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22-(4-O-Methyl-α-D-Glucuronyl)-xylotriose

22-4-O-Methyl-alpha-D-Glucuronosyl-xylotriose O-XUX
Product code: O-XUX
€146.00

10 mg

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Content: 10 mg
Shipping Temperature: Ambient
Storage Temperature: Below -10oC
Physical Form: Powder
Stability: > 10 years under recommended storage conditions
CAS Number: 103784-24-3
Molecular Formula: C22H36O19
Molecular Weight: 604.5
Purity: > 90%
Substrate For (Enzyme): endo-1,4-β-Xylanase, α-Glucuronidase

High purity 22-(4-O-Methyl-α-D-Glucuronyl)-xylotriose for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

Documents
Certificate of Analysis
Safety Data Sheet
Data Sheet
Publications
Publication

Unique features of the bifunctional GH30 from Thermothelomyces thermophila revealed by structural and mutational studies.

Nikolaivits, E., Pentari, C., Kosinas, C., Feiler, C. G., Spiliopoulou, M., Weiss, M. S., Dimarogona, M. & Topakas, E. (2021). Carbohydrate Polymers, 273, 118553.

Fungal xylanases belonging to family GH30_7, initially categorized as endo-glucuronoxylanases, are now known to differ both in terms of substrate specificity, as well as mode of action. Recently, TtXyn30A, a GH30_7 xylanase from Thermothelomyces thermophila, was shown to possess dual activity, acting on the xylan backbone in both an endo- and an exo- manner. Here, in an effort to identify the structural characteristics that append these functional properties to the enzyme, we present the biochemical characterization of various TtXyn30A mutants as well as its crystal structure, alone, and in complex with the reaction product. An auxiliary catalytic amino acid has been identified, while it is also shown that glucuronic acid recognition is not mediated by a conserved arginine residue, as shown by previously determined GH30 structures.

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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

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.

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Safety Information
Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
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