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Xylotetraose

Xylotetraose O-XTE
Product code: O-XTE
€164.00

30 mg

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Content: 30 mg
Shipping Temperature: Ambient
Storage Temperature: Ambient
Physical Form: Powder
Stability: > 10 years under recommended storage conditions
CAS Number: 22416-58-6
Molecular Formula: C20H34O17
Molecular Weight: 546.5
Purity: > 95%
Substrate For (Enzyme): endo-1,4-β-Xylanase

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

Documents
Certificate of Analysis
Safety Data Sheet
FAQs Data Sheet
Publications
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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Publication

Partial acid-hydrolysis of TEMPO-oxidized arabinoxylans generates arabinoxylan-structure resembling oligosaccharides.

Pandeirada, C. O., Speranza, S., Bakx, E., Westphal, Y., Janssen, H. G. & Schols, H. A. (2021). Carbohydrate Polymers, 275, 118795.

Arabinoxylans (AXs) display biological activities that depend on their chemical structures. To structurally characterize and distinguish AXs using a non-enzymatic approach, various TEMPO-oxidized AXs were partially acid-hydrolysed to obtain diagnostic oligosaccharides (OS). Arabinurono-xylo-oligomer alditols (AUXOS-A) with degree of polymerization 2-5, comprising one and two arabinuronic acid (AraA) substituents were identified in the UHPLC-PGC-MS profiles of three TEMPO-oxidized AXs, namely wheat (ox-WAX), partially-debranched WAX (ox-pD-WAX), and rye (ox-RAX). Characterization of these AUXOS-A highlighted that single-substitution of the Xyl unit preferably occurs at position O-3 for these samples, and that ox-WAX has both more single substituted and more double-substituted xylose residues in its backbone than the other AXs. Characteristic UHPLC-PGC-MS OS profiles, differing in OS abundance and composition, were obtained for each AX. Thus, partial acid-hydrolysis of TEMPO-oxidized AXs with analysis of the released OS by UHPLC-PGC-MS is a promising novel non-enzymatic approach to distinguish AXs and obtain insights into their structures.

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Publication

Lignocellulose degradation for the bioeconomy: the potential of enzyme synergies between xylanases, ferulic acid esterase and laccase for the production of arabinoxylo-oligosaccharides.

Schmitz, E., Leontakianakou, S., Norlander, S., Karlsson, E. N. & Adlercreutz, P. (2021). Bioresource Technology, 343, 126114.

The success of establishing bioeconomies replacing current economies based on fossil resources largely depends on our ability to degrade recalcitrant lignocellulosic biomass. This study explores the potential of employing various enzymes acting synergistically on previously pretreated agricultural side streams (corn bran, oat hull, soluble and insoluble oat bran). Degrees of synergy (oligosaccharide yield obtained with the enzyme combination divided by the sum of yields obtained with individual enzymes) of up to 88 were obtained. Combinations of a ferulic acid esterase and xylanases resulted in synergy on all substrates, while a laccase and xylanases only acted synergistically on the more recalcitrant substrates. Synergy between different xylanases (glycoside hydrolase (GH) families 5 and 11) was observed particularly on oat hulls, producing a yield of 57%. The synergistic ability of the enzymes was found to be partly due to the increased enzyme stability when in combination with the substrates.

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Publication

Production of thermostable xylanase using Streptomyces thermocarboxydus ME742 and application in enzymatic conversion of xylan from oil palm empty fruit bunch to xylooligosaccharides.

Khangkhachit, W., Suyotha, W., Leamdum, C., & Prasertsan, P. (2021). Biocatalysis and Agricultural Biotechnology, 102180.

Empty fruit bunch (EFB), the largest amount of biomass from a palm oil mill, is a promising renewable source for many value-added products. This study aimed to utilize EFB for production of xylanase by Streptomyces thermocarboxydus ME742 and applied the enzyme to the production of xylooligosaccharides (XOS) from EFB derived xylan (EFB-xylan). The strain ME742 produced the maximum xylanase (473.21 ± 6.55 U/mL) in a medium containing 50 g/L EFB supplemented with 3.0 g/L peptone at 40°C for 4 days. Xylanase ME742 was purified 23.68 fold with specificity of 1229 U/mg by acetone precipitation and DEAE-Sepharose chromatography. It was stable in a wide range of pH (4.0-9.5) and in elevated temperatures up to 55°C. Xylanase ME742 effectively hydrolyzed EFB-xylan. HPLC analysis revealed that the hydrolysate was composed of xylose and XOS with degree of polymerization between 2 and 5 and xylobiose was the predominant product. The XOS yield ranging in 95.01-151.19 mg/g EFB-xylan was generated from enzymatic processing for 12-72 h. Interestingly, arabinosyl-xylooligosaccharides were also predicted to be produced from EFB-xylan. XOS mixture exhibited high antioxidant activity (71.36 ± 0.57%) against DPPH at 100 μg/mL concentration and moderate activity (45.18 ± 1.56%) against ABTS radical. These findings reveal the potential use of Streptomyces thermocarboxydus ME742 and xylanase produced in a sustainable bioprocess to add value of EFB waste.

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Publication

Rapid profiling strategy for oligosaccharides and polysaccharides by MALDI TOF mass spectrometry.

Wang, J., Zhao, J., Nie, S., Xie, M. & Li, S. (2021). Food Hydrocolloids, 124, 107237.

The application of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI TOF MS) in glycan was limited due to their poor ionization efficiency, compared with biomolecules such as proteins and peptides. Aiming to improve the ionization efficiency and simplify preparation procedure simultaneously during MALDI MS analysis, an on-target derivatization method using 3-aminoquinoline (3-AQ)/α-cyano-4-hydroxycinnamic acid (CHCA) as matrix was employed and it was conducted both in the positive and negative ion MALDI TOF MS. Results indicated that after on-target derivatization, the ions generated had substantially improved S/N ratios and sensitivity in the tandem mass spectra. The B/Y- type ions of 3-AQ-labeled glycans could be easily recognized, and cross-ring A- type ions provided additional information to reveal the linkage patterns. Specifically, positive ion mass spectra with protonated adduct as precursor ion produced a simple fragmentation pattern benefited for sequencing and observation of branches. Furthermore, this method was successfully applied in polysaccharides analysis, including arabinoxylan, xylan, arabinogalactan and dextran after enzymatic or acid degradation. This study demonstrated that it was feasible to analyze higher molecular weight polysaccharides by MALDI TOF MS using 3-AQ/CHCA matrix through appropriate hydrolysis, and it allowed much efficient structural interpretation with increased sensitivity and characteristic fragment ions.

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Publication

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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Publication

Controlling autohydrolysis conditions to produce xylan-derived fibers that modulate gut microbiota responses and metabolic outputs.

Zhao, S., Dien, B. S., Lindemann, S. R. & Chen, M. H. (2021). Carbohydrate Polymers, 271, 118418.

Autohydrolysis is used for producing xylan-derived oligosaccharides from lignocellulosic biomass. Although numerous studies report optimized autohydrolysis conditions for various plants, few of these studies correlate process parameters with the resulting structural properties to their impact on intestinal bacterial communities. Thus, to further clarify these relationships, beechwood xylan (BWX)-derived substrates, processed under five conditions, were fermented in vitro by human gut microbiota. Autohydrolysis reduced the mean molecular size and substitutions of BWX. Distinct fermentation kinetics were observed with differing processing of BWX substrates, which correlated with impacts on community species evenness. The relative abundances of Bacteroides, Fusicatenibacter, Bifidobacterium, and Megasphaera within the fermentations varied with processing conditions. While the total short-chain fatty acid concentrations were the same among the treatments, processing conditions varied the extent of propionate and butyrate generation. Autolysis parameters may be an important tool for optimizing beneficial effects of xylan-derived fibers on human gut microbiota structure and function.

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Publication

Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost‐derived consortium.

Kadowaki, M. A., Briganti, L., Evangelista, D. E., Echevarría‐Poza, A., Tryfona, T., Pellegrini, V. O., Nakayama, D. G., Dupree, P. & Polikarpov, I. (2021). Biotechnology and Bioengineering, 11(10), 4052-4064.

The heteropolysaccharide xylan is a valuable source of sustainable chemicals and materials from renewable biomass sources. A complete hydrolysis of this major hemicellulose component requires a diverse set of enzymes including endo-β-1,4-xylanases, β-xylosidases, acetylxylan esterases, α-l-arabinofuranosidases, and α-glucuronidases. Notably, the most studied xylanases from glycoside hydrolase family 11 (GH11) have exclusively been endo-β-1,4- and β-1,3-xylanases. However, a recent analysis of a metatranscriptome library from a microbial lignocellulose community revealed GH11 enzymes capable of releasing solely xylobiose from xylan. Although initial biochemical studies clearly indicated their xylobiohydrolase mode of action, the structural features that drive this new activity still remained unclear. It was also not clear whether the enzymes acted on the reducing or nonreducing end of the substrate. Here, we solved the crystal structure of MetXyn11 in the apo and xylobiose-bound forms. The structure of MetXyn11 revealed the molecular features that explain the observed pattern on xylooligosaccharides released by this nonreducing end xylobiohydrolase.

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Publication

Two-step acetic acid/sodium acetate and xylanase hydrolysis for xylooligosaccharides production from corncob.

Liao, H., Li, X., Lian, Z., Xu, Y. & Zhang, J. (2021). Bioresource Technology, 342, 125979.

At present, xylooligosaccharides (XOS) from corncob using acid-base conjugate system has not been reported. In this study, XOS production from corncob by two-step acetic acid/sodium acetate (AC/SA) conjugate system hydrolysis and xylanase hydrolysis was optimized, and monosaccharides were subsequently produced from corncob residues by cellulase hydrolysis. The XOS of 19.9 g/L was obtained from corncob (10%, w/v) using 0.15 M AC/SA hydrolysis at a molar ratio of 3.0 at 170 °C for 60 min, followed by xylanase hydrolysis. The second-step AC/SA hydrolysis of hydrolyzed corncob (10%, w/v) produced 3.1 g/L of XOS. Finally, the maximum XOS yield of 74.8% (based on xylan in corncob) was achieved, which is the highest yield among yields reported previously. The purity of XOS was high, whereas the contents of by-products were very low. This work presents a novel and promising strategy for co-production of XOS and monosaccharides from corncob without xylan isolation and purification.

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Publication

Characterization of a novel multidomain CE15-GH8 enzyme encoded by a polysaccharide utilization locus in the human gut bacterium Bacteroides eggerthii.

Kmezik, C., Krska, D., Mazurkewich, S. & Larsbrink, J. (2021). Scientific Reports, 11(1), 1-13.

Bacteroidetes are efficient degraders of complex carbohydrates, much thanks to their use of polysaccharide utilization loci (PULs). An integral part of PULs are highly specialized carbohydrate-active enzymes, sometimes composed of multiple linked domains with discrete functions-multicatalytic enzymes. We present the biochemical characterization of a multicatalytic enzyme from a large PUL encoded by the gut bacterium Bacteroides eggerthii. The enzyme, BeCE15A-Rex8A, has a rare and novel architecture, with an N-terminal carbohydrate esterase family 15 (CE15) domain and a C-terminal glycoside hydrolase family 8 (GH8) domain. The CE15 domain was identified as a glucuronoyl esterase (GE), though with relatively poor activity on GE model substrates, attributed to key amino acid substitutions in the active site compared to previously studied GEs. The GH8 domain was shown to be a reducing-end xylose-releasing exo-oligoxylanase (Rex), based on having activity on xylooligosaccharides but not on longer xylan chains. The full-length BeCE15A-Rex8A enzyme and the Rex domain were capable of boosting the activity of a commercially available GH11 xylanase on corn cob biomass. Our research adds to the understanding of multicatalytic enzyme architectures and showcases the potential of discovering novel and atypical carbohydrate-active enzymes from mining PULs.

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Publication

Efficient production of nutraceuticals and lactic acid from lignocellulosic biomass by combining organosolv fractionation with enzymatic/fermentative routes.

Karnaouri, A., Asimakopoulou, G., Kalogiannis, K. G., Lappas, A. A. & Topakas, E. (2021). Bioresource Technology, 341, 125846.

The aim of this work was to investigate the use of isobutanol as organic solvent for the efficient delignification and fractionation of beechwood through the OxiOrganosolv process in the absence of any catalyst. The results demonstrate that cellulose-rich solid pulp produced after pretreatment is a source of fermentable sugars that can be easily hydrolyzed and serve as a carbon source in microbial fermentations for the production of omega-3 fatty acids and D-lactic acid. The C5 sugars are recovered in the aqueous liquid fractions and comprise a fraction rich in xylo-oligosaccharides with prebiotic potential. The maximum production of optically pure D-lactic from Lactobacillus delbrueckii sp. bulgaricus reached 51.6 g/L (0.57 g/gbiomass), following a simultaneous saccharification and fermentation strategy. Crypthecodenium cohnii accumulated up to 52.1 wt% lipids with a DHA content of 54.1 %, while up to 43.3 % hemicellulose recovery in form of oligosaccharides was achieved in the liquid fraction.

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Publication

Efficient production of xylooligosaccharides and fermentable sugars from corncob by propionic acid and enzymatic hydrolysis.

Liao, H., Xu, Y. & Zhang, J. (2021). Bioresource Technology, 342, 125680.

Xylooligosaccharides (XOS) are usually produced by xylan isolation from lignocellulose by alkaline followed by enzymatic hydrolysis, but the process is complicated. Recently acid hydrolysis for XOS preparation has become popular as it is faster and easier. This study investigated a novel strategy for producing XOS from corncob using propionic acid (PA) hydrolysis, then producing monosaccharides from solid residues by cellulase hydrolysis. The effect of alkaline post-treatment on enzymatic hydrolysis was studied. The maximum XOS yield of 68.5% was achieved using 5% PA at 170°C for 50 min. About 84% of lignin in PA-hydrolyzed corncob was removed using alkaline post-treatment. The yields of glucose and xylose reached 89.8% and 80.1%, respectively, using 5 FPU cellulase/g dry matter. The results indicated that alkaline post-treatment reduced 50% cellulase loading and improved the saccharification of PA-hydrolyzed corncob. This study presents an innovative option for efficient production of XOS and monosaccharides from corncob.

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Valorization of peach palm (Bactris gasipaes Kunth) waste: Production of antioxidant xylooligosaccharides.

Vieira, T. F., Corrêa, R. C. G., Moreira, R. D. F. P. M., Peralta, R. A., de Lima, E. A., Helm, C. V., Garcia, J. A. A., Bracht, A. & Peralta, R. M. (2021). Waste and Biomass Valorization, 1-14.

In Brazil, the production and consumption of palm heart, especially from the Bactris gasipaes Kunth, generates a large number of lignocellulosic by-products. This study reports the obtainment of xylooligosaccharides (XOS) from xylans extracted from these residues. Xylans from peach palm waste (inner sheath and peel) were extracted using a mild alkali treatment with recovery yields of 82% and 80%, respectively. XOS were obtained through enzymatic hydrolysis employing a commercial xylanase with yields from xylan inner sheath and xylan peel of 50.1% and 48.8%, respectively. The antioxidant potential of XOS was measured employing five of the most commonly used procedures. In overall terms, the XOS from the xylans of peach palm wastes showed higher antioxidant capacity than the XOS obtained from the commercial xylans. The chemical structures of the XOS were determined by mass spectrometry (ESI–MS). The ESI-MS spectra suggest that XOS with grouped xylose or arabinose units ranging from 2 to 5 (differing by 132 Da) and as sodium adduct ions [M + Na]+ in the range of 100-1000 m/z. These results indicate that peach palm wastes can be explored to XOS production, which could be applied as natural antioxidants in functional food and pharmaceutical preparations.

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Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity.

Talens-Perales, D., Jiménez-Ortega, E., Sánchez-Torres, P., Sanz-Aparicio, J. & Polaina, J. (2021). Computational and Structural Biotechnology Journal, 19, 2676-2686.

Endoxylanases active under extreme conditions of temperature and alkalinity can replace the use of highly pollutant chemicals in the pulp and paper industry. Searching for enzymes with these properties, we carried out a comprehensive bioinformatics study of the GH10 family. The phylogenetic analysis allowed the construction of a radial cladogram in which protein sequences putatively ascribed as thermophilic and alkaliphilic appeared grouped in a well-defined region of the cladogram, designated TAK Cluster. One among five TAK sequences selected for experimental analysis (Xyn11) showed extraordinary xylanolytic activity under simultaneous conditions of high temperature (90°C) and alkalinity (pH 10.5). Addition of a carbohydrate binding domain (CBM2) at the C-terminus of the protein sequence further improved the activity of the enzyme at high pH. Xyn11 structure, which has been solved at 1.8 Å resolution by X-ray crystallography, reveals an unusually high number of hydrophobic, ionic and hydrogen bond atomic interactions that could account for the enzyme’s extremophilic nature.

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Xylanase-polymer conjugates as new catalysts for xylooligosaccharides production from lignocellulose.

Hu, Y., Shi, C. Y., Xun, X. M., Huang, B. R., You, S., Wu, F. A. & Wang, J. (2021). Biochemical Engineering Journal, 171, 108025.

In the past few years, xylooligosaccharides produced from lignocellulosic biomass have attracted great attention. Enzyme catalysis is widely used because of its mild reaction conditions. In order to solve the shortcomings of poor stability and high cost of enzyme, a carrier-free enzyme immobilization technology was introduced. For this purpose, protein-polymer conjugates, kinds of carrier-free immobilized enzymes, were first established by growing poly (N-isopropylacrylamide) chains on xylanase using a grafting-from method, to obtain reusable and high-value xylanase. SDS-PAGE and circular dichroism spectra showed the successful preparation of xylanase-PNIPAAm conjugates, and the integrity of the protein secondary structure. The remaining activity of the xylanase-PNIPAAm conjugates after heat treatment (90°C) for 60 min was approximately 20 % higher than that of the free xylanase, and a higher pH stability was obtained in the pH range of 2-8. The remaining activity of xylanase-PNIPAAm conjugates was more than 60 % after recycling 5 times. In addition, the mulberry bark synergistic treated by xylanase-PNIPAAm conjugates and cellulase was studied. More than 99.95 % yield of XOS in the degree of polymerization range of 1-3 was produced from mulberry bark. Overall, the construction of xylanase-PNIPAAm conjugates provides a novel method to produce xylooligosaccharides from waste biomass.

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Valorisation of walnut shell and pea pod as novel sources for the production of xylooligosaccharides.

Cebin, A. V., Ralet, M. C., Vigouroux, J., Karača, S., Martinić, A., Komes, D. & Bonnin, E. (2021). Carbohydrate Polymers, 263, 117932.

According to the high interest in agro-industrial waste reutilisation, underutilised lignocellulosic materials, such as walnut shell (WS) and pea pod (PP), come in focus. The aim of this paper was to evaluate WS and PP as sources for the production of xylooligosaccharides (XOS). Hemicelluloses from WS and PP were recovered by combining varying parameters of delignification and alkaline extraction. At optimal recovery conditions, the fractions were further hydrolysed to XOS using GH11 endo-xylanase, by varying time and enzyme concentration. Xylose was predominant in the monomeric composition of the obtained hemicelluloses, building low-branched (arabino)glucuronoxylan, in WS exclusively, while in PP some xyloglucan as well. Delignification was essential for high recovery of total xylose from the materials, up to at least 70%. High xylan conversions were obtained for 24 h hydrolysis, resulting in xylobiose and xylotriose when using low enzyme concentration, while in xylose and xylobiose with high enzyme concentration.

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Evaluation of Xylooligosaccharides Production for a Specific Degree of Polymerization by Liquid Hot Water Treatment of Tropical Hardwood.

Jang, S. K., Kim, J. H., Choi, J. H., Cho, S. M., Kim, J. C., Kim, H. & Choi, I. G. (2021). Foods, 10(2), 463.

Eucalyptus pellita is known as attractive biomass, and it has been utilized for eucalyptus oil, furniture, and pulp and paper production that causes a significant amount of byproducts. Liquid hot water treatment depending on combined severity factor (CSF) was subjected to isolate hemicellulose fraction from E. pellita and to produce xylooligosaccharides (XOS). The xylan extraction ratio based on the initial xylan content of the feedstock was maximized up to 77.6% at 170°C for 50 min condition (CSF: 1.0), which had accounted for XOS purity of 76.5% based on the total sugar content of the liquid hydrolysate. In this condition, the sum of xylobiose, xylotriose, and xylotetraose which has a low degree of polymerization (DP) of 2 to 4 was determined as 80.6% of the total XOS. The highest XOS production score established using parameters including the xylan extraction ratio, XOS purity, and low DP XOS ratio was 5.7 at CSF 1.0 condition. XOS production score evaluated using the CSF is expected to be used as a productivity indicator of XOS in the industry (R-squared value: 0.92).

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Structure-based substrate specificity analysis of GH11 xylanase from Streptomyces olivaceoviridis E-86.

Fujimoto, Z., Kishine, N., Teramoto, K., Tsutsui, S. & Kaneko, S. (2021). Applied Microbiology and Biotechnology, 1-10.

Although many xylanases have been studied, many of the characteristics of xylanases toward branches in xylan remain unclear. In this study, the substrate specificity of a GH11 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn11B) was elucidated based on its three-dimensional structure. Subsite mapping suggests that SoXyn11B has seven subsites (four subsites on the - side and three subsites on the + side), and it is one longer than the GH10 xylanase from S. olivaceoviridis (SoXyn10A). SoXyn11B has no affinity for the subsites at either end of the scissile glycosidic bond, and the sugar-binding energy at subsite - 2 was the highest, followed by subsite + 2. These properties were very similar to those of SoXyn10A. In contrast, SoXyn11B produced different branched oligosaccharides from bagasse compared with those of SoXyn10A. These branched oligosaccharides were identified as O-β-D-xylopyranosyl-(1→4)-[O-α-L-arabinofuranosyl-(1→3)]-O-β-D-xylopyranosyl-(1→4)-β-D-xylopyranosyl-(1→4)-β-D-xylopyranose (Ara3Xyl4) and O-β-D-xylopyranosyl-(1→4)-[O-4-O-methyl-α-D-glucuronopyranosyl-(l→2)]-β-D-xylopyranosyl-(1→4)-β-D-xylopyranosyl-(1→4)-β-D-xylopyranose (MeGlcA3Xyl4) by nuclear magnetic resonance (NMR) and electrospray ionization mass spectrometry (ESI-MS) and confirmed by crystal structure analysis of SoXyn11B in complex with these branched xylooligosaccharides. SoXyn11B has a β-jerryroll fold structure, and the catalytic cleft is located on the inner β-sheet of the fold. The ligand-binding structures revealed seven subsites of SoXyn11B. The 2- and 3-hydroxy groups of xylose at the subsites + 3, + 2, and – 3 face outwards, and an arabinose or a glucuronic acid side chain can be linked to these positions. These subsite structures appear to cause the limited substrate specificity of SoXyn11B for branched xylooligosaccharides.

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Safety Data Sheet
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