The product has been successfully added to your shopping list.
Xylotriose O-XTR
Product code: O-XTR
€155.00

50 mg

Prices exclude VAT

Available for shipping

Content: 50 mg
Shipping Temperature: Ambient
Storage Temperature: Ambient
Physical Form: Powder
Stability: > 10 years under recommended storage conditions
CAS Number: 47592-59-6
Molecular Formula: C15H26O13
Molecular Weight: 414.4
Purity: > 95%
Substrate For (Enzyme): endo-1,4-β-Xylanase

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

Documents
Certificate of Analysis
Safety Data Sheet
FAQs Booklet
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.

Hide Abstract
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.

Hide Abstract
Publication

Novel xylanase producing Bacillus strain X2: molecular phylogenetic analysis and its application for production of xylooligosaccharides.

Dhruw, C., Husain, K., Kumar, V., & Sonawane, V. C. (2020). Biotech, 10(8), 1-15.

Bacillus strain X2 that produced extracellular endo-xylanase (GH 11) (EC: 3.2.1.8) was isolated from the soil of the Northeast India region. This aerobic culture was Gram positive and endospore forming. Chemotaxonomic characterization showed variance with the fatty acid profile of related species in the Bacillus subtilis group. In Bacillus strain X2, distinct occurrence of iso-C14:0 lipids is absent in other related species. The 16S rRNA gene sequence homology showed 99% similarity with Bacillus subtilis subsp. inaquosorum. The phylogenetic analysis by the multilocus sequence analysis (MLSA) of the nucleotide sequence of six concatenated genes (16S rRNA, groELgyrApolCpurH and rpoB) resolved the taxonomic position of the Bacillus strain X2 in the Bacillus subtilis subsp. group. The MLSA showed that it is a member of a clade that includes Bacillus subtilis subsp. stercoris. In in silico DNA–DNA hybridization (DDH), the highest matching score was obtained with Bacillus subtilis subsp. stercoris (87%). The in silico DDH of the genome (G + C 43.7 mol %) shared 48.5%, with Bacillus subtilis subsp. inaquosorum. The MLSA phylogenetic tree and the highest degree of DNA hybridization, indicating that it belongs to the Bacillus subtilis subspecies stercoris.

Hide Abstract
Publication

Improved development in magnetic Xyl-CLEAs technology for biotransformation of agro-industrial by-products through the use of a novel macromolecular cross-linker.

Hero, J. S., Morales, A. H., Perotti, N. I., Romero, C. M. & Martinez, M. A. (2020). Reactive and Functional Polymers, 154, 104676.

Cross-Linked Enzyme Aggregates (CLEAs) technologies for enzyme immobilization are influenced by mass transference problems as the degree of molecular crosslinking achieved strongly affects the enzyme exposure to the substrates. Therefore, this work seeks to improve the accessibility of high molecular weight substrates by using macromolecular cross-linkers to the synthesis of a xylanolytic biocatalyst. After confirming that commercial polymers used as macromolecular cross-linkers significantly upgraded the xylanase activity from a crude preparation, a novel biopolymer/amyloid protein complex (BPAP) extracted from a microbial biofilm was used producing a remarkable recovery (83%) of the enzyme activity. A response surface methodology was applied to contrast the features of a previously developed biocatalyst with glutaraldehyde (GA@Xyl-CLEAs) and a novel one synthesized with BPAP combined with functionalized magnetic nanoparticles: mBPAP@Xyl-CLEAs. It was observed that the crosslinking agent used was the factor that most affected the enzyme activity. Also, the mBPAP system showed a similar and higher hydrolytic activity than those synthesized with GA, which was not affected by the mNPs/protein ratio. Finally, the mBPAP@Xyl-CLEAs were successfully tested for xylooligosaccharides production from agroindustrial-derived substrates, making this technology a promising practice to obtain green and suitable biocatalysts.

Hide Abstract
Publication

An integrated process to produce prebiotic xylooligosaccharides by autohydrolysis, nanofiltration and endo-xylanase from alkali-extracted xylan.

Lian, Z., Wang, Y., Luo, J., Lai, C., Yong, Q., & Yu, S. (2020). Bioresource Technology, 314, 123685.

Alkali-extracted xylan from lignocellulosics is a promising feedstock for production of prebiotic xylooligosaccharides (XOS). An integrated process was established combining autohydrolysis, nanofiltration and xylanase hydrolysis. Results show that after autohydrolysis 48.37% of xylan was degraded into oligomers and dissolved into the autohydrolysate, of which 57.83% were XOS. By-products and xylose were removed by nanofiltration with discontinuous diafiltration, while high recovery yields of XOS (84.15%) and xylan (87.45%) were obtained. High yields of XOS were obtained by adding xylanase to the autohydrolysates; after enzymatic hydrolysis an XOS yield of 96-98% was obtained. The enzymatic hydrolysates showed positive prebiotic effects on B. adolescentis with an increase in cell concentration by 4.8-fold after fermentation for 24 h. The main products were short-chain fatty acids with carbon balanced during the whole fermentation process. This integrated strategy resulted in a final XOS conversion of 41.22% contrasted to the initial xylan in raw alkali-extracted xylan.

Hide Abstract
Publication

Enzyme synergy for the production of arabinoxylo-oligosaccharides from highly substituted arabinoxylan and evaluation of their prebiotic potential.

Bhattacharya, A., Ruthes, A., Vilaplana, F., Karlsson, E. N., Adlecreutz, P. & Stålbrand, H. (2020). LWT, 131, 109762.

Wheat bran arabinoxylan can be converted by enzymatic hydrolysis into short arabinoxylo-oligosaccharides (AXOS) with prebiotic potential. Alkali extraction of arabinoxylan from wheat-bran offers advantages in terms of yield and results in arabinoxylan with highly-substituted regions which has been a challenge to hydrolyse using endoxylanases. We show that this hurdle can be overcome by selecting an arabinoxylanase that attacks these regions. The yield of AXOS can be increased by enzyme synergy, involving the hydrolysis of some arabinoxylan side groups. Thus, arabinoxylanase (CtXyl5At) from Clostridium thermocellum, belonging to subfamily 34 of glycoside hydrolase (GH) family 5 was investigated pertaining to its specificity for highly-substituted regions in the arabinoxylan-backbone. CtXyl5At preferentially hydrolysed the water-soluble fraction of alkali-extracted arabinoxylan. AXOS with DP 2-4 were determined as major products from CtXyl5At catalyzed hydrolysis. Increase in AXOS yield was observed with enzyme synergy, involving an initial treatment of soluble arabinoxylan with a GH43 α-l-arabinofuranosidase from Bifidobacterium adolescentis termed BaAXHd3 (30°C, 6h), followed by hydrolysis with CtXyl5At (50°C, 24h). The prebiotic potential of AXOS was shown by growth analysis using the human gut bacteria Bifidobacterium adolescentis ATCC 15703 and Roseburia hominis DSM 6839. Importantly, AXOS were utilized by the bacteria and short-chain fatty acids were produced.

Hide Abstract
Publication

Symbiont Digestive Range Reflects Host Plant Breadth in Herbivorous Beetles.

Salem, H., Kirsch, R., Pauchet, Y., Berasategui, A., Fukumori, K., Moriyama, M., et al. (2020). Current Biology, 30(15), 2875-2886

Numerous adaptations are gained in light of a symbiotic lifestyle. Here, we investigated the obligate partnership between tortoise leaf beetles (Chrysomelidae: Cassidinae) and their pectinolytic Stammera symbionts to detail how changes to the bacterium’s streamlined metabolic range can shape the digestive physiology and ecological opportunity of its herbivorous host. Comparative genomics of 13 Stammera strains revealed high functional conservation, highlighted by the universal presence of polygalacturonase, a primary pectinase targeting nature’s most abundant pectic class, homogalacturonan (HG). Despite this conservation, we unexpectedly discovered a disparate distribution for rhamnogalacturonan lyase, a secondary pectinase hydrolyzing the pectic heteropolymer, rhamnogalacturonan I (RG-I). Consistent with the annotation of rhamnogalacturonan lyase in Stammera, cassidines are able to depolymerize RG-I relative to beetles whose symbionts lack the gene. Given the omnipresence of HG and RG-I in foliage, Stammera that encode pectinases targeting both substrates allow their hosts to overcome a greater diversity of plant cell wall polysaccharides and maximize access to the nutritionally rich cytosol. Possibly facilitated by their symbionts’ expanded digestive range, cassidines additionally endowed with rhamnogalacturonan lyase appear to utilize a broader diversity of angiosperms than those beetles whose symbionts solely supplement polygalacturonase. Our findings highlight how symbiont metabolic diversity, in concert with host adaptations, may serve as a potential source of evolutionary innovations for herbivorous lineages.

Hide Abstract
Publication

Enzyme-aided xylan extraction from alkaline-sulfite pretreated sugarcane bagasse and its incorporation onto eucalyptus kraft pulps.

Cornetti, A. A. A., A., Ferraz, A. & Milagres, A. M. (2020). Carbohydrate Research, 108003.

Hemicellulose-rich substrates produced in the lignocellulose biorefinery context can yield macromolecular xylan structures with assorted application in the chemical industry. Xylan presents natural affinity to cellulose and its incorporation onto fibers increases the physical processability of pulp; however, current studies diverge on how molar mass affects xylan interaction with cellulose. In the current work, xylans with varied structural characteristics were prepared from alkaline-sulfite pretreated sugarcane bagasse with aid of an alkaline-active xylanase and selective precipitations using different ethanol concentrations. Prepared xylan fractions, containing low levels of lignin contamination (4-9%) and molar masses ranging from 2.3 kDa to 34 kDa, were incorporated onto eucalyptus pulp fibers up to 4.7 g xylan/100 g pulp. The efficiency of xylan incorporation onto cellulosic fibers was dependent on the xylan structures, where low molar mass and low substitution degree favored high incorporation levels.

Hide Abstract
Publication

High Enzymatic Recovery and Purification of Xylooligosaccharides from Empty Fruit Bunch via Nanofiltration.

Wijaya, H., Sasaki, K., Kahar, P., Rahmani, N., Hermiati, E., Yopi, Y., Ogino, C. Prasetya, B. & Kondo, A. (2020). Processes, 8(5), 619.

Xylooligosaccharides (XOS) are attracting an ever-increasing amount of interest for use as food prebiotics. In this study, we used efficient membrane separation technology to convert lignocellulosic materials into a renewable source of XOS. This study revealed a dual function of nanofiltration membranes by first achieving a high yield of xylobiose (a main component of XOS) from alkali-pretreated empty fruit bunch (EFB) hydrolysate, and then by achieving a high degree of separation for xylose as a monosaccharide product. Alkali pretreatment could increase the xylan content retention of raw EFB from 23.4% to 26.9%, which eventually contributed to higher yields of both xylobiose and xylose. Nanofiltration increased the total amount of XYN10Ks_480 endoxylanase produced from recombinant Streptomyces lividans 1326 without altering its specific activity. Concentrated XYN10Ks_480 endoxylanase was applied to the recovery of both xylobiose and xylose from alkali-pretreated EFB hydrolysate. Xylobiose and xylose yields reached 41.1% and 17.3%, respectively, and when unconcentrated XYN10Ks_480 endoxylanase was applied, those yields reached 35.1% and 8.3%, respectively. The last step in nanofiltration was to separate xylobiose over xylose, and 41.3 g.L−1 xylobiose (90.1% purity over xylose) was achieved. This nanofiltration method should shorten the processes used to obtain XOS as a high-value end product from lignocellulosic biomass.

Hide Abstract
Publication

Isolation and Characterization of a Novel Cold-Active, Halotolerant Endoxylanase from Echinicola rosea Sp. Nov. JL3085T.

He, J., Liu, L., Liu, X. & Tang, K. (2020). Marine Drugs, 18(5), 245.

We cloned a xylanase gene (xynT) from marine bacterium Echinicola rosea sp. nov. JL3085T and recombinantly expressed it in Escherichia coli BL21. This gene encoded a polypeptide with 379 amino acid residues and a molecular weight of ~43 kDa. Its amino acid sequence shared 45.3% similarity with an endoxylanase from Cellvibrio mixtus that belongs to glycoside hydrolases family 10 (GH10). The XynT showed maximum activity at 40°C and pH 7.0, and a maximum velocity of 62 μmoL min−1 mg−1. The XynT retained its maximum activity by more than 69%, 51%, and 26% at 10°C, 5°C, and 0°C, respectively. It also exhibited the highest activity of 135% in the presence of 4 M NaCl and retained 76% of its activity after 24 h incubation with 4 M NaCl. This novel xylanase, XynT, is a cold-active and halotolerant enzyme that may have promising applications in drug, food, feed, and bioremediation industries.

Hide Abstract
Publication

Oligosaccharides from rice straw and rice husks produced by glycoside hydrolase family 10 and 11 xylanases.

Pattarapisitporn, A., Jaichakan, P. & Klangpetch, W. (2020). Asia-Pacific Journal of Science and Technology, 25(01).

Rice straw (RS) and rice husks (RH) are the by-products obtained from rice farming, which are the remaining non-starch polysaccharides, called cellulose and hemicellulose. The objectives of this study were to investigate the abilities of the glycoside hydrolase family 10 (GH10) and 11 (GH11) commercial xylanases on the production of oligosaccharides from RS and RH by hydrothermal assisted enzymatic hydrolysis. Firstly, RS and RH were pretreated with acetone/ethanol. Then the pretreated biomass was heated by autoclave at 180˚C for 10-30 min. The oligosaccharides content in the RS and RH hydrolysates (HRS and HRH) were analyzed by High Performance Anion Exchange Chromatography (HPAEC-PAD). The results indicated that RS and RH treated for 10 min had shown the highest total oligosaccharides content. After that, the HRS and HRH were hydrolyzed with Ultraflo Max (UM10) and Ultraflo L (UL11), belonged to GH10 and GH11 respectively, under condition at 50˚C pH of 6.0 for 0-4 h. The highest sugar-reducing content was found while incubating HRS and HRH for 1 h with the aforementioned xylanases. The sugar-reducing contents of HRS and HRH treated with UM10 increased up to 0.24% and 0.17%, respectively, whereas those treated with UL11 increased up to 0.18% and 0.14%, respectively. The results revealed that HRS and HRH treated with UM10 had mainly consisted of xylobiose, while those treated with UL11 had mainly consisted of xylotriose. This study has suggested the potential of GH10 and GH11 xylanases on Xylooligosaccharide (XOS) production using RS and RH as alternative sources.

Hide Abstract
Publication

Inter domain interactions influence the substrate affinity and hydrolysis product specificity of xylanase from Streptomyces chartreusis L1105.

Xiong, K., Yan, Z. X., Liu, J. Y., Pei, P. G., Deng, L., Gao, L. & Sun, B. G. (2020). Annals of Microbiology, 70, 1-12.

Purpose: This study investigated the influence of inter-domain interactions on the substrate affinity and hydrolysis product specificity of xylanase. Methods: Genes encoding a GH10 endo-xylanase from Streptomyces chartreusis L1105 xynA and its truncated derivative were cloned and expressed in Escherichia coli. The catalytic activities of the enzyme (xynA) and the derivative xynADCBM, lacking the carbohydrate binding module (CBM), were assessed to evaluate the role of CBM in xynA. Results: Recombinant xynA (44 kDa) was found to be optimally active on beechwood xylan at 65°C with pH 7.7, while xynADCBM (34 kDa) exhibited optimal activity at 65°C with pH 7.2. Additionally, xynA and xynADCBM were found to be highly thermostable at 40-60°C, each retaining 80% of their original activity after 30 min. The xynADCBM without the CBM domain was highly efficient at hydrolyzing xylan to produce xylobiose (over 67%), which may be because the CBM domain facilitates substrate binding with xylanase. Meanwhile, the xylan hydrolysis efficiency of xynADCBM was higher than that of xynA. Conclusion: These findings showed that the CBM domain with non-catalytic activity has no significant effect on the characteristics of the enzyme at optimum pH and pH tolerance. It has also been suggested that the derivative xynADCBM without CBM components can promote hydrolysis of xylan to yield xylooligosaccharides, which has great potential economic benefits.

Hide Abstract
Publication

Enzymatic Hydrolysis of Xylan from Coffee Parchment in Membrane Bioreactors.

Acosta-Fernández, R., Poerio, T., Nabarlatz, D., Giorno, L., & Mazzei, R. (2020). Industrial & Engineering Chemistry Research, 59(16), 7346-7354.

Xylooligosaccharides (XOs) production from xylan, extracted from coffee parchment, using two stirred tank reactors (STRs) and two membrane bioreactors (MBRs) was studied for the first time. In the reactors, xylanase either free in a solution (E-STR, E-MBR) or covalently immobilized on magnetic nanoparticles (MNP-STR, MNP-MBR) was used. A continuous production of reducing sugars in both MBRs was obtained. In the E-MBR, the same conversion of E-STR at a low substrate concentration (1 mg mL-1) (97%) was obtained. At higher substrate concentration, the conversion increases by a quarter in E-MBR on increasing the residence time and doubles in MNP-MBR by increasing the amount of immobilized enzyme. The unchanged apparent KM (about 8 mg mL-1) showed that the affinity of the enzyme for the substrate was not altered by the immobilization process. In E-MBR, the enzyme/substrate affinity is even improved (KM: 2.58 mg mL-1), thanks to the continuous removal of the inhibition products, present in the initial xylan solution, by the membrane process.

Hide Abstract
Publication

Production of xylooligosaccharides from xylan catalyzed by endo-1, 4-β-D-xylanase-immobilized nanoscale carbon, silica and zirconia matrices.

Shivudu, G., Chandraraj, K. & Selvam, P. (2020). Molecular Catalysis, 484, 110745.

Nanoscale materials of carbon, silica and zirconia were used to immobilize a recombinant endo-1, 4-β-D-xylanase (XynC) of Bsubtilis KCX006. The adsorption of endo-1, 4-β-D-xylanase on nanomaterials of carbon, silica and zirconia followed the pseudo-second-order kinetic model. The activation energies for adsorption of endoxylanase on carbon, silica and zirconia nanomaterials were 9.94 kJ mol−1, 40.44 kJ mol−1 and 16.33 kJ mol−1 respectively. The recovered activity (RA) of endoxylanase immobilized on carbon, silica and zirconia nanomaterials was in the range of 52%–92%. The endoxylanase immobilized on zirconia nanoparticles showed maximum RA. All immobilized endoxylanase showed optimum activity at pH 6.6 similar to that of free/soluble endoxylanase. But compared to free endoxylanase, all immobilized endoxylanase had broad optimum temperature range (50-65°C) for catalytic activity. The Michaelis-Menten constant (Km) increased for all immobilized endoxylanase due to substrate diffusion limit. The endoxylanase immobilized on above nanomaterials was used repeatedly for XOS production from xylan. All immobilized endoxylanase produced X2-X6 and substituted XOS similar to free endoxylanase from beechwood xylan and extracted crude xylans from sorghum and sugarcane bagasse. The endoxylanase immobilized on above nanoparticles did not lose activity after five batches of repeated use. The results showed that endoxylanase immobilized on carbon, silica and zirconia matrices would be useful for production of XOS by enzyme recycling.

Hide Abstract
Publication

Modified-dietary fiber from cassava pulp reduces abdominal fat and meat cholesterol contents without affecting growth performance of broiler chickens.

Okrathok, S. & Khempaka, S. (2020). Journal of Applied Poultry Research, 29(1), 229-239. 

This study aimed to investigate the effects of modified-dietary fiber from cassava pulp (M-DFCP), mostly classified as insoluble dietary fiber (IDF), as a feed supplement on productive performance, nutrient digestibility, weight of digestive organs, abdominal fat storage, and cholesterol in meat and blood of broiler chickens. A total of 336 one-day-old male broiler chickens (Ross 308) were allocated to 4 groups in 7 replicate pens with 12 chicks each, based on a completely randomized design. Four dietary treatments composed of control and 3 M-DFCP inclusion levels: 0.5, 1.0, and 1.5%. The results showed that M-DFCP showed no negative effects on growth performance in broiler chickens. The inclusion of M-DFCP in diets at 1.0 to 1.5% had positive effects on increased gizzard weight, reduced gizzard pH, and reduced abdominal fat. The M-DFCP at 1.0% can also increase nutrient digestibility (dry matter, organic matter, and ether extract). In addition, the supplementation of M-DFCP at 1.0 to 1.5% in diets represented lower cholesterol in serum, breast and thigh meats, and liver of broiler chickens. In conclusion, these results indicate that M-DFCP can be used as an IDF source in broiler diets. The inclusion of 1.0% M-DFCP in broiler diet has positive effects on enhancing gizzard function, improving nutrient digestibility, and reducing abdominal fat and cholesterol in chicken meat, blood, and liver.

Hide Abstract
Publication

In vitro versus in situ evaluation of xylan hydrolysis into xylo-oligosaccharides in broiler chicken gastrointestinal tract.

Morgan, N. K., Wallace, A., Bedford, M. R., Hawking, K. L., Rodrigues, I., Hilliar, M. & Choct, M. (2020). Carbohydrate Polymers, 230, 115645.

Xylan hydrolysis into xylo-oligosaccharides (XOS) was evaluated both in the gizzard and ileum of broiler chickens, and by a 2-step in vitro digestion assay that simulated the pH, temperature and time period of the gastric and small intestine (SI) phases. Twelve dietary treatments with varying soluble and insoluble xylan levels, either with or without supplemental xylanase, were fed to broiler chickens (n = 576) for the in situ analysis, and were exposed to the in vitro assay. Relatedness of the two methods was strong for determination of XOS production in all dietary treatments for X5, X4, X3, X2 and X1, respectively, in both the gastric (r = 0.980, 0.853, 0.894, 0.870 and 0.951) and small intestine phase (r = 0.957, 0.923, 0.940, 0.970, 0.969) (P < 0.05). Consequently, the in vitro assay was used to illustrated the diversity of XOS production across different batches of wheat and barley in the presence of xylanase.

Hide Abstract
Publication

Production of xylooligosaccharides and monosaccharides from hydrogen peroxide-acetic acid-pretreated poplar by two-step enzymatic hydrolysis.

Hao, X., Wen, P., Wang, J., Wang, J., You, J. & Zhang, J. (2020). Bioresource Technology, 297, 122349.

The severe pretreatment of poplar makes xylan difficult to utilize efficiently. In this work, poplar was pretreated by hydrogen peroxide-acetic acid (HPAC) with H2SO4 as catalyst to remove lignin, and the solid residues were used to produce xylooligosaccharides (XOS) and monosaccharides by two-step xylanase and cellulase hydrolysis. The results indicated that higher H2SO4 concentrations in the HPAC pretreatment of poplar afforded stronger lignin removal ability. An increased XOS yield of 19.8% was obtained from 200 mM H2SO4-catalyzed poplar by xylanase and the XOS purity was high, with a very low xylose/XOS ratio of 0.14. Higher glucose (75.2%) and xylose (61.4%) yields were obtained from the HPAC-pretreated poplar using 50 mM H2SO4 as catalyst. Finally, 16.9 g XOS and 296.4 g glucose were produced from 1 kg poplar by xylanase and cellulase. This study provides a method for producing functional XOS and monosaccharides from poplar using a simple reduced-pollution strategy.

Hide Abstract
Publication

Pilot-scale production of xylo-oligosaccharides and fermentable sugars from Miscanthus using steam explosion pretreatment.

Bhatia, R., Winters, A., Bryant, D. N., Bosch, M., Clifton-Brown, J., Leak, D. & Gallagher, J. (2020). Bioresource Technology, 296, 122285.

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.

Hide Abstract
Publication

Comparison of Japanese and Indian intestinal microbiota shows diet-dependent interaction between bacteria and fungi.

Pareek, S., Kurakawa, T., Das, B., Motooka, D., Nakaya, S., Rongsen-Chandola, T. et al. (2019). NPJ Biofilms and Microbiomes, 5(1), 1-13.

The bacterial species living in the gut mediate many aspects of biological processes such as nutrition and activation of adaptive immunity. In addition, commensal fungi residing in the intestine also influence host health. Although the interaction of bacterium and fungus has been shown, its precise mechanism during colonization of the human intestine remains largely unknown. Here, we show interaction between bacterial and fungal species for utilization of dietary components driving their efficient growth in the intestine. Next generation sequencing of fecal samples from Japanese and Indian adults revealed differential patterns of bacterial and fungal composition. In particular, Indians, who consume more plant polysaccharides than Japanese, harbored increased numbers of Prevotella and CandidaCandida spp. showed strong growth responses to the plant polysaccharide arabinoxylan in vitro. Furthermore, the culture supernatants of Candida spp. grown with arabinoxylan promoted rapid proliferation of Prevotella copri. Arabinose was identified as a potential growth-inducing factor in the Candida culture supernatants. Candida spp. exhibited a growth response to xylose, but not to arabinose, whereas P. copri proliferated in response to both xylose and arabinose. Candida spp., but not P. copri, colonized the intestine of germ-free mice. However, P. copri successfully colonized mouse intestine already harboring Candida. These findings demonstrate a proof of concept that fungal members of gut microbiota can facilitate a colonization of the intestine by their bacterial counterparts, potentially mediated by a dietary metabolite.

Hide Abstract
Publication

Secondary lactic acid bacteria fermentation with wood-derived xylooligosaccharides as a tool to expedite sour beer production.

Dysvik, A., La Rosa, S. L., Buffetto, F., Liland, K. H., Myhrer, K. S., Rukke, E. O., Wicklund, T. & Westereng, B. (2019). Journal of Agricultural and Food Chemistry, 68(1), 301-314.

Xylooligosaccharides (XOS) from woody biomass were evaluated as a substrate for secondary lactic acid bacteria (LAB) fermentation in sour beer production. XOS were extracted from birch (Betula pubescens) and added to beer to promote the growth of Lactobacillus brevis BSO 464. Growth, pH, XOS degradation, and metabolic products were monitored throughout fermentations, and the final beer was evaluated sensorically. XOS were utilized, metabolic compounds were produced (1800 mg/L lactic acid), and pH was reduced from 4.1 to 3.6. Secondary fermentation changed sensory properties significantly, and the resulting sour beer was assessed as similar to a commercial reference in multiple attributes, including acidic taste. Overall, secondary LAB fermentation induced by wood-derived XOS provided a new approach to successfully produce sour beer with reduced fermentation time (from 1-3 years to 4 weeks). The presented results demonstrate how hemicellulosic biomass can be valorized for beverage production and to obtain sour beer with improved process control.

Hide Abstract
Safety Information
Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
Customers also viewed
Total Starch Assay Kit AA/AMG K-TSTA TSTA
Total Starch Assay Kit (AA/AMG)
€155.00
23-(4-O-Methyl-α-D-Glucuronyl)-xylotriose
23-(4-O-Methyl-α-D-Glucuronyl)-xylotriose
€166.00
22-(4-O-Methyl-α-D-Glucuronyl)-xylobiose
22-(4-O-Methyl-α-D-Glucuronyl)-xylobiose
€146.00
Beta-Nicotinamide Adenine Dinucleotide Phosphate (NADP+), Oxidised Sodium Salt, C-NADP
β-Nicotinamide Adenine Dinucleotide Phosphate (NADP+), Oxidised Sodium Salt
€173.00
Cellotetraose
Cellotetraose
€165.00
Cellotriose
Cellotriose
€156.00
23,33-di-α-L-Arabinofuranosyl-xylotriose (A2,3XX)
23,33-di-α-L-Arabinofuranosyl-xylotriose (A2,3XX)
€164.00
Protease (Subtilisin A from Bacillus licheniformis)
Protease (Subtilisin A from Bacillus licheniformis)
€86.00