called hydrolysates. The first part of the study is dedicated to the improvement of the chemical diversity assessment of the hydrolysates through an original three-dimensional Van Krevelen diagram displaying the double bond equivalent (DBE) as third dimension. In a second part, the evaluation of data by multivariate data analysis allowed the discrimination of sample according to the biomass type and the level of enzymatic reactivity. In the last part, a potential descriptor of low enzymatic reactivity was selected and used in a case study. An in-depth structural analysis was performed on the feature annotated as carbohydrate derivative. Considering the intricate fragmentation spectrum exhibited by the selected feature, trapped ion mobility was employed to enhance separation prior to the HRMS/MS experiments. This final step improved data interpretation and increased the identification confidence level leading to the characterization of xylotriose, 3,5-dimethoxy-4-hydroxybenzaldehyde and 4-hydroxy-3-methoxy-cinnamaldehyde. This is the first study to present an untargeted multidimensional approach for the identification of enzymatic hydrolysis inhibitors in industrial hydrolysate samples.

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A novel class of xylanases specifically degrade marine red algal β1, 3/1, 4-mixed-linkage xylan.

Zhao, F., Yu, C. M., Sun, H. N., Zhao, L. S., Ding, H. T., Cao, H. Y., Chen, Y., Qin, Q., Zhang, Y. Z. & Chen, X. L. (2023). Journal of Biological Chemistry, 299(9), 105116.

Xylans are polysaccharides composed of xylose and include β1,4-xylan, β1,3-xylan, and β1,3/1,4-mixed-linkage xylan (MLX). MLX is widely present in marine red algae and constitutes a significant organic carbon in the ocean. Xylanases are hydrolase enzymes that play an important role in xylan degradation. While a variety of β1,4-xylanases and β1,3-xylanases involved in the degradation of β1,4-xylan and β1,3-xylan have been reported, no specific enzyme has yet been identified that degrades MLX. Herein, we report the characterization of a new MLX-specific xylanase from the marine bacterium Polaribacter sp. Q13 which utilizes MLX for growth. The bacterium secretes xylanases to degrade MLX, among which is Xyn26A, an MLX-specific xylanase that shows low sequence similarities (<27%) to β1,3-xylanases in the glycoside hydrolase family 26 (GH26). We show that Xyn26A attacks MLX precisely at β1,4-linkages, following a β1,3-linkage toward the reducing end. We confirm that Xyn26A and its homologs have the same specificity and mode of action on MLX, and thus represent a new xylanase group which we term as MLXases. We further solved the structure of a representative MLXase, AlXyn26A. Structural and biochemical analyses revealed that the specificity of MLXases depends critically on a precisely positioned β1,3-linkage at the −2/−1 subsite. Compared to the GH26 β1,3-xylanases, we found MLXases have evolved a tunnel-shaped cavity that is fine-tuned to specifically recognize and hydrolyze MLX. Overall, this study offers a foremost insight into MLXases, shedding light on the biochemical mechanism of bacterial degradation of MLX.

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Two-Step Hydrothermal Pretreatments for Co-Producing Xylooligosaccharides and Humic-like Acid from Vinegar Residue.

Jiao, N., Zhu, Y., Li, H., Yu, Y., Xu, Y. & Zhu, J. (2023). Fermentation, 9(7), 589.

This study proposes an efficient strategy for co-producing high-value-added xylooligosaccharides (XOS) and humic-like acid (HLA) from vinegar residue based on two-step hydrothermal pretreatments. During the first-step hydrothermal pretreatment (170°C, 50 min), 29.1% of XOS (X2-X6) was obtained. The XOS yield was further improved to 36.2% with endoxylanase hydrolysis, thereby increasing the value of (X2-X4)/XOS from 0.8 to 1.0. Subsequently, the second-step hydrothermal pretreatment was investigated to produce HLA from the solid residue of the first-step hydrothermal pretreatment. The highest HLA yield was 15.3% in the presence of 0.6 mol/L of KOH at 210°C for 13 h. In addition, 31.7% of hydrochar by-product was obtained. The mass balance results showed that 1000 g of vinegar residue produced 67.9 g of XOS, 91.6 g of HLA, and 189.5 g of hydrochar. Therefore, this study provides a promising pathway for comprehensive use of lignocellulosic biomass in producing XOS and HLA.

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The secretome of Agaricus bisporus: temporal dynamics of plant polysaccharides and lignin degradation.

Duran, K., Magnin, J., America, A. H., Peng, M., Hilgers, R., de Vries, R. P., Baars, J. J. P., Berkel, W. J. H., Kuyper, T. W. & Kabel, M. A. (2023). iScience, 26(7): 107087.

Despite substantial lignocellulose conversion during mycelial growth, previous transcriptome and proteome studies have not yet revealed how secretomes from the edible mushroom Agaricus bisporus develop and whether they modify lignin models in vitro. To clarify these aspects, A. bisporus secretomes collected throughout a 15-day industrial substrate production and from axenic lab-cultures were subjected to proteomics, and tested on polysaccharides and lignin models. Secretomes (day 6-15) comprised A. bisporus endo-acting and substituent-removing glycoside hydrolases, whereas β-xylosidase and glucosidase activities gradually decreased. Laccases appeared from day 6 onwards. From day 10 onwards, many oxidoreductases were found, with numerous multicopper oxidases (MCO), aryl alcohol oxidases (AAO), glyoxal oxidases (GLOX), a manganese peroxidase (MnP), and unspecific peroxygenases (UPO). Secretomes modified dimeric lignin models, thereby catalyzing syringylglycerol-β-guaiacyl ether (SBG) cleavage, guaiacylglycerol-β-guaiacyl ether (GBG) polymerization, and non-phenolic veratrylglycerol-β-guaiacyl ether (VBG) oxidation. We explored A. bisporus secretomes and insights obtained can help to better understand biomass valorization.

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