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Laminaribiose

Laminaribiose O-LAM2
Product code: O-LAM2
€240.00

50 mg

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Content: 50 mg
Shipping Temperature: Ambient
Storage Temperature: Ambient
Physical Form: Powder
Stability: > 2 years under recommended storage conditions
CAS Number: 34980-39-7
Molecular Formula: C12H22O11
Molecular Weight: 342.3
Purity: > 95%
Substrate For (Enzyme): exo-1,3-β-Glucanase, β-Glucosidase

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

Documents
Certificate of Analysis
Safety Data Sheet
Data Sheet
Publications
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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New colours for old in the blue-cheese fungus Penicillium roqueforti.

Cleere, M. M., Novodvorska, M., Geib, E., Whittaker, J., Dalton, H., Salih, N., Hewitt, S., Kokolski, M. Brock, M. & Dyer, P. S. (2024). npj Science of Food, 8(1), 3.

Penicillium roqueforti is used worldwide in the production of blue-veined cheese. The blue-green colour derives from pigmented spores formed by fungal growth. Using a combination of bioinformatics, targeted gene deletions, and heterologous gene expression we discovered that pigment formation was due to a DHN-melanin biosynthesis pathway. Systematic deletion of pathway genes altered the arising spore colour, yielding white to yellow-green to red-pink-brown phenotypes, demonstrating the potential to generate new coloured strains. There was no consistent impact on mycophenolic acid production as a result of pathway interruption although levels of roquefortine C were altered in some deletants. Importantly, levels of methyl-ketones associated with blue-cheese flavour were not impacted. UV-induced colour mutants, allowed in food production, were then generated. A range of colours were obtained and certain phenotypes were successfully mapped to pathway gene mutations. Selected colour mutants were subsequently used in cheese production and generated expected new colourations with no elevated mycotoxins, offering the exciting prospect of use in future cheese manufacture.

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Plant immunity suppression by an exo-β-1, 3-glucanase and an elongation factor 1α of the rice blast fungus. 

Liu, H., Lu, X., Li, M., Lun, Z., Yan, X., Yin, C., .et al. (2023). Nature Communications, 14(1), 5491.

Fungal cell walls undergo continual remodeling that generates β-1,3-glucan fragments as products of endo-glycosyl hydrolases (GHs), which can be recognized as pathogen-associated molecular patterns (PAMPs) and trigger plant immune responses. How fungal pathogens suppress those responses is often poorly understood. Here, we study mechanisms underlying the suppression of β-1,3-glucan-triggered plant immunity by the blast fungus Magnaporthe oryzae. We show that an exo-β-1,3-glucanase of the GH17 family, named Ebg1, is important for fungal cell wall integrity and virulence of M. oryzae. Ebg1 can hydrolyze β-1,3-glucan and laminarin into glucose, thus suppressing β-1,3-glucan-triggered plant immunity. However, in addition, Ebg1 seems to act as a PAMP, independent of its hydrolase activity. This Ebg1-induced immunity appears to be dampened by the secretion of an elongation factor 1 alpha protein (EF1α), which interacts and co-localizes with Ebg1 in the apoplast. Future work is needed to understand the mechanisms behind Ebg1-induced immunity and its suppression by EF1α.

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Biochemical and structural characterization of a glucan synthase GFGLS2 from edible fungus Grifola frondosa to synthesize β-1, 3-glucan.

Yang, Y. M., Fu, X., Cui, F. J., Sun, L., Zan, X. Y. & Sun, W. J. (2023). Biotechnology for Biofuels and Bioproducts, 16(1), 163.

Background: Grifola frondosa is a Basidiomycete fungus belonging to the family of Grifolaceae and the order of Polyporales. β-Glucans are the main polymers in G. frondosa, playing a crucial role in the physiology and representing the healthy benefits for humans. The membrane-integrated β-1, 3-glucan synthase (GLS) is responsible for glucan synthesis, cell wall assembly, differentiation and growth of the edible fungi. However, the structural/catalytic characteristics and mechanisms of β-1, 3-glucan synthases in G. frondosa are still unknown due to their extremely complex structures with multi-transmembranes and large molecular masses. Results: Herein, a β-1, 3-glucan synthase (GFGLS2) was purified and identified from the cultured mycelia with a specific activity of 60.01 pmol min−1 μg−1 for the first time. The GFGLS2 showed a strict specificity to UDP-glucose with a Vmax value of 1.29 ± 0.04 µM min−1 at pH 7.0 and synthesized β-1, 3-glucan with a maximum degree of polymerization (DP) of 62. Sequence Similarity Network (SSN) analysis revealed that GFGLS2 has a close relationship with others in Ganoderma sinenseTrametes coccineaPolyporus brumalis, and Trametes pubescens. With the assistance of 3D structure modelling by AlphaFold 2, molecular docking and molecular dynamics simulations, the central hydrophilic domain (Class III) in GFGLS2 was the main active sites through binding the substrate UDP–glucose to 11 amino acid residues via hydrogen bonds, π-stacking and salt bridges. Conclusions: The biochemical, 3D structural characterization and potential catalytic mechanism of a membrane-bound β-1, 3-glucan synthase GFGLS2 from cultured mycelia of G. frondosa were well investigated and would provide a reasonable full picture of β-1, 3-glucan synthesis in fungi.

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Utilization of dietary mixed-linkage β-glucans by the Firmicute Blautia producta.

Singh, R. P., Niharika, J., Thakur, R., Wagstaff, B. A., Kumar, G., Kurata, R., Patel, D., Levy, C. W., Miyazaki, T. & Field, R. A. (2023). Journal of Biological Chemistry, 299(6).

The β-glucans are structurally varied, naturally occurring components of the cell walls, and storage materials of a variety of plant and microbial species. In the human diet, mixed-linkage glucans [MLG - β-(1,3/4)-glucans] influence the gut microbiome and the host immune system. Although consumed daily, the molecular mechanism by which human gut Gram-positive bacteria utilize MLG largely remains unknown. In this study, we used Blautia producta ATCC 27340 as a model organism to develop an understanding of MLG utilization. B. producta encodes a gene locus comprising a multi-modular cell-anchored endo-glucanase (BpGH16MLG), an ABC transporter, and a glycoside phosphorylase (BpGH94MLG) for utilizing MLG, as evidenced by the upregulation of expression of the enzyme- and solute binding protein (SBP)-encoding genes in this cluster when the organism is grown on MLG. We determined that recombinant BpGH16MLG cleaved various types of β-glucan, generating oligosaccharides suitable for cellular uptake by B. producta. Cytoplasmic digestion of these oligosaccharides is then performed by recombinant BpGH94MLG and β-glucosidases (BpGH3-AR8MLG and BpGH3-X62MLG). Using targeted deletion, we demonstrated BpSBPMLG is essential for B. producta growth on barley β-glucan. Furthermore, we revealed that beneficial bacteria, such as Roseburia faecis JCM 17581T, Bifidobacterium pseudocatenulatum JCM 1200T, Bifidobacterium adolescentis JCM 1275T, and Bifidobacterium bifidum JCM 1254, can also utilize oligosaccharides resulting from the action of BpGH16MLG. Disentangling the β-glucan utilizing the capability of B. producta provides a rational basis on which to consider the probiotic potential of this class of organism.

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Structural and mechanistic insights into fungal β-1, 3-glucan synthase FKS1.

Hu, X., Yang, P., Chai, C., Liu, J., Sun, H., Wu, Y., Zhang, M., Zhang, M, Liu, X. & Yu, H. (2023). Nature, 38, 1-9.

The membrane-integrated synthase FKS is involved in the biosynthesis of β-1,3-glucan, the core component of the fungal cell wall. FKS is the target of widely prescribed antifungal drugs, including echinocandin and ibrexafungerp. Unfortunately, the mechanism of action of FKS remains enigmatic and this has hampered development of more effective medicines targeting the enzyme. Here we present the cryo-electron microscopy structures of Saccharomyces cerevisiae FKS1 and the echinocandin-resistant mutant FKS1(S643P). These structures reveal the active site of the enzyme at the membrane-cytoplasm interface and a glucan translocation path spanning the membrane bilayer. Multiple bound lipids and notable membrane distortions are observed in the FKS1 structures, suggesting active FKS1-membrane interactions. Echinocandin-resistant mutations are clustered at a region near TM5-6 and TM8 of FKS1. The structure of FKS1(S643P) reveals altered lipid arrangements in this region, suggesting a drug-resistant mechanism of the mutant enzyme. The structures, the catalytic mechanism and the molecular insights into drug-resistant mutations of FKS1 revealed in this study advance the mechanistic understanding of fungal β-1,3-glucan biosynthesis and establish a foundation for developing new antifungal drugs by targeting FKS.

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Synergistic immunomodulatory effect of complex polysaccharides from seven herbs and their major active fractions.

Deng, Y., Xie, J., Luo, Z., Li, S. P. & Zhao, J. (2020). International Journal of Biological Macromolecules, 165, 530-541.

In this report, we present the strategy for the revelation of synergistic effect and elucidation of active fractions from an immunomodulatory complex polysaccharide derived from seven herbs (Lentinula edodes, Ganodorma lucidum, Tremella fuciformis, Chrysanthemum, Lycium barbarum, Codonopsis pilosula and Poria cocos), a formula used as health product in China market, using the combination of HPSEC-MALLS, immunological bioassay and saccharide mapping analysis. The effects of complex polysaccharide and their fractions on RAW 246.7 macrophages demonstrated that the fractions (CD1, CD2, CD3) with molecular weight above 10 kDa exhibited immune activity by directly stimulated NO release and phagocytosis, and induced macrophages to secrete cytokines. Especially, fraction CD2 with molecular weight of 100-1000 kDa showed the strongest bioactivity (EC50 = 0.19 μg/mL) compared with their individual corresponding herbal polysaccharides fractions due to synergistic effect, which supported the scientific use of Chinese herbal mixture. Moreover, their chemical characters were analyzed by HPSEC-MALLS and saccharide mapping, and the original herbs, including L. edodes, G. lucidum, T. fuciformis and Chrysanthemum, responsible for the immunomodulatory activity were tentatively revealed. Results are beneficial for the quality analysis and formula optimization of complex polysaccharides in both biomedical and functional food field.

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Degradative GH5 β-1, 3-1, 4-glucanase PpBglu5A for glucan in Paenibacillus polymyxa KF-1.

Yuan, Y., Zhang, X., Zhang, H., Wang, W., Zhao, X., Gao, J. & Zhou, Y. (2020). Process Biochemistry, 98, 183-192.

A novel β-1,3-1,4-glucanase in the glycoside hydrolase family 5 (GH5) has been identified in the secretome of Paenibacillus polymyxa KF-1. The recombinant GH5 enzyme PpBglu5A shows broad substrate specificity, with strong lichenase activity, medium β-1,3-glucanase activity, and minimal cellulase activity. Barley β-glucan, lichenan, curdlan, and carboxymethyl cellulose are hydrolyzed to varying degrees by PpBglu5A, with the highest catalytic activity being observed with barley β-glucan. Hydrolysates from barley β-glucan or lichenan are primarily glucan oligosaccharides with degrees of polymerization from 2 to 4. PpBglu5A also hydrolyzes oat bran into oligosaccharides mainly consisted of di-, tri-, and tetra- oligosaccharides that are useful in the preparation of gluco-oligosaccharides. In addition to hydrolytic activity, transglycosylation was also observed with PpBglu5A and cellotriose as substrate. An in vitro assay indicated that the recombinant PpBglu5A has antifungal activity and can inhibit the growth of Canidia albicans. These results suggest that PpBglu5A exhibits unique properties and may be useful as an antifungal agent.

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Taxogenomic assessment and genomic characterisation of Weissella cibaria strain 92 able to metabolise oligosaccharides derived from dietary fibres.

Anna, M., Phebe, V., Guðmundsdóttir, E. E., Santesson, S., Nilsson, A., Óli, H. G., Linares-Pasten, J. A. & Nordberg, K. E. (2020). Scientific Reports, 10(1), 5853.

The importance of the gut microbiota in human health has led to an increased interest to study probiotic bacteria. Fermented food is a source of already established probiotics, but it also offers an opportunity to discover new taxa. Four strains of Weissella sp. isolated from Indian fermented food have been genome sequenced and classified into the species W. cibaria based on whole-genome phylogeny. The genome of W. cibaria strain 92, known to utilise xylooligosaccharides and produce lactate and acetate, was analysed to identify genes for oligosaccharide utilisation. Clusters including genes involved in transportation, hydrolysis and metabolism of xylooligosaccharides, arabinooligosaccharides and β-glucosides were identified. Growth on arabinobiose and laminaribiose was detected. A 6-phospho-β-glucosidase clustered with a phosphotransferase system was found upregulated during growth on laminaribiose, indicating a mechanism for laminaribiose utilisation. The genome of W. cibaria strain 92 harbours genes for utilising the phosphoketolase pathway for the production of both acetate and lactate from pentose and hexose sugars but lacks two genes necessary for utilising the pentose phosphate pathway. The ability of W. cibaria strain 92 to utilise several types of oligosaccharides derived from dietary fibres, and produce lactate and acetate makes it interesting as a probiotic candidate for further evaluation.

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Amorphization and Semi-Dry Conversion of Crystalline Cellulose to Oligosaccharides by Impregnated Phosphoric Acid.

Hirayama, J., Kobayashi, H., & Fukuoka, A. (2020). Bulletin of the Chemical Society of Japan93(2), 273-278.

Efficient conversion of crystalline cellulose to useful chemicals is a grand challenge in biorefining. In this work, we report that amorphization and semi-dry conversion of crystalline cellulose to oligosaccharides is achieved by impregnated H3PO4. Specifically, the impregnation of crystalline cellulose with H3PO4 under 5 MPa of He and subsequent drying at room temperature produces amorphous cellulose. The impregnated H3PO4 likely permeates bulk phase cellulose by dissociating the hydrogen bonding network of cellulose during the treatment. The resulting swollen solid is depolymerized to oligosaccharides in 40% yield with 72% selectivity by heat-treatment at 100°C with no solvent. The analysis of obtained oligosaccharides using nuclear magnetic resonance and mass spectroscopy reveals that the products are oligomers of glucose linked by various kinds of glycosidic bonds that may be useful as prebiotics.

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Safety Data Sheet
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