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  • 301. Tan, Tien-Chye
    et al.
    Mijts, Benjamin N.
    Swaminathan, Kunchithapadam
    Patel, Bharat K. C.
    Divne, Christina
    KTH, School of Biotechnology (BIO), Glycoscience.
    Crystal structure of the polyextremophilic alpha-amylase AmyB from Halothermothrix orenii: Details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch2008In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 378, no 4, p. 852-870Article in journal (Refereed)
    Abstract [en]

    The gene for a membrane-bound, halophilic, and thermostable alpha-amylase, AmyB, from Halothermothrix orenii was cloned and sequenced. The crystal structure shows that, in addition to the typical domain organization of family 13 glycoside hydrolases, AmyB carries an additional N-terminal domain (N domain) that forms a large groove-the N-C groove some 30 angstrom away from the active site. The structure of AmyB with the inhibitor acarbose at 1.35 angstrom resolution shows that a nonasaccharide has been synthesized through successive transglycosylation reactions of acarbose. Unexpectedly, in a complex of wild-type AmyB with alpha-cyclodextrin and maltoheptaose at 2.2 angstrom resolution, a maltotetraose molecule is bound in subsites -1 to +3, spanning the cleavage point at -1 / + 1, with the -1 glucosyl residue present as a S-2(o) skew boat. This wild-type AmyB complex was obtained in the presence of a large excess of substrate, a condition under which it is possible to capture Michaelis complexes, which may explain the observed binding across -1/+ 1 and ring distortion. We observe three methionine side chains that serve as '' binding platforms '' for glucosyl rings in AmyB, a seemingly rare occurrence in carbohydrate-binding proteins. The structures and results from the biochemical characterization of AmyB and AmyB lacking the N domain show that the N domain increases binding of the enzyme to raw starch. Furthermore, theoretical modeling suggests that the N-C groove can accommodate, spatially and chemically, large substrates such as A-starch.

  • 302.
    Tang, Hu
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Butchosa, Nuria
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology, Biocomposites.
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Zhou, Qi
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Transparent, hazy and strong macroscopic ribbon of oriented cellulose nanofibrils bearing poly(ethylene glycol)Manuscript (preprint) (Other academic)
  • 303.
    Tang, Hu
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Butchosa, Nuria
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology, Biocomposites.
    Zhou, Qi
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    A Transparent, Hazy, and Strong Macroscopic Ribbon of Oriented Cellulose Nanofibrils Bearing Poly(ethylene glycol)2015In: Advanced Materials, ISSN 0935-9648, E-ISSN 1521-4095, Vol. 27, no 12, p. 2070-2076Article in journal (Refereed)
    Abstract [en]

    A macroscopic ribbon of oriented cellulose nanofibrils bearing polyethylene glycol is fabricated by stretching the cellulose nanofibrils network structure in the hydrogel state. The covalently grafted polyethylene glycol on the nanofibril surface facilitates the alignment and compartmentalization of individual nanofibrils in the ribbon. The ribbon has ultrahigh tensile strength (576 +/- 54 MPa), modulus (32.3 +/- 5.7 GPa), high transparency, and haze.

  • 304.
    Teeri, Tuula T.
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Daniel, Geoff
    Gatenholm, Paul
    Biomimetic engineering of cellulose-based materials2007In: Trends in Biotechnology, ISSN 0167-7799, E-ISSN 1879-3096, Vol. 25, no 7, p. 299-306Article, review/survey (Refereed)
    Abstract [en]

    Biomimetics is a field of science that investigates biological structures and processes for their use as models for the development of artificial systems. Biomimetic approaches have considerable potential in the development of new high-performance materials with low environmental impact. The cell walls of different plant species represent complex and highly sophisticated composite materials that can provide inspiration on how to design and fabricate lightweight materials with unique properties. Such materials can provide environmentally compatible solutions in advanced packaging, electronic devices, vehicles and sports equipment. This review gives an overview of the structures and interactions in natural plant cell walls and describes the first attempts towards mimicking them to develop novel biomaterials.

  • 305.
    Teeri, Tuula T
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Henriksson, Gunnar
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology.
    Enzymes degrading wood components2009In: Pulp and Paper Chemistry and Technology: Volume 1: Wood Chemistry and Wood Biotechnology / [ed] M Ek, G Gellerstedt and G Henriksson, Berlin: Walter de Gruyter, 2009, p. 245-271Chapter in book (Other academic)
  • 306. Testoni, Giorgia
    et al.
    Duran, Jordi
    Garcia-Rocha, Mar
    Vilaplana, Francisco
    KTH, School of Biotechnology (BIO), Glycoscience.
    Serrano, Antonio L.
    Sebastian, David
    Lopez-Soldado, Iliana
    Sullivan, Mitchell A.
    Slebe, Felipe
    Vilaseca, Marta
    Munoz-Canoves, Pura
    Guinovart, Joan J.
    Lack of Glycogenin Causes Glycogen Accumulation and Muscle Function Impairment2017In: Cell Metabolism, ISSN 1550-4131, E-ISSN 1932-7420, Vol. 26, no 1, p. 256-266Article in journal (Refereed)
    Abstract [en]

    Glycogenin is considered essential for glycogen synthesis, as it acts as a primer for the initiation of the polysaccharide chain. Against expectations, glycogenin-deficient mice (Gyg KO) accumulate high amounts of glycogen in striated muscle. Furthermore, this glycogen contains no covalently bound protein, thereby demonstrating that a protein primer is not strictly necessary for the synthesis of the polysaccharide in vivo. Strikingly, in spite of the higher glycogen content, Gyg KO mice showed lower resting energy expenditure and less resistance than control animals when subjected to endurance exercise. These observations can be attributed to a switch of oxidative myofibers toward glycolytic metabolism. Mice overexpressing glycogen synthase in the muscle showed similar alterations, thus indicating that this switch is caused by the excess of glycogen. These results may explain the muscular defects of GSD XV patients, who lack glycogenin-1 and show high glycogen accumulation in muscle.

  • 307.
    Thongpoo, Preeyanuch
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    McKee, Lauren S.
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Araújo, Ana Catarina
    KTH, School of Biotechnology (BIO), Glycoscience.
    Kongsaeree, Prachumporn T.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Identification of the acid/base catalyst of a glycoside hydrolase family 3 (GH3) beta-glucosidase from Aspergillus niger ASKU282013In: Biochimica et Biophysica Acta - General Subjects, ISSN 0304-4165, E-ISSN 1872-8006, Vol. 1830, no 3, p. 2739-2749Article in journal (Refereed)
    Abstract [en]

    Background: The commercially important glycoside hydrolase family 3 (GH3) beta-glucosidases from Aspergillus niger are anomeric-configuration-retaining enzymes that operate through the canonical double-displacement glycosidase mechanism. Whereas the catalytic nucleophile is readily identified across all GH3 members by sequence alignments, the acid/base catalyst in this family is phylogenetically variable and less readily divined. Methods: In this report, we employed three-dimensional structure homology modeling and detailed kinetic analysis of site-directed mutants to identify the catalytic acid/base of a GH3 beta-glucosidase from A. niger ASKU28. Results: In comparison to the wild-type enzyme and other mutants, the E490A variant exhibited greatly reduced k(cat) and k(cat)/K-m values toward the natural substrate cellobiose (67,000- and 61,000-fold, respectively). Correspondingly smaller kinetic effects were observed for artificial chromogenic substrates p-nitrophenyl beta-D-glucoside and 2,4-dinitrophenyl beta-D-glucoside, the aglycone leaving groups of which are less dependent on add catalysis, although changes in the rate-determining catalytic step were revealed for both, pH-rate profile analyses also implicated E490 as the general acid/base catalyst. Addition of azide as an exogenous nucleophile partially rescued the activity of the E490A variant with the aryl beta-glucosides and yielded beta-glucosyl azide as a product. Conclusions and general significance: These results strongly support the assignment of E490 as the acid/base catalyst in a beta-glucosidase from A. niger ASKU28, and provide crucial experimental support for the bioinformatic identification of the homologous residue in a range of related GH3 subfamily members.

  • 308. Trovatti, E.
    et al.
    Tang, Hu
    KTH, School of Biotechnology (BIO).
    Hajian, Alireza
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Meng, Qijun
    KTH, School of Biotechnology (BIO).
    Gandini, A.
    Berglund, Lars A.
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Zhou, Qi
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Enhancing strength and toughness of cellulose nanofibril network structures with an adhesive peptide2018In: Carbohydrate Polymers, ISSN 0144-8617, E-ISSN 1879-1344, Vol. 181, p. 256-263Article in journal (Refereed)
    Abstract [en]

    The mechanical properties of cellulose nanofibrils network structure are essential for their applications in functional materials. In this work, an adhesive peptide consisting of just 11 amino acid residues with a hydrophobic core sequence of FLIVI (F – phenylalanine, L – leucine, I – isoleucine, V – valine) flanked by three lysine (K) residues was adsorbed to 2,2,6,6-Tetramethyl-1-piperidinyloxy radical (TEMPO) oxidized cellulose nanofibrils (TO-CNF). Composite films were prepared by solution casting from water suspensions of TO-CNF adsorbed with the adhesive peptide. The nanofibrils network structure of the composite was characterized by atomic force microscopy (AFM). The structure of the peptide in the composites and the interactions between TO-CNF and the peptide were studied by Fourier transform infrared spectroscopy (FTIR) and X-ray diffraction (XRD). The mechanical properties of the composites were characterized by tensile tests and dynamic mechanical analysis (DMA). With 6.3 wt.% adhesive peptide adsorbed onto TO-CNF, the composite showed a modulus of 12.5 ± 1.4 GPa, a tensile strength of 344.5 ± (15.3) MPa, and a strain to failure of 7.8 ± 0.4%, which are 34.4%, 48.8%, and 23.8% higher than those for neat TO-CNF, respectively. This resulted in significantly improved toughness (work to fracture) for the composite, 77% higher than that for the neat TO-CNF.

  • 309. Ubeda-Tomas, Susana
    et al.
    Edvardsson, Ellinor
    Eland, Cathlene
    Singh, Sunil Kumar
    Zadik, Daniel
    Aspeborg, Henrik
    Gorzsas, Andras
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Sundberg, Bjorn
    Persson, Per
    Bennett, Malcolm
    Marchant, Alan
    Genomic-assisted identification of genes involved in secondary growth in Arabidopsis utilising transcript profiling of poplar wood-forming tissues2007In: Physiologia Plantarum: An International Journal for Plant Biology, ISSN 0031-9317, E-ISSN 1399-3054, Vol. 129, no 2, p. 415-428Article in journal (Refereed)
    Abstract [en]

    Despite the importance of secondary growth in plants, relatively few genes regulating this process have been identified to date. By using data from detailed transcript profiling of the poplar wood-forming tissues, 150 genes that are differentially expressed within the zone of secondary growth were identified. In order to determine the possible function of these poplar genes, potential Arabidopsis thaliana orthologs were identified and gene knockout lines analysed. Three selection filters were used to identify the most likely orthologous genes using poplar and Arabidopsis sequence comparisons, expression profiling in secondary thickened Arabidopsis hypocotyls and global expression analysis of Arabidopsis tissues. Three genes encoding AtCSLA2 (At5g22740), the AtGUT1 GT47 glycosyltransferase (At1g27440) and a protein with no proposed function AtUNKA (At4g27435) were selected for further detailed analysis of their role in secondary growth in Arabidopsis. The presented genome-based approach using both poplar and Arabidopsis systems provides powerful means towards assigning biological functions to enzymes with poorly understood biochemical activity, such as AtCSLA2 and AtGUT1, as well as for proteins with no known function.

  • 310. Urbanowicz, B. R.
    et al.
    Bennett, A. B.
    Del Campillo, E.
    Catalá, C.
    Hayashi, T.
    Henrissat, B.
    Höfte, H.
    McQueen-Mason, S. J.
    Patterson, S. E.
    Shoseyov, O.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Rose, J. K. C.
    Structural organization and a standardized nomenclature for plant endo-1,4-β-glucanases (cellulases) of glycosyl hydrolase family 92007In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 144, no 4, p. 1693-1696Article in journal (Refereed)
  • 311. Vanholme, Bartel
    et al.
    Vanholme, Ruben
    Turumtay, Halbay
    Goeminne, Geert
    Cesarino, Igor
    Goubet, Florence
    Morreel, Kris
    Rencoret, Jorge
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Hooijmaijers, Cortwa
    KTH, School of Biotechnology (BIO), Glycoscience.
    De Rycke, Riet
    Gheysen, Godelieve
    Ralph, John
    De Block, Marc
    Meulewaeter, Frank
    Boerjan, Wout
    Accumulation of N-Acetylglucosamine Oligomers in the Plant Cell Wall Affects Plant Architecture in a Dose-Dependent and Conditional Manner2014In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 165, no 1, p. 290-308Article in journal (Refereed)
    Abstract [en]

    To study the effect of short N-acetylglucosamine (GlcNAc) oligosaccharides on the physiology of plants, N-ACETYLGLUCOSAMINYLTRANSFERASE (NodC) of Azorhizobium caulinodans was expressed in Arabidopsis (Arabidopsis thaliana). The corresponding enzyme catalyzes the polymerization of GlcNAc and, accordingly, beta-1,4-GlcNAc oligomers accumulated in the plant. A phenotype characterized by difficulties in developing an inflorescence stem was visible when plants were grown for several weeks under short-day conditions before transfer to long-day conditions. In addition, a positive correlation between the oligomer concentration and the penetrance of the phenotype was demonstrated. Although NodC overexpression lines produced less cell wall compared with wildtype plants under nonpermissive conditions, no indications were found for changes in the amount of the major cell wall polymers. The effect on the cell wall was reflected at the transcriptome level. In addition to genes encoding cell wall-modifying enzymes, a whole set of genes encoding membrane- coupled receptor-like kinases were differentially expressed upon GlcNAc accumulation, many of which encoded proteins with an extracellular Domain of Unknown Function26. Although stress-related genes were also differentially expressed, the observed response differed from that of a classical chitin response. This is in line with the fact that the produced chitin oligomers were too small to activate the chitin receptor-mediated signal cascade. Based on our observations, we propose a model in which the oligosaccharides modify the architecture of the cell wall by acting as competitors in carbohydrate-carbohydrate or carbohydrate-protein interactions, thereby affecting noncovalent interactions in the cell wall or at the interface between the cell wall and the plasma membrane.

  • 312. Vaten, Anne
    et al.
    Dettmer, Jan
    Wu, Shuang
    Stierhof, York-Dieter
    Miyashima, Shunsuke
    Yadav, Shri Ram
    Roberts, Christina J.
    Campilho, Ana
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Lichtenberger, Raffael
    Lehesranta, Satu
    Mahonen, Ari Pekka
    Kim, Jae-Yean
    Jokitalo, Eija
    Sauer, Norbert
    Scheres, Ben
    Nakajima, Keiji
    Carlsbecker, Annelie
    Gallagher, Kimberly L.
    Helariutta, Yka
    Callose Biosynthesis Regulates Symplastic Trafficking during Root Development2011In: Developmental Cell, ISSN 1534-5807, E-ISSN 1878-1551, Vol. 21, no 6, p. 1144-1155Article in journal (Refereed)
    Abstract [en]

    Plant cells are connected through plasmodesmata (PD), membrane-lined channels that allow symplastic movement of molecules between cells. However, little is known about the role of PD-mediated signaling during plant morphogenesis. Here, we describe an Arabidopsis gene, CALS3/GSL12. Gain-of-function mutations in CALS3 result in increased accumulation of callose (beta-1,3-glucan) at the PD, a decrease in PD aperture, defects in root development, and reduced intercellular trafficking. Enhancement of CALS3 expression during phloem development suppressed loss-of-function mutations in the phloem abundant callose synthase, CALS7 indicating that CALS3 is a bona fide callose synthase. CALS3 alleles allowed us to spatially and temporally control the PD aperture between plant tissues. Using this tool, we are able to show that movement of the transcription factor SHORT-ROOT and microRNA1 65 between the stele and the endodermis is PD dependent. Taken together, we conclude that regulated callose biosynthesis at PD is essential for cell signaling.

  • 313.
    Vilaplana, Francisco
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Martinez-Abad, Antonio
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ruthes, Andrea Caroline
    KTH, School of Biotechnology (BIO), Glycoscience.
    MS techniques in structure analysis of complex glycans2017In: Abstract of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 253Article in journal (Other academic)
  • 314.
    Vilaplana, Francisco
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience. Huazhong University of Science and Technology, China.
    Meng, Di
    Hasjim, Jovin
    Gilbert, Robert G.
    Two-dimensional macromolecular distributions reveal detailed architectural features in high-amylose starches2014In: Carbohydrate Polymers, ISSN 0144-8617, E-ISSN 1879-1344, Vol. 113, p. 539-551Article in journal (Refereed)
    Abstract [en]

    Two-dimensional (2D) structural distributions based on macromolecular size and branch chain-length are obtained for three maize starches with different amylose contents (one normal and two high-amylose varieties). Data were obtained using an analytical methodology combining chemical fractionation, enzymatic debranching, and offline 2D size-exclusion chromatography with multiple detection. The 2D distributions reveal novel features in the branching structure of high-amylose maize starches. Normal maize starch shows well-resolved structural topologies, corresponding to the amylopectin and amylose macromolecular populations. However, high-amylose maize starches exhibit very complex topologies with significant features between those of amylose and amylopectin, showing the presence of distinct intermediate components. These have the macromolecular size of amylose but similar branching structure to amylopectin, except for a higher proportion of longer branches. These structural features of the intermediate components can be related to a less tightly controlled biosynthesis of the branching structures in high-amylose maize starch mutants, which may prevent these molecules from maturing into full-size amylopectin. This altered macromolecular branched architecture of high-amylose starches probably contribute to their better nutritional properties.

  • 315.
    Vilaplana, Francisco
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology.
    Nilsson, Johanna
    Sommer, Dorte V. P.
    Karlsson, Sigbritt
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology. University of Skövde, Sweden .
    Analytical markers for silk degradation: comparing historic silk and silk artificially aged in different environments2015In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 407, no 5, p. 1433-1449Article in journal (Refereed)
    Abstract [en]

    Suitable analytical markers to assess the degree of degradation of historic silk textiles at molecular and macroscopic levels have been identified and compared with silk textiles aged artificially in different environments, namely (i) ultraviolet (UV) exposure, (ii) thermo-oxidation, (iii) controlled humidity and (iv) pH. The changes at the molecular level in the amino acid composition, the formation of oxidative moieties, crystallinity and molecular weight correlate well with the changes in the macroscopic properties such as brightness, pH and mechanical properties. These analytical markers are useful to understand the degradation mechanisms that silk textiles undergo under different degradation environments, involving oxidation processes, hydrolysis, chain scission and physical arrangements. Thermo-oxidation at high temperatures proves to be the accelerated ageing procedure producing silk samples that most resembled the degree of degradation of early seventeenth-century silk. These analytical markers will be valuable to support the textile conservation tasks currently being performed in museums to preserve our heritage.

  • 316.
    Vilaplana, Francisko
    KTH, School of Biotechnology (BIO), Glycoscience.
    Editorial2014In: Journal of Renewable Materials, ISSN 2164-6325, Vol. 2, no 2, p. 93-94Article in journal (Refereed)
  • 317. Villalobos, David P.
    et al.
    Díaz-Moreno, Sara M.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Said, El-Sayed S.
    Canas, Rafael A.
    Osuna, Daniel
    Van Kerckhoven, Sonia H. E.
    Bautista, Rocio
    Gonzalo Claros, Manuel
    Canovas, Francisco M.
    Canton, Francisco R.
    Reprogramming of gene expression during compression wood formation in pine: Coordinated modulation of S-adenosylmethionine, lignin and lignan related genes2012In: BMC Plant Biology, ISSN 1471-2229, E-ISSN 1471-2229, Vol. 12, p. 100-Article in journal (Refereed)
    Abstract [en]

    Background: Transcript profiling of differentiating secondary xylem has allowed us to draw a general picture of the genes involved in wood formation. However, our knowledge is still limited about the regulatory mechanisms that coordinate and modulate the different pathways providing substrates during xylogenesis. The development of compression wood in conifers constitutes an exceptional model for these studies. Although differential expression of a few genes in differentiating compression wood compared to normal or opposite wood has been reported, the broad range of features that distinguish this reaction wood suggest that the expression of a larger set of genes would be modified. Results: By combining the construction of different cDNA libraries with microarray analyses we have identified a total of 496 genes in maritime pine (Pinus pinaster, Ait.) that change in expression during differentiation of compression wood (331 up-regulated and 165 down-regulated compared to opposite wood). Samples from different provenances collected in different years and geographic locations were integrated into the analyses to mitigate the effects of multiple sources of variability. This strategy allowed us to define a group of genes that are consistently associated with compression wood formation. Correlating with the deposition of a thicker secondary cell wall that characterizes compression wood development, the expression of a number of genes involved in synthesis of cellulose, hemicellulose, lignin and lignans was up-regulated. Further analysis of a set of these genes involved in S-adenosylmethionine metabolism, ammonium recycling, and lignin and lignans biosynthesis showed changes in expression levels in parallel to the levels of lignin accumulation in cells undergoing xylogenesis in vivo and in vitro. Conclusions: The comparative transcriptomic analysis reported here have revealed a broad spectrum of coordinated transcriptional modulation of genes involved in biosynthesis of different cell wall polymers associated with within-tree variations in pine wood structure and composition. In particular, we demonstrate the coordinated modulation at transcriptional level of a gene set involved in S-adenosylmethionine synthesis and ammonium assimilation with increased demand for coniferyl alcohol for lignin and lignan synthesis, enabling a better understanding of the metabolic requirements in cells undergoing lignification.

  • 318. von Schantz, Laura
    et al.
    Gullfot, Fredrika
    KTH, School of Biotechnology (BIO), Glycoscience.
    Scheer, Sebastian
    Filonova, Lada
    Gunnarsson, Lavinia Cicortas
    Flint, James E.
    Daniel, Geoffrey
    Nordberg-Karlsson, Eva
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ohlin, Mats
    Affinity maturation generates greatly improved xyloglucan-specific carbohydrate binding modules2009In: BMC Biotechnology, ISSN 1472-6750, E-ISSN 1472-6750, Vol. 9Article in journal (Refereed)
    Abstract [en]

    Background: Molecular evolution of carbohydrate binding modules (CBM) is a new approach for the generation of glycan-specific molecular probes. To date, the possibility of performing affinity maturation on CBM has not been investigated. In this study we show that binding characteristics such as affinity can be improved for CBM generated from the CBM4-2 scaffold by using random mutagenesis in combination with phage display technology. Results: Two modified proteins with greatly improved affinity for xyloglucan, a key polysaccharide abundant in the plant kingdom crucial for providing plant support, were generated. Both improved modules differ from other existing xyloglucan probes by binding to galactose-decorated subunits of xyloglucan. The usefulness of the evolved binders was verified by staining of plant sections, where they performed better than the xyloglucan-binding module from which they had been derived. They discriminated non-fucosylated from fucosylated xyloglucan as shown by their ability to stain only the endosperm, rich in non-fucosylated xyloglucan, but not the integument rich in fucosylated xyloglucan, on tamarind seed sections. Conclusion: We conclude that affinity maturation of CBM selected from molecular libraries based on the CBM4-2 scaffold is possible and has the potential to generate new analytical tools for detection of plant carbohydrates.

  • 319.
    Wang, Yang
    KTH, School of Biotechnology (BIO), Glycoscience.
    Exploring glycoside hydrolase family 5 (GH5) enzymes2013Licentiate thesis, comprehensive summary (Other academic)
    Abstract [en]

    In 1990, the classification of carbohydrate-active enzymes (CAZymes) was introduced by the scientist Bernard Henrissat. According to sequence similarity, these enzymes were separated into families with conserved structures and reaction mechanisms. One interesting class of CAZymes is the group of glycoside hydrolases (GHs) containing more than 138000 modules divided into 131 families as of February 2013. One of the most versatile and the largest of these GH families, containing enzymes with numerous biomass-deconstructing activities, is glycoside hydrolase family 5 (GH5). However, for large and diverse families like the GH5 family, another layer of classification is required to get a better understanding of the evolution of diverse enzyme activities. In Paper I, a new subfamily classification of GH5 is presented in order to sort the family members into distinct groups with predictive power. In total, 51 subfamilies were defined. Despite the fact that several hundred GH5 enzymes have been characterized, 20 subfamilies lacking biochemically characterized enzymes and 38 subfamilies without structural data were identified. These highlighted subfamilies contain interesting targets for future investigation.

    The GH5 family includes endo-β-mannanases catalyzing the hydrolysis of the β-1,4-linked backbone of mannan polysaccharides, which are common hemicelluloses found as storage and structural polymers in plant cell walls. Mannans are commonly utilized as raw biomaterials in food, feed, paper, textile and cosmetic industries, and mannanases are often applied for modifying and controlling the property of mannan polysaccharides in such applications. The overwhelming majority of characterized mannanases are from microbial origin. The situation for plant mannanases is quite different, as the catalytic properties for only a handful have been determined. Paper II describes the first characterization of a heterologously expressed Arabidopsis β-mannanase.

  • 320.
    Wang, Yang
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Vilaplana, Francisco
    KTH, School of Biotechnology (BIO), Glycoscience.
    Brumer, Harry
    Aspeborg, Henrik
    KTH, School of Biotechnology (BIO), Glycoscience.
    Enzymatic characterization of a GH5_7 mannanase from Arabidopsis thalianaManuscript (preprint) (Other academic)
  • 321.
    Wang, Yang
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Biotechnology (BIO), Industrial Biotechnology.
    Vilaplana, Francisco
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Aspeborg, Henrik
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Biotechnology (BIO), Industrial Biotechnology.
    Enzymatic characterization of a glycoside hydrolase family 5 subfamily 7 (GH5_7) mannanase from Arabidopsis thaliana2014In: Planta, ISSN 0032-0935, E-ISSN 1432-2048, Vol. 239, no 3, p. 653-665Article in journal (Refereed)
    Abstract [en]

    Each plant genome contains a repertoire of beta-mannanase genes belonging to glycoside hydrolase family 5 subfamily 7 (GH5_7), putatively involved in the degradation and modification of various plant mannan polysaccharides, but very few have been characterized at the gene product level. The current study presents recombinant production and in vitro characterization of AtMan5-1 as a first step towards the exploration of the catalytic capacity of Arabidopsis thaliana beta-mannanase. The target enzyme was expressed in both E. coli (AtMan5-1e) and P. pastoris (AtMan5-1p). The main difference between the two forms was a higher observed thermal stability for AtMan5-1p, presumably due to glycosylation of that particular variant. AtMan5-1 displayed optimal activity at pH 5 and 35 A degrees C and hydrolyzed polymeric carob galactomannan, konjac glucomannan, and spruce galactoglucomannan as well as oligomeric mannopentaose and mannohexaose. However, the galactose-rich and highly branched guar gum was not as efficiently degraded. AtMan5-1 activity was enhanced by Co2+ and inhibited by Mn2+. The catalytic efficiency values for carob galactomannan were 426.8 and 368.1 min(-1) mg(-1) mL for AtMan5-1e and AtMan5-1p, respectively. Product analysis of AtMan5-1p suggested that at least five substrate-binding sites were required for manno-oligosaccharide hydrolysis, and that the enzyme also can act as a transglycosylase.

  • 322.
    Winzell, Anders
    KTH, School of Biotechnology (BIO), Glycoscience.
    Investigation of genes and proteins involved in xylan biosynthesis2010Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Wood formation or xylogenesis is a fundamental process for so diverse issues as industry, shelter and a sustainable environment. Wood is comprised of secondary xylem, rigid large cells with thick cell walls that are lignified. The basis for the sturdy cells is an advanced composite made up of cellulose fibers cross-linked by hemicelluloses and finally embedded in lignin. This fiber-composite is the secondary cell walls of woody plants. Cell division and differentiation is regulated by switching on and off genes. Proteins encoded by these genes execute the major functions in the cells. They steer the entire machinery operating the structure and function of the cells, maintaining growth and synthesising essential products such as the cell wall carbohydrates.

     

    Here we describe the investigation of genes and proteins involved in xylan formation as well as the development of a model system that will aid the functional analysis of wood formation. Xylan is the main hemicellulose or cross linking glycan in dicot wood and thereby one of the most abundant carbohydrates on earth. We demonstrate that hybrid aspen cell suspension cultures can be used as a model system for secondary cell wall formation. We have also examined glycosyltransferases from CAZy family 43 that play a part in secondary cell wall formation. We have focused on one of these, Pt×tGT43A, a likely ortholog of Arabidopsis IRX9, which plays a crucial role in xylan formation. The protein was transiently expressed in Nicotiana benthamiana and its function and localization is described. Also, we investigate a glycoside hydrolase, Pt×tXyn10A, involved in wood formation. Its role is not clear but it most likely modifies xylan as it gets incorporated into the secondary cell wall after secretion from the Golgi. This influences the interaction between cellulose, xylan and lignin in the finished wood cell. We have also cloned a transcription factor, Pt×tMYB021, a likely ortholog of Arabidopsis MYB46 and we show that it activates GT43A, GT43B and Xyn10A. By analysis of the promoter sequences we identify a CA-rich motif putatively important for xylem-specific genes.

     

    By mastering proteins involved in xylogenesis we will acquire the tools to improve and develop the wood product market. Xylan is an immense unexploited source of renewable carbohydrate. New products envisioned include e.g. faster growing trees, changed fiber characteristics, optimised utilization of wood carbohydrates for biofuels and biomaterials as well as invention of intelligent materials by biomimetic engineering.

  • 323.
    Winzell, Anders
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Aspeborg, Henrik
    KTH, School of Biotechnology (BIO), Glycoscience.
    Wang, Yucheng
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ezcurra, Ines
    KTH, School of Biotechnology (BIO), Glycoscience.
    Conserved CA-rich motifs in gene promoters of Pt x tMYB021-responsive secondary cell wall carbohydrate-active enzymes in Populus2010In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 394, no 3, p. 848-853Article in journal (Refereed)
    Abstract [en]

    In order to understand gene regulation during wood formation, we cloned a MYB46-like gene in hybrid aspen. Populus tremula x tremuloides, called PtxtMYB021 Phylogenetic and paired identity analysis of MYB46-like genes in Populus and Arabidopsis reveals relationships between paralogous pairs of Populus MYB46-like proteins and their Arabidopsis counterparts MYB46 and MYB83, and suggest that PtxtMYB021 is the ortholog of MYB46 Ptxt-MYB021 is expressed mainly in xylem tissues, and transiently expressed PtxtMYB46 transactivates gene promoters of xylan-active CAZymes GT43A, GT43B and Xyn10A Analysis of conserved motifs within these promoters identify the sequence CCACCAAC, called ACTYP, which is similar to the AC elements mediating transactivation by MYB transcription factors during lignin biosynthesis Further analysis by Motif Finder identifies four 6 bp CA-rich motifs overlapping ACTYP, and we show that these motifs are enriched in xylem-specific promoters We propose that AC-type regulatory elements mediate xylem-specific MYB46-dependent expression of secondary cell wall carbohydrate-active enzymes (CAZymes), besides activating gene expression of lignin biosynthesis enzymes.

  • 324.
    Winzell, Anders
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Aspeborg, Henrik
    KTH, School of Biotechnology (BIO), Glycoscience.
    Wang, Yucheng
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ezcurra, Ines
    KTH, School of Biotechnology (BIO), Glycoscience.
    Molecular cloning and functional characterization of Pt×tMYB021, a MYB46-like transcription factor in PopulusManuscript (preprint) (Other academic)
  • 325.
    Winzell, Anders
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Guerriero, Gea
    KTH, School of Biotechnology (BIO), Glycoscience.
    Aspeborg, Henrik
    KTH, School of Biotechnology (BIO), Glycoscience.
    Wang, Yiqiang
    KTH, School of Biotechnology (BIO), Glycoscience.
    Rajangam, Alex S.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ezcurra, Inés
    KTH, School of Biotechnology (BIO), Glycoscience.
    Biochemical characterization of family 43 glycosyltransferases in the Populus xylem: challenges and prospects2010In: Plant Biotechnology, ISSN 1342-4580, Vol. 27, no 3, p. 283-288Article in journal (Refereed)
    Abstract [en]

    Wood formation is a biological process of great economical importance. Genes active during the secondary cellwall formation of wood fibers from Populus tremulatremuloides were previously identified by expression profilingthrough microarray analyses. A number of these genes encode glycosyltransferases (GTs) with unknown substratespecificities. Here we report heterologous expression of one of these enzymes, PttGT43A, a putative IRREGULARXYLEM9 (IRX9) homologue. Expression trials in Pichia pastoris and insect cells revealed very low levels of accumulationof immunoreactive PttGT43A, whereas transient expression in Nicotiana benthamiana leaves by Agrobacterium infiltration(agroinfiltration) using a viral vector produced substantial amounts of protein that mostly precipitated in the crude pellet.Agroinfiltration induced weak endogenous xylosyltransferase activity in microsomal extracts, and transient PttGT43Aexpression further increased this activity, albeit only to low levels. PttGT43A may be inactive as an individual subunit,requiring complex formation with unknown partners to display enzymatic activity. Our results suggest that transient coexpressionin leaves of candidate subunit GTs may provide a viable approach for formation of an active xylanxylosyltransferase enzymatic complex.

  • 326.
    Winzell, Anders
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ratke, Christine
    Naumann, Marcel
    Wang, Yucheng
    KTH, School of Biotechnology (BIO), Glycoscience.
    Aspeborg, Henrik
    KTH, School of Biotechnology (BIO), Glycoscience.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Mellerowicz, Ewa
    Ezcurra, Ines
    KTH, School of Biotechnology (BIO), Glycoscience.
    Family 43 glycosyltransferases in Populus and Arabidopsis: phylogeny and expression analysisManuscript (preprint) (Other academic)
  • 327. Wycliffe, P.
    et al.
    Sitbon, F.
    Wernersson, J.
    Ezcurra, Inés
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ellerstrom, M.
    Rask, L.
    Continuous expression in tobacco leaves of a Brassica napus PEND homologue blocks differentiation of plastids and development of palisade cells2005In: The Plant Journal, ISSN 0960-7412, E-ISSN 1365-313X, Vol. 44, no 1, p. 1-15Article in journal (Refereed)
    Abstract [en]

    Brassica napus complementary deoxyribonucleic acid (cDNA) clones encoding a DNA-binding protein, BnPEND, were isolated by Southwestern screening. A distinctive feature of the protein was a bZIP-like sequence in the amino-terminal portion, which, after expression in Escherichia coli, bound DNA. BnPEND transcripts were present in B. napus roots and flower buds, and to a lesser extent in stems, flowers and young leaves. Treatment in the dark for 72 h markedly increased the amount of BnPEND transcript in leaves of all ages. Sequence comparison showed that BnPEND was similar to a presumed transcription factor from B. napus, GSBF1, a protein deduced from an Arabidopsis thaliana cDNA (BX825084) and the PEND protein from Pisum sativum, believed to anchor the plastid DNA to the envelope early during plastid development. Homology to expressed sequence tag (EST) sequences from additional species suggested that BnPEND homologues are widespread among the angiosperms. Transient expression of BnPEND fused with green fluorescent protein (GFP) in Nicotiana benthamiana epidermal cells showed that BnPEND is a plastid protein, and that the 15 amino acids at the amino-terminal contain information about plastid targeting. Expression of BnPEND in Nicotiana tabacum from the Cauliflower Mosaic Virus 35S promoter gave stable transformants with different extents of white to light-green areas in the leaves, and even albino plants. In the white areas, but not in adjacent green tissue, the development of palisade cells and chloroplasts was disrupted. Our data demonstrate that the BnPEND protein, when over-expressed at an inappropriate stage, functionally blocks the development of plastids and leads to altered leaf anatomy, possibly by preventing the release of plastid DNA from the envelope.

  • 328.
    Xing, Xiaohui
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience. University of Adelaide, Australia.
    Hsieh, Yves S.Y.
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Yap, Kuok
    Ang, Main E.
    Lahnstein, Jelle
    Tucker, Matthew R.
    Burton, Rachel A.
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center. University of Adelaide, Australia.
    Isolation and structural elucidation by 2D NMR of planteose, a major oligosaccharide in the mucilage of chia (Salvia hispanica L.) seeds2017In: Carbohydrate Polymers, ISSN 0144-8617, E-ISSN 1879-1344, Vol. 175, p. 231-240Article in journal (Refereed)
    Abstract [en]

    An oligosaccharide was isolated in high purity and excellent yield from the water-extractable mucilage of chia (Salvia hispanica L.) seeds using an optimized solid-phase extraction method. LC–MS analysis showed that the compound presents a molecular mass of 504 Da and trifluoroacetic acid hydrolysis revealed that it consists of galactose, glucose and fructose. Glycosidic linkage analysis showed that the oligosaccharide contains two non-reducing ends corresponding to terminal glucopyranose and terminal galactopyranose, respectively. The oligosaccharide was identified as planteose by the complete assignment of a series of 2D NMR spectra (COSY, TOCSY, ROESY, HSQC, and HMBC). The significance of the presence of planteose in chia seeds is discussed in the context of nutrition and food applications.

  • 329.
    Xu, Chunlin
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Spadiut, Oliver
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Araujo, Ana Catarina
    KTH, School of Biotechnology (BIO), Glycoscience.
    Nakhai, Azadeh
    KTH, School of Biotechnology (BIO), Glycoscience.
    Willfor, Stefan
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Chemo-enzymatic assembly of clickable cellulose surfaces via multivalent polysaccharides2012In: Abstract of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 243Article in journal (Other academic)
  • 330.
    Xu, Chunlin
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Spadiut, Oliver
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Araújo, Ana Catarina
    KTH, School of Biotechnology (BIO).
    Nakhai, Azadeh
    KTH, School of Biotechnology (BIO), Glycoscience.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Chemo-enzymatic Assembly of Clickable Cellulose Surfaces via Multivalent Polysaccharides2012In: ChemSusChem, ISSN 1864-5631, Vol. 5, no 4, p. 661-665Article in journal (Refereed)
    Abstract [en]

    The chemist′s guide to the galactosyl unit: A chemo-enzymatic process is developed for the multivalent functionalization of cellulose surfaces via regioselective oxidation of heteropolysaccharides with galactose 6-oxidase. Reductive amination, surface sorption, and click chemistry enable the assembly of (bio)chemically active cellulose surfaces for applications ranging from functional biocomposites to in vitro diagnostics.

  • 331.
    Yao, Kun
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Huang, Shu
    KTH, School of Biotechnology (BIO).
    Tang, Hu
    KTH, School of Biotechnology (BIO).
    Xu, Y.
    Buntkowsky, G.
    Berglund, Lars A.
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Zhou, Qi
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Bioinspired Interface Engineering for Moisture Resistance in Nacre-Mimetic Cellulose Nanofibrils/Clay Nanocomposites2017In: ACS Applied Materials and Interfaces, ISSN 1944-8244, E-ISSN 1944-8252, Vol. 9, no 23, p. 20169-20178Article in journal (Refereed)
    Abstract [en]

    The interfacial adhesion design between "mortar" and "bricks" is essential for mechanical and barrier performance of nanocellulose-based nacre-mimetic nanocomposites, especially at high moisture conditions. To address this fundamental challenge, dopamine (DA) has been conjugated to cellulose nanofibrils (CNFs) and subsequently assembled with montmorillonite (MTM) to generate layered nanocomposite films inspired by the strong adhesion of mussel adhesive proteins to inorganic surfaces under water. The selective formation of catechol/metal ion chelation and hydrogen bonding at the interface between MTM platelets and CNFs bearing DA renders transparent films with strong mechanical properties, particularly at high humidity and in wet state. Increasing the amount of conjugated DA on CNFs results in nanocomposites with increased tensile strength and modulus, up to 57.4 MPa and 1.1 GPa, respectively, after the films are swollen in water. The nanocomposites also show excellent gas barrier properties at high relative humidity (95%), complementing the multifunctional property profile.

  • 332.
    Yao, Kun
    et al.
    KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center. KTH, School of Biotechnology (BIO), Glycoscience.
    Meng, Qijun
    Bulone, Vincent
    Zhou, Qi
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Flexible and Responsive Chiral Nematic Cellulose Nanocrystal/Poly(ethylene glycol) Composite Films with Uniform and Tunable Structural Color2017In: Advanced Materials, ISSN 0935-9648, E-ISSN 1521-4095, Vol. 29, no 28, article id 1701323Article in journal (Refereed)
    Abstract [en]

    The fabrication of responsive photonic structures from cellulose nanocrystals (CNCs) that can operate in the entire visible spectrum is challenging due to the requirements of precise periodic modulation of the pitch size of the self-assembled multilayer structures at the length scale within the wavelength of the visible light. The surface charge density of CNCs is an important factor in controlling the pitch size of the chiral nematic structure of the dried solid CNC films. The assembly of poly(ethylene glycol) (PEG) together with CNCs into smaller chiral nematic domains results in solid films with uniform helical structure upon slow drying. Large, flexible, and flat photonic composite films with uniform structure colors from blue to red are prepared by changing the composition of CNCs and PEG. The CNC/PEG(80/20) composite film demonstrates a reversible and smooth structural color change between green and transparent in response to an increase and decrease of relative humidity between 50% and 100% owing to the reversible swelling and dehydration of the chiral nematic structure. The composite also shows excellent mechanical and thermal properties, complementing the multifunctional property profile.

  • 333. Yu, L.
    et al.
    Yakubov, G. E.
    Zeng, W.
    Xing, Xiaohui
    KTH, School of Biotechnology (BIO), Glycoscience.
    Stenson, J.
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Stokes, J. R.
    Multi-layer mucilage of Plantago ovata seeds: Rheological differences arise from variations in arabinoxylan side chains2017In: Carbohydrate Polymers, ISSN 0144-8617, E-ISSN 1879-1344, Vol. 165, p. 132-141Article in journal (Refereed)
    Abstract [en]

    Mucilages are hydrocolloid solutions produced by plants for a variety of functions, including the creation of a water-holding barrier around seeds. Here we report our discovery of the formation of three distinct mucilage layers around Plantago ovata seeds upon their hydration. Each layer is dominated by different arabinoxylans (AXs). These AXs are unusual because they are highly branched and contain β-1,3-linked xylose in their side chains. We show that these AXs have similar monosaccharide and linkage composition, but vary in their polymer conformation. They also exhibit distinct rheological properties in aqueous solution, despite analytical techniques including NMR showing little difference between them. Using enzymatic hydrolysis and chaotropic solvents, we reveal that hydrogen bonding and side chain distribution are key factors underpinning the distinct rheological properties of these complex AXs.

  • 334. Zabotina, Olga
    et al.
    Malm, Erik
    KTH, School of Biotechnology (BIO), Glycoscience.
    Drakakaki, Georgia
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Raikhel, Natasha
    Identification and Preliminary Characterization of a New Chemical Affecting Glucosyltransferase Activities Involved in Plant Cell Wall Biosynthesis2008In: MOLECULAR PLANT, ISSN 1674-2052, Vol. 1, no 6, p. 977-989Article in journal (Refereed)
    Abstract [en]

    Chemical genetics as a part of chemical genomics is a powerful and fast developing approach to dissect biological processes that may be difficult to characterize using conventional genetics because of gene redundancy or lethality and, in the case of polysaccharide biosynthesis, plant flexibility. Polysaccharide synthetic enzymes are located in two main compartments-the Golgi apparatus and plasma membrane-and can be studied in vitro using membrane fractions. Here, we first developed a high-throughput assay that allowed the screening of a library of chemicals with a potential effect on glycosyltransferase activities. Out of the 4800 chemicals screened for their effect on Golgi glucosyltransferases, 66 compounds from the primary screen had an effect on carbohydrate biosynthesis. Ten of these compounds were confirmed to inhibit glucose incorporation after a second screen. One compound exhibiting a strong inhibition effect (ID 6240780 named chemical A) was selected and further studied. it reversibly inhibits the transfer of glucose from UDPglucose by Golgi membranes, but activates the plasma membrane-bound callose synthase. The inhibition effect is dependent on the chemical structure of the compound, which does not affect endomembrane morphology of the plant cells, but causes changes in cell wall composition. Chemical A represents a novel drug with a great potential for the study of the mechanisms of Golgi and plasma membrane-bound glucosyltransferases.

  • 335. Zamocky, M.
    et al.
    Ludwig, R.
    Peterbauer, C.
    Hallberg, B. M.
    Divne, Christina
    KTH, School of Biotechnology (BIO), Glycoscience.
    Nicholls, P.
    Haltrich, D.
    Cellobiose dehydrogenase - A flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi2006In: Current protein and peptide science, ISSN 1389-2037, E-ISSN 1875-5550, Vol. 7, no 3, p. 255-280Article, review/survey (Refereed)
    Abstract [en]

    Cellobiose dehydrogenase, the only currently known extracellular flavocytochrome. is formed not only by a number of wood-degrading but also by various phytopathogenic fungi. This inducible enzyme participates in early events of lignocellulose degradation, as investigated in several basidiomycete fungi at the transcriptional and translational level. However, its role in the ascomycete fungi is not yet obvious. Comprehensive sequence analysis of CDH-encoding genes and their translational products reveals significant sequence similarities along the entire sequences and also a common domain architecture. All known cellobiose dehydrogenases fall into two related subgroups. Class-I members are represented by sequences from basidiomycetcs whereas class-II comprises longer, more complex sequences from ascomycete fungi. Cellobiose dehydrogenase is typically a monomeric protein consisting of two domains joined by a protease-sensitive linker region. Each larger (dehydrogenase) domain is flavin-associated while the smaller (cytochrome) domains are haem-binding. The latter shorter domains are unique sequence motifs for all currently known flavocytochromes. Each cytochrome domain of CDH can bind a single haem b as prosthetic group. The larger dehydrogenase domain belongs to the glucose-methanol-choline (GMC) oxidoreductase superfamily - a widespread flavoprotein evolutionary line. The larger domains can be further divided into a flavin-binding subdomain and a substrate-binding subdomain. In addition, the class-II (but not class-I) proteins can possess a short cellulose-binding module of type I at their C-termini. All the cellobiose dehydrogenases oxidise cellobiose, cellodextrins, and lactose to the corresponding lactones using a wide spectrum of different electron acceptors. Their flexible specificity serves as a base for the development of possible biotechnological applications.

  • 336.
    Zhang, Qiong
    et al.
    KTH, School of Biotechnology (BIO), Theoretical Chemistry and Biology.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ågren, Hans
    KTH, School of Biotechnology (BIO), Theoretical Chemistry and Biology.
    Tu, Yaoquan
    KTH, School of Biotechnology (BIO), Theoretical Chemistry and Biology.
    The adsorption of xyloglucan on cellulose: effects of explicit water and side chain variation2011In: Carbohydrate Research, ISSN 0008-6215, E-ISSN 1873-426X, Vol. 346, no 16, p. 2595-2602Article in journal (Refereed)
    Abstract [en]

    The interaction between para-crystalline cellulose and the cross-linking glycan xyloglucan (XG) plays a central role for the strength and extensibility of plant cell walls. The coating of XGs on cellulose surfaces is believed to be one of the most probable interaction patterns. In this work, the effects of explicit water and side chain variation on the adsorption of XGs on cellulose are investigated by means of atomistic molecular dynamics simulations. The adsorption properties are studied in detail for three XGs on cellulose I beta 1-10 surface in aqueous environment, namely GXXXGXXXG, GXXLGXXXG, and GXXFGXXXG, which differ in the length and composition of one side chain. Our work shows that when water molecules are included in the theoretical model, the total interaction energies between the adsorbed XGs and cellulose are considerably smaller than in vacuo. Furthermore, in water environment the van der Waals interactions prevail over the electrostatic interactions in the adsorption. Variation in one side chain does not have significant influence on the interaction energy and the binding affinity, but does affect the equilibrium structural properties of the adsorbed XGs to facilitate the interaction between both the backbone and the side chain residues with the cellulose surface. Together, this analysis provides new insights into the nature of the XG-cellulose interaction, which helps to further refine current molecular models of the composite plant cell wall.

  • 337.
    Zhang, Qiong
    et al.
    KTH, School of Biotechnology (BIO), Theoretical Chemistry (closed 20110512). KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ågren, Hans
    KTH, School of Biotechnology (BIO), Theoretical Chemistry (closed 20110512). KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.
    Tu, Yaoquan
    A molecular dynamics study of the thermal response of crystalline cellulose I beta2011In: Cellulose (London), ISSN 0969-0239, E-ISSN 1572-882X, Vol. 18, no 2, p. 207-221Article in journal (Refereed)
    Abstract [en]

    Molecular dynamics simulations were performed to better understand the atomic details of thermal induced transitions in cellulose I beta. The latest version of the GLYCAM force field series (GLYCAM06) was used for the simulations. The unit cell parameters, density, torsion angles and hydrogen-bonding network of the crystalline polymer were carefully analyzed. The simulated data were validated against the experimental results obtained by X-ray diffraction for the crystal structure of cellulose I beta at room and high temperatures, as well as against the temperature-dependent IR measurements describing the variation of hydrogen bonding patterns. Distinct low and high temperature structures were identified, with a phase transition temperature of 475-500 K. In the high-temperature structure, all the origin chains rotated around the helix axis by about 30A degrees and the conformation of all hydroxymethyl groups changed from tg to either gt on origin chains or gg on center chains. The hydrogen-bonding network was reorganized along with the phase transition. Compared to the previously employed GROMOS 45a4 force field, GLYCAM06 yields data in much better agreement with experimental observations, which reflects that a cautious parameterization of the nonbonded interaction terms in a force field is critical for the correct prediction of the thermal response in cellulose crystals.

  • 338. Zhang, S. W.
    et al.
    Ren, L.
    Lv, H. X.
    Zhu, F. P.
    Zhang, M. Y.
    Yao, Kun
    KTH, School of Biotechnology (BIO), Glycoscience.
    Synthesis of narrowly distributed polystyrene-encapsulated silica nanoparticles via emulsion polymerization2017In: Journal of Dispersion Science and Technology, ISSN 0193-2691, E-ISSN 1532-2351, Vol. 38, no 3, p. 451-456Article in journal (Refereed)
    Abstract [en]

    Polystyrene (PS)-encapsulated silica nanoparticles were successfully synthesized by conventional emulsion polymerization for solving the aggregation matter of nanoscaled silica. The grafting coupling agents and PS on the silica surface were detected by Fourier Transform Infrared (FTIR) spectroscopy. The influence of silica and monomer to water ratios and initiator concentration on particle size distribution of the nanocomposite latex was investigated. The particle size distribution firstly narrowed and then broadened with the increase of silica and monomer to water ratios and initiator concentration. The narrow distribution could be controlled in an appropriate silica and monomer to water ratio and an initiator concentration of 1/15 and 2wt%, respectively. From the evaluation of transmission electron microscopy (TEM) micrographs and dynamic light scattering (DLS) measurement, it was proved that the nanocomposite latex did not have all sphere-like shape, but contained tiny amounts of irregular bodies. The formation mechanism of PS-encapsulated silica nanoparticles was also discussed.

  • 339.
    Zhou, Juan
    et al.
    KTH, School of Chemical Science and Engineering (CHE), Chemistry.
    Butchosa, Nuria
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology.
    Jayawardena, H. Surangi N.
    Zhou, Qi
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Yan, Mingdi
    KTH, School of Chemical Science and Engineering (CHE), Chemistry.
    Ramström, Olof
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Organic Chemistry.
    Glycan-Functionalized Fluorescent Chitin Nanocrystals for Biorecognition Applications2014In: Bioconjugate chemistry, ISSN 1043-1802, E-ISSN 1520-4812, Vol. 25, no 4, p. 640-643Article in journal (Refereed)
    Abstract [en]

    A new platform based on chitin nanocrystals has been developed for biorecognition applications. TEMPO-oxidized chitin nanocrystals (TCNs) were labeled with a fluorescent imidazoisoquinolinone dye, and simultaneously conjugated with carbohydrate ligands, resulting in dually functionalized TCNs. The biorecognition properties of the nanocrystals were probed with lectins and bacteria, resulting in selective interactions with their corresponding cognate carbohydrate-binding proteins, as visualized by optical, fluorescence, STEM, and TEM imaging. This represents a new approach to multifunctional nanomaterials based on naturally occurring polymers, holding high potential for biomedical applications.

  • 340.
    Zhou, Juan
    et al.
    KTH, School of Chemical Science and Engineering (CHE), Chemistry.
    Robles, Nuria
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology.
    Zhou, Qi
    KTH, School of Biotechnology (BIO), Glycoscience.
    Ramström, Olof
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Organic Chemistry.
    Yan, Mingdi
    Dually functionalized chitin nanocrystals for biorecognition applications2013In: Abstract of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 246, p. 192-POLY-Article in journal (Other academic)
  • 341.
    Zhou, Qi
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Baumann, M. J.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    The influence of surface chemical composition on the adsorption of xyloglucan to chemical and mechanical pulps2006In: Carbohydrate Polymers, ISSN 0144-8617, E-ISSN 1879-1344, Vol. 63, no 4, p. 449-458Article in journal (Refereed)
    Abstract [en]

    Adsorption kinetics of xyloglucan (XG) onto bleached chemical and mechanical wood pulps were studied to better understand the application of this plant polysaccharide to the modification of key industrial cellulosic materials. Bleached pulps prepared by the kraft process adsorbed significantly larger amounts of xyloglucan than did thermomechanical pulps (TMP) and chemi-thermomechanical pulps (CTMP). The ability of pulps to adsorb xyloglucan was intimately related to the surface amounts Of Cellulose, lignin and extractives, as determined by electron spectroscopy for chemical analysis (ESCA). The distribution of absorbed XG on bleached Pulp fibers was examined with an XG-fluorescein conjugate (XG-FITC), which was prepared by xyloglucan endotransglycosylase (XET, EC 2.4.1.207)-mediated incorporation of fluoresce-inlabeled xyloglucan oligosaccharides (XGO-FITC) into XG. Fluorescence microscopy revealed that XG-FITC preferentially adsorbed on fiber surfaces, and was adsorbed in higher amounts to chemical pulps than mechanical pulps, as observed for the unmodified parent polysaccharide. Addition of hybrid aspen XET (PttXET16A) and XGO-FITC to bleached and unbleached mechanical Pulps indicated that the amount of enzyme-accessible xyloglucan presented on TMP and CTMP surfaces is low.

  • 342.
    Zhou, Qi
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Baumann, Martin J.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Piispanen, Peter S.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Xyloglucan and xyloglucan endo-transglycosylases (XET): Tools for ex vivo cellulose surface modification2006In: Biocatalysis and Biotransformation, ISSN 1024-2422, E-ISSN 1029-2446, Vol. 24, no 1-2, p. 107-120Article in journal (Refereed)
    Abstract [en]

    Wood fibres constitute a renewable raw material for the production of novel biomaterials. The development of efficient methods for cellulose surface modification is essential for expanding the properties of wood fibres for increased reactivity and compatibility with other materials. By combining the high affinity between xyloglucan and cellulose, the unique mechanistic property of xyloglucan endo-transglycosylases (XET, EC 2.4.1.207) to catalyze polysaccharide-oligosaccharide coupling reactions, and traditional carbohydrate synthesis, a new system for the attachment of a wide variety of functional groups to wood pulps has been generated. An overview of recent developments is presented in the context of the structure, physical properties, and historical applications of xyloglucan.

  • 343.
    Zhou, Qi
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Teeri, Teeri T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Stolt, J. P.
    Oedberg, L. G.
    Copolymer, modified polymer carbohydrate material, modified buld polymer, composite material, and methods of preparation2006Patent (Other (popular science, discussion, etc.))
    Abstract [en]

    The present invention relates to a novel group of copolymers comprising a soluble carbohydrate polymer (SCP), which typically is a non-starch carbohydrate, and a macromolecule covalently attached to the SCP. The macromolecule may e.g. be a hydrophobic copolymer, a polyelectrolyte polymer or a biodegradable polymer. The present invention furthermore relates to a method of preparing the copolymer, products comprising the copolymer, and to methods of preparing the products comprising the copolymer. The products comprising a copolymer are for example a polymeric carbohydrate material (PCM) modified by attachment of a copolymer, and a composite material comprising the modified PCM.

  • 344.
    Zhou, Qi
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Self-Organization of Cellulose Nanocrystals Adsorbed with Xyloglucan Oligosaccharide-Poly(ethylene glycol)-Polystyrene Triblock Copolymer2009In: Macromolecules, ISSN 0024-9297, E-ISSN 1520-5835, Vol. 42, no 15, p. 5430-5432Article in journal (Refereed)
  • 345.
    Zhou, Qi
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Centres, Wallenberg Wood Science Center.
    Butchosa, Núria
    KTH, School of Biotechnology (BIO), Glycoscience.
    Nanocellulose-based Green Nanocomposite Materials2016In: Biodegradable Green Composites, John Wiley & Sons, 2016, p. 118-148Chapter in book (Refereed)
  • 346.
    Zhou, Qi
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Greffe, Lionel
    KTH, School of Biotechnology (BIO), Glycoscience.
    Baumann, Martin
    KTH, School of Biotechnology (BIO).
    Malmström, Eva
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Use of xyloglucan as a molecular anchor for the elaboration of polymers from cellulose surfaces: A general route for the design of biocomposites2005In: Macromolecules, ISSN 0024-9297, E-ISSN 1520-5835, Vol. 38, no 9, p. 3547-3549Article in journal (Refereed)
    Abstract [en]

    The controlled graft copolymerization of methyl methacrylate (MMA) on cellulose fibers through a combination of the XET and atom transfer radical polymerization (ATRP) was investigated. It was found that graft polymerization of MMA on the initiator-laden filter paper under appropriate ATRP conditions yielded fibers that had altered surface properties. Controlled ATRP carried out using an initiator specifically immobilized on cellulose fibers through the XG/XET system provided a new route for the generation of biocomposite materials. The method provided a novel approach for the immobilization of polymerization initiators on cellulose, which was complementary to previously established chemical routes.

  • 347.
    Zhou, Qi
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Malm, Erik
    KTH, School of Biotechnology (BIO), Glycoscience.
    Nilsson, Helena
    Larsson, Per Tomas
    Iversen, Tommy
    Berglund, Lars A.
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology, Biocomposites.
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Biomimetic design of cellulose-based nanostructured composites using bacterial cultures2009In: Polymer Preprints, ISSN 0032-3934, Vol. 50, no 2, p. 7-8Article in journal (Refereed)
  • 348.
    Zhou, Qi
    et al.
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology. KTH, School of Biotechnology (BIO), Glycoscience.
    Malm, Erik
    KTH, School of Biotechnology (BIO), Glycoscience.
    Nilsson, Helena
    Larsson, Per Tomas
    Iversen, Tommy
    Berglund, Lars A.
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology.
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Nanostructured biocomposites based on bacterial cellulosic nanofibers compartmentalized by a soft hydroxyethylcellulose matrix coating2009In: Soft Matter, ISSN 1744-683X, E-ISSN 1744-6848, Vol. 5, no 21, p. 4124-4130Article in journal (Refereed)
    Abstract [en]

    Biomimetic approaches involving environmentally-friendly synthetic pathways provide an opportunity to elaborate novel high-performance biocomposites. Here we have developed a low-energy biosynthetic system for the production of a high-strength composite material consisting of self-assembled and nanostructured cellulosic nanofibers. This biocomposite is analogous to natural composite materials with high strength and hierarchical organization such as wood or tendon. It was generated by growing the bacterium Acetobacter, which naturally produces cellulosic nanofibers, in the presence of hydroxyethylcellulose (HEC). Individual cellulose fibrils were coated by HEC and exhibited a smaller lateral dimension than pure bacterial cellulose (BC) fibrils. They self-assembled to form compartmentalized nanofibers and larger cellulose fibril aggregates compared to pure BC. The tensile strength of nanocomposite films prepared from the compartmentalized cellulosic nanofibers was 20% higher than that of pure BC sheets and wood cellulose nanopapers, and 60% higher than that of conventional BC/HEC blends, while no strain-to-failure decrease was observed. The thin nanoscale coating consisting of hydrated HEC significantly increased the mechanical performance of the nanocomposite films by provoking compartmentalization of individual fibrils.

  • 349.
    Zhou, Qi
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Rutland, Mark W
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Surface Chemistry.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Xyloglucan in cellulose modification2007In: Cellulose (London), ISSN 0969-0239, E-ISSN 1572-882X, Vol. 14, no 6, p. 625-641Article, review/survey (Refereed)
    Abstract [en]

    Xyloglucans are the principal polysaccharides coating and crosslinking cellulose microfibrills in the majority of land plants. This review summarizes current knowledge of xyloglucan structures, solution properties, and the mechanism of interaction of xyloglucans with cellulose. This knowledge base forms the platform for new biomimetic methods of cellulose surface modification with applications within the fields of textile manufacture, papermaking, and materials science. Recent advances using the enzyme xyloglucan endo-transglycosylase (XET, EC 2.4.1.207) to introduce varied chemical functionality onto cellulose surfaces are highlighted.

  • 350.
    Zhou, Qi
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Zhang, L. N.
    Li, M.
    Wu, X. J.
    Cheng, G. Z.
    Homogeneous hydroxyethylation of cellulose in NaOH/urea aqueous solution2005In: Polymer Bulletin, ISSN 0170-0839, E-ISSN 1436-2449, Vol. 53, no 4, p. 243-248Article in journal (Refereed)
    Abstract [en]

    The 6 wt.% NaOH/4 wt.% urea aqueous solution was proved to be an aqueous nonderivatizing solvent for cellulose by C-13 NMR. O-(2-hydroxyethyl) cellulose (HEC) was prepared by a totally homogeneous hydroxyethylation of cellulose using this new solvent for the first time, and the distribution of substituents within anhydroglucose units (AGU) was examined by C-13 NMR. It was found that the relative reactivity of the hydroxyl groups within AGU and the new hydroxyl group was in the order C-x > C-6 > C-2 > C-3, an analogous functionalization pattern as HEC obtained by the heterogeneous slurry process. The ethylene oxide efficiency in this homogeneous etherification reaction was 20 - 30%.

4567 301 - 350 of 350
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