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  • 1. Fairweather, J. K.
    et al.
    Him, J. L. K.
    Heux, L.
    Driguez, H.
    Bulone, Vincent
    KTH, Superseded Departments, Biotechnology.
    Structural characterization by C-13-NMR spectroscopy of products synthesized in vitro by polysaccharide synthases using C-13-enriched glycosyl donors: application to a UDP-glucose:(1 -> 3)-beta-D-glucan synthase from blackberry (Rubus fruticosus)2004In: Glycobiology, ISSN 0959-6658, E-ISSN 1460-2423, Vol. 14, no 9, p. 775-781Article in journal (Refereed)
    Abstract [en]

    A simple and sensitive method for the characterization of products synthesized in vitro by polysaccharide synthases is described. it relies on the use of C-13-enriched nucleotide sugars as substrates and on the analysis of the newly synthesized polysaccharides by C-13-nuclear magnetic resonance (NMR) spectroscopy. The method was validated with a (1-->3)-beta-D-glucan synthase from blackberry, but it may be applied to the study of any glycosyltransferase. The chemical synthesis of UDP-D-[U-C-13]glucose was achieved in a classical procedure with an overall yield of 50%. A uniformly labeled (1-->3)-beta-D-glucan was synthesized from this substrate, using detergent extracts of blackberry cell membranes as a source of synthase. One hundred micrograms of product was sufficient for liquid and solid-state C-13-NMR spectroscopy analyses. The method is at least 100 times more sensitive than in the case of non-enriched polysaccharides. It allows the unequivocal identification and direct structural characterization of the products synthesized in vitro, as opposed to conventional methods that rely on the use of radioactive substrates and enzymatic hydrolysis of the polysaccharides with specific glycoside hydrolases. The method proves that the glycan analyzed was synthesized de novo because the final product is enriched in C-13. Information on the 3D organization of the polymer may also be obtained by solid-state NMR spectroscopy.

  • 2. Greffe, L.
    et al.
    Bessueille, L.
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Synthesis, preliminary characterization, and application of novel surfactants from highly branched xyloglucan oligosaccharides2005In: Glycobiology, ISSN 0959-6658, E-ISSN 1460-2423, Vol. 15, no 4, p. 437-445Article in journal (Refereed)
    Abstract [en]

    A novel class of nonionic, carbohydrate-based surfactants has been synthesized from the plant polysaccharide xyloglucan. Enzymatic hydrolysis of xyloglucan yielded a series of well-defined, highly branched oligosaccharides that, following reductive amination, were readily conjugated with fatty acids bearing C-8 to C-18 chains under mild conditions. The critical micelle concentration, determined by tensiometry and dye-inclusion measurements, showed a typical dependence on acyl chain length and was sensitive to the degree of galactosylation of the head group. Several compounds from this new group of surfactants, especially those with C-14 and C-16 chains, were useful for the extraction of membrane-bound enzyme markers from different plant cell compartments in catalytically active form.

  • 3. Gunnarsson, Lavinia Cicortas
    et al.
    Zhou, Qi
    KTH, School of Biotechnology (BIO), Glycoscience.
    Montanier, Cedric
    Karlsson, Eva Nordberg
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ohlin, Mats
    Engineered xyloglucan specificity in a carbohydrate-binding module2006In: Glycobiology, ISSN 0959-6658, E-ISSN 1460-2423, Vol. 16, no 12, p. 1171-1180Article in journal (Refereed)
    Abstract [en]

    The field of plant cell wall biology is constantly growing and consequently so is the need for more sensitive and specific probes for individual wall components. Xyloglucan is a key polysaccharide widely distributed in the plant kingdom in both structural and storage tissues that exist in both fucosylated and non-fucosylated variants. Presently, the only xyloglucan marker available is the monoclonal antibody CCRC-M1 that is specific to terminal alpha-1,2-linked fucosyl residues on xyloglucan oligo- and polysaccharides. As a viable alternative to searches for natural binding proteins or creation of new monoclonal antibodies, an approach to select xyloglucan-specific binding proteins from a combinatorial library of the carbohydrate-binding module, CBM4-2, from xylanase Xyn10A of Rhodothermus marinus is described. Using phage display technology in combination with a chemoenzymatic method to anchor xyloglucan to solid supports, the selection of xyloglucan-binding modules with no detectable residual wild-type xylan and beta-glucan-binding ability was achieved.

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