Synthesis, preliminary characterization, and application of novel surfactants from highly branched xyloglucan oligosaccharides

Greffe, Lionel; Bessueille, Laurence; Bulone, Vincent; Brumer, Harry

doi:10.1093/glycob/cwi013

Cited by 43 publications

(38 citation statements)

References 64 publications

(80 reference statements)

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“…Remaining cell debris was removed by filtration through a Mini Capsule filter with a 0.45-mm pore size Versapor (Pall Europe) membrane. An affinity purification method was developed by coupling XGO-NH 2 (Greffe et al, 2005) to 6 mL of HiTrap NHS-activated HP medium (GE Healthcare) (column dimensions: diameter, 1.4 cm; height, 3 cm). The column material was pretreated according to the manufacturer's instructions.…”

Section: Mutagenesis Of Tm-nxg2 To Tm-nxg1 and Preparation Of Tm-nxg1mentioning

confidence: 99%

Structural Evidence for the Evolution of Xyloglucanase Activity from Xyloglucan Endo-Transglycosylases: Biological Implications for Cell Wall Metabolism

et al. 2007

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High-resolution, three-dimensional structures of the archetypal glycoside hydrolase family 16 (GH16) endo-xyloglucanases Tm-NXG1 and Tm-NXG2 from nasturtium (Tropaeolum majus) have been solved by x-ray crystallography. Key structural features that modulate the relative rates of substrate hydrolysis to transglycosylation in the GH16 xyloglucan-active enzymes were identified by structure–function studies of the recombinantly expressed enzymes in comparison with data for the strict xyloglucan endo-transglycosylase Ptt-XET16-34 from hybrid aspen (Populus tremula × Populus tremuloides). Production of the loop deletion variant Tm-NXG1-ΔYNIIG yielded an enzyme that was structurally similar to Ptt-XET16-34 and had a greatly increased transglycosylation:hydrolysis ratio. Comprehensive bioinformatic analyses of XTH gene products, together with detailed kinetic data, strongly suggest that xyloglucanase activity has evolved as a gain of function in an ancestral GH16 XET to meet specific biological requirements during seed germination, fruit ripening, and rapid wall expansion.

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Section: Mutagenesis Of Tm-nxg2 To Tm-nxg1 and Preparation Of Tm-nxg1mentioning

confidence: 99%

Structural Evidence for the Evolution of Xyloglucanase Activity from Xyloglucan Endo-Transglycosylases: Biological Implications for Cell Wall Metabolism

et al. 2007

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“…Trichoderma reesei EGII (TrCel5A) was a kind gift from Dr. Kathleen Piens, Gent University. Per-O-acetylated XXXG was produced from tamarind (Tamarindus indica) seed xyloglucan as previously described (Greffe et al, 2005;Ibatullin et al, 2008). Following conversion to the corresponding a-glycosyl bromide with 33% solution of HBr in glacial HOAc (Ibatullin et al, 2008), aglycone coupling was performed under phase-transfer conditions (Dess et al, 1981;Kleine et al, 1985): A solution of resorufin sodium salt (Aldrich; 1.5-2 mmol) and benzyltributylammonium chloride (Aldrich; 1 mmol) in water (10-15 mL) was added to a stirred solution of the a-glycosyl bromide (1 mmol) in CH 2 Cl 2 (15-20 mL), followed by vigorous stirring overnight at room temperature.…”

Section: Generalmentioning

confidence: 99%

A Real-Time Fluorogenic Assay for the Visualization of Glycoside Hydrolase Activity in Planta

Ibatullin

Banasiak²,

Baumann³

et al. 2009

Plant Physiol.

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There currently exists a diverse array of molecular probes for the in situ localization of polysaccharides, nucleic acids, and proteins in plant cells, including reporter enzyme strategies (e.g. protein-glucuronidase fusions). In contrast, however, there is a paucity of methods for the direct analysis of endogenous glycoside hydrolases and transglycosidases responsible for cell wall remodeling. To exemplify the potential of fluorogenic resorufin glycosides to address this issue, a resorufin b-glycoside of a xylogluco-oligosaccharide (XXXG-b-Res) was synthesized as a specific substrate for in planta analysis of XEH activity. The resorufin aglycone is particularly distinguished for high sensitivity in muro assays due to a low pK a (5.8) and large extinction coefficient (« 62,000 M 21 cm 21 ), long-wavelength fluorescence (excitation 571 nm/emission 585 nm), and high quantum yield (0.74) of the corresponding anion. In vitro analyses demonstrated that XXXG-b-Res is hydrolyzed by the archetypal plant XEH, nasturtium (Tropaeolum majus) NXG1, with classical Michaelis-Menten substrate saturation kinetics and a linear dependence on both enzyme concentration and incubation time. Further, XEH activity could be visualized in real time by observing the localized increase in fluorescence in germinating nasturtium seeds and Arabidopsis (Arabidopsis thaliana) inflorescent stems by confocal microscopy. Importantly, this new in situ XEH assay provides an essential complement to the in situ xyloglucan endotransglycosylase assay, thus allowing delineation of the disparate activities encoded by xyloglucan endotransglycosylase/ hydrolase genes directly in plant tissues. The observation that XXXG-b-Res is also hydrolyzed by diverse microbial XEHs indicates that this substrate, and resorufin glycosides in general, may find broad applicability for the analysis of wall restructuring by polysaccharide hydrolases during morphogenesis and plant-microbe interactions.

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“…Such interest stems not only from the role of these polysaccharides and their catalysts in plant cell wall morphogenesis (9,10,13), but also from biotechnological applications as diverse as fruit juice clarification (19,20), textile processing (21,22), cellulose surface modification (23)(24)(25)(26)(27), pharmaceutical delivery (28 -30), production of food thickening agents (30,31), as well as the production of xylogluco-oligosaccharides for cell wall analysis (4,5,32), plant growth modulation (33,34), surfactant synthesis (35), and enzyme kinetic studies (36). Furthermore, the goal of biofuel production from plant biomass, which strives to substantially reduce fossil fuel usage, has caused a great resurgence of interest in plant cell wall degrading enzymes (37).…”

mentioning

confidence: 99%

Characterization and Three-dimensional Structures of Two Distinct Bacterial Xyloglucanases from Families GH5 and GH12

Gloster

Ibatullin

Macauley

et al. 2007

Journal of Biological Chemistry

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106

114

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The plant cell wall is a complex material in which the cellulose microfibrils are embedded within a mesh of other polysaccharides, some of which are loosely termed "hemicellulose." One such hemicellulose is xyloglucan, which displays a ␤-1,4-linked D-glucose backbone substituted with xylose, galactose, and occasionally fucose moieties. Both xyloglucan and the enzymes responsible for its modification and degradation are finding increasing prominence, reflecting both the drive for enzymatic biomass conversion, their role in detergent applications, and the utility of modified xyloglucans for cellulose fiber modification. Here we present the enzymatic characterization and three-dimensional structures in ligandfree and xyloglucan-oligosaccharide complexed forms of two distinct xyloglucanases from glycoside hydrolase families GH5 and GH12. The enzymes, Paenibacillus pabuli XG5 and Bacillus licheniformis XG12, both display open active center grooves grafted upon their respective (␤/␣) 8 and ␤-jelly roll folds, in which the side chain decorations of xyloglucan may be accommodated. For the ␤-jelly roll enzyme topology of GH12, binding of xylosyl and pendant galactosyl moieties is tolerated, but the enzyme is similarly competent in the degradation of unbranched glucans. In the case of the (␤/␣) 8 GH5 enzyme, kinetically productive interactions are made with both xylose and galactose substituents, as reflected in both a high specific activity on xyloglucan and the kinetics of a series of aryl glycosides. The differential strategies for the accommodation of the side chains of xyloglucan presumably facilitate the action of these microbial hydrolases in milieus where diverse and differently substituted substrates may be encountered.

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Synthesis, preliminary characterization, and application of novel surfactants from highly branched xyloglucan oligosaccharides

Cited by 43 publications

References 64 publications

Structural Evidence for the Evolution of Xyloglucanase Activity from Xyloglucan Endo-Transglycosylases: Biological Implications for Cell Wall Metabolism

Structural Evidence for the Evolution of Xyloglucanase Activity from Xyloglucan Endo-Transglycosylases: Biological Implications for Cell Wall Metabolism

A Real-Time Fluorogenic Assay for the Visualization of Glycoside Hydrolase Activity in Planta

Characterization and Three-dimensional Structures of Two Distinct Bacterial Xyloglucanases from Families GH5 and GH12

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