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|Storage Temperature:||Below -10oC|
|Stability:||> 10 years under recommended storage conditions|
|Synonyms:||Cellotriosyl-(1→3)-β-D-Glucose, 1,3:1,4-β-Glucotetraose B|
|Substrate For (Enzyme):||β-Glucanase/Lichenase|
High purity 31-β-D-Cellotriosyl-glucose for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
Tetrasaccharide produced on hydrolysis of 1:3,1:4-β-D-glucan by lichenase.
33-β-D-Glucosyl-cellotriose O-CTR-50MG - Cellotriose O-CTE-50MG - Cellotetraose O-CPE-20MG - Cellopentaose O-CHE - Cellohexaose O-CTRRD - 1,4-β-D-Cellotriitol (borohydride reduced) O-CTERD - 1,4-β-D-Cellotetraitol (borohydride reduced) O-CPERD - 1,4-β-D-Cellopentaitol (borohydride reduced) O-CHERD - 1,4-β-D-Cellohexaitol (borohydride reduced) P-BGBL - β-Glucan (Barley; Low Viscosity)
(Bacillus subtilis) E-LICACT - Non-specific endo-1,3(4)-β-Glucanase
(Clostridium thermocellum) E-CELTR - Cellulase (endo-1,4-β-D-glucanase)
(Trichoderma longibrachiatum) E-BGLUC - β-Glucosidase (Aspergillus niger) E-BGOSAG - β-Glucosidase (Agrobacterium sp.) E-BGOSPC - β-Glucosidase (Phanerochaete chrysosporium) E-BGOSTM - β-Glucosidase (Thermotoga maritima) E-EXBGOS - exo-1,3-β-D-Glucanase + β-Glucosidase
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
FGB1 and WSC3 are in planta‐induced β‐glucan‐binding fungal lectins with different functions.
Wawra, S., Fesel, P., Widmer, H., Neumann, U., Lahrmann, U., Becker, S., Hehemann, J. H., Langen, G. & & Zuccaro, A. (2019). New Phytologist, 222(3), 1493-1506.
In the root endophyte Serendipita indica, several lectin‐like members of the expanded multigene family of WSC proteins are transcriptionally induced in planta and are potentially involved in β-glucan remodeling at the fungal cell wall. Using biochemical and cytological approaches we show that one of these lectins, SiWSC3 with three WSC domains, is an integral fungal cell wall component that binds to long‐chain β1‐3‐glucan but has no affinity for shorter β1‐3‐ or β1‐6‐linked glucose oligomers. Comparative analysis with the previously identified β-glucan‐binding lectin SiFGB1 demonstrated that whereas SiWSC3 does not require β1‐6‐linked glucose for efficient binding to branched β1‐3‐glucan, SiFGB1 does. In contrast to SiFGB1, the multivalent SiWSC3 lectin can efficiently agglutinate fungal cells and is additionally induced during fungus-fungus confrontation, suggesting different functions for these two β-glucan‐binding lectins. Our results highlight the importance of the β-glucan cell wall component in plant–fungus interactions and the potential of β-glucan‐binding lectins as specific detection tools for fungi in vivo.Hide Abstract
Hughes, S. A., Shewry, P. R., Gibson, G. R., McCleary, B. V. & Rastall, R. A. (2008). FEMS Microbiology Ecology, 64(3), 482-493.
Fermentation of β-glucan fractions from barley [average molecular mass (MM), of 243, 172, and 137 kDa] and oats (average MM of 230 and 150 kDa) by the human faecal microbiota was investigated. Fractions were supplemented to pH-controlled anaerobic batch culture fermenters inoculated with human faecal samples from three donors, in triplicate, for each substrate. Microbiota changes were monitored by fluorescent in situ hybridization; groups enumerated were: Bifidobacterium genus, Bacteroides and Prevotella group, Clostridium histolyticum subgroup, Ruminococcus-Eubacterium-Clostridium (REC) cluster, Lactobacillus-Enterococcus group, Atopobium cluster, and clostridial cluster IX. Short-chain fatty acids and lactic acid were measured by HPLC. The C. histolyticum subgroup increased significantly in all vessels and clostridial cluster IX maintained high populations with all fractions. The Bacteroides-Prevotella group increased with all but the 243-kDa barley and 230-kDa oat substrates. In general β-glucans displayed no apparent prebiotic potential. The SCFA profile (51 : 32 : 17; acetate : propionate : butyrate) was considered propionate-rich. In a further study a β-glucan oligosaccharide fraction was produced with a degree of polymerization of 3-4. This fraction was supplemented to small-scale faecal batch cultures and gave significant increases in the Lactobacillus-Enterococcus group; however, the prebiotic potential of this fraction was marginal compared with that of inulin.Hide Abstract
Mechelke, M., Herlet, J., Benz, J. P., Schwarz, W. H., Zverlov, V. V., Liebl, W. & Kornberger, P. (2017). Analytical and Bioanalytical Chemistry, 1-13.
The rising importance of accurately detecting oligosaccharides in biomass hydrolyzates or as ingredients in food, such as in beverages and infant milk products, demands for the availability of tools to sensitively analyze the broad range of available oligosaccharides. Over the last decades, HPAEC-PAD has been developed into one of the major technologies for this task and represents a popular alternative to state-of-the-art LC-MS oligosaccharide analysis. This work presents the first comprehensive study which gives an overview of the separation of 38 analytes as well as enzymatic hydrolyzates of six different polysaccharides focusing on oligosaccharides. The high sensitivity of the PAD comes at cost of its stability due to recession of the gold electrode. By an in-depth analysis of the sensitivity drop over time for 35 analytes, including xylo- (XOS), arabinoxylo- (AXOS), laminari- (LOS), manno- (MOS), glucomanno- (GMOS), and cellooligosaccharides (COS), we developed an analyte-specific one-phase decay model for this effect over time. Using this model resulted in significantly improved data normalization when using an internal standard. Our results thereby allow a quantification approach which takes the inevitable and analyte-specific PAD response drop into account.Hide Abstract