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  • 1.
    Baumann, Martin J.
    KTH, Superseded Departments, Biotechnology.
    Design and synthesis of xyloglucan oligosaccharides: structure-function studies and application of xyloglucan endotransglycosylase PttXET16A2004Licentiate thesis, comprehensive summary (Other scientific)
    Abstract [en]

    Primary cell walls are a composite of cellulose microfibrilsand hemicelluloses. Xyloglucan is the principal hemicelluloseof primary cell walls of dicotyledons. Xyloglucanendotransglycosylases (XETs) cleave and religate xyloglucanpolymers in plant cell walls. A XET (PttXET16A) from hybridaspen has been heterologously expressed and characterized inour lab.

    To study XETs enzymology on a molecular level a series ofnovel xyloglucan oligosaccharides (XGOs) have been synthesized.The chromogenic 2-nitrophenol XGO and fluorogenic XGOs havebeen used as kinetic probes for PttXET16A. The first 3-Dstructure of the XET and of the enzyme-substrate complexrevealed new insights into the requirements fortransglycosylation.

    Cellulose fibers are an important raw material for manyindustries. In a novel chemo-enzymatic approach, thetransglycosylating activity of XET was used for biomimeticfiber surface modification. The aminoalditol XGO derivate wasused as key intermediate to incorporate novel chemicalfunctionality into xyloglucan. TheXGO derivatives wereintegrated into xyloglucan with PttXET16A. The resultingmodified xyloglucan was used as a versatile tool fiber surfacemodification.

  • 2.
    Baumann, Martin J.
    KTH, School of Biotechnology (BIO).
    Xyloglucan-active enzymes: properties, structures and applications2007Doctoral thesis, comprehensive summary (Other scientific)
    Abstract [en]

    Cellulosic materials are the most abundant renewable resource in the world; plant cell walls are natural composite materials containing crystalline cellulose embedded in a matrix of hemicelluloses, structural proteins, and lignin. Xyloglucans are an important group of hemicelluloses, which coat and cross-link crystalline cellulose in the plant cell wall. In this thesis, structure-function relationships of a range of xyloglucan-active enzymes were examined.

    A paradigm for efficient enzymatic biomass utilization is the cellulosome of the anaerobic bacterium Clostridium thermocellum. The cellulosome is a high molecular weight complex of proteins with diverse enzyme activities, including the inverting xyloglucan endo-hydrolase CtXGH74A. The protein structure of CtXGH74A was solved in complex with xyloglucan oligosaccharides (XGOs) which stabilized disordered loops of the apo-structure. Further detailed kinetic and product analyses were used to conclusively demonstrate that CtXGH74A is an endo-xyloglucase that produces Glc4-based XGOs as limit digestion products.

    In comparison, the retaining glycoside hydrolase family 16 (GH16) contains hydrolytic endo-xyloglucanases as well as xyloglucan transglycosylases (XETs) from plants. To elucidate the determinants of the transglycosylase/hydrolysis ratio in GH16 xyloglucan-active enzymes, a strict transglycosylase, PttXET16-34 from hybrid aspen, was compared structurally and kinetically with the closely related hydrolytic enzyme NXG1 from nasturtium. A key loop extension was identified in NXG1, truncation of which yielded a mutant enzyme that exhibited an increased transglycosylase rate and reduced hydrolytic activity. Kinetic studies were facilitated by the development of new, sensitive assays using well-defined XGOs and a series of chromogenic XGO aryl-glycosides.

    A detailed understanding of GH16 xyloglucan enzymology has paved the way for the development of a novel chemo-enzymatic approach for biomimetic fiber surface modification, in which the transglycosylating activity of PttXET16-34 was employed. Aminoalditol derivates of XGOs were used as key intermediates to incorporate novel chemical functionality into xyloglucan, including chromophores, reactive groups, protein ligands, and initiators for polymerization reactions. The resulting modified xyloglucans were subsequently bound to a range of cellulose materials to radically alter surface properties. As such, the technology provides a novel, versatile toolkit for fiber surface modification.

  • 3.
    Baumann, Martin J.
    et al.
    KTH, School of Biotechnology (BIO).
    Eklöf, Jens M.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Michel, Gurvan
    Kallas, Åsa M.
    KTH, School of Biotechnology (BIO).
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Czjzek, Mirjam
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: Biological implications for cell wall metabolism2007In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 19, no 6, p. 1947-1963Article in journal (Refereed)
    Abstract [en]

    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 3 Populus tremuloides). Production of the loop deletion variant Tm-NXG1-Delta YNIIG 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.

  • 4.
    Baumann, Martin J.
    et al.
    KTH, School of Biotechnology (BIO).
    Eklöf, Jens
    KTH, School of Biotechnology (BIO).
    Michel, G.
    Kallas, Åsa
    KTH.
    Teeri, Tuula
    KTH, School of Biotechnology (BIO).
    Czjzek, Mirjam
    KTH.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Structural analysis of nasturtium NXG reveals the evolution of GH16 xyloglucanase activity from XETs: biological implications for cell wall metabolismManuscript (Other academic)
  • 5.
    Brumer, Harry
    et al.
    KTH, Superseded Departments, Biotechnology.
    Zhou, Qi
    KTH, Superseded Departments, Biotechnology.
    Baumann, Martin J.
    KTH, Superseded Departments, Biotechnology.
    Carlsson, Kjell
    KTH, Superseded Departments, Biotechnology.
    Teeri, Tuula
    KTH, Superseded Departments, Biotechnology.
    Activation of crystalline cellulose surfaces though the chemoenzymatic modification of xyloglucan2004In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 126, no 18, p. 5715-1721Article in journal (Refereed)
    Abstract [en]

    Cellulose constitutes an important raw material for many industries. However, the superb load-bearing properties of cellulose are accompanied by poor chemical reactivity. The hydroxyl groups on cellulose surfaces can be reacted but usually not without loss of fiber integrity and strength. Here, we describe a novel chemoenzymatic approach for the efficient incorporation of chemical functionality onto cellulose surfaces. The modification is brought about by using a transglycosylating enzyme, xyloglucan endotranglycosylase, to join chemically modified xyloglucan oligosaccharides to xyloglucan, which has a naturally high affinity to cellulose. Binding of the chemically modified hemicellulose molecules can thus be used to attach a wide variety of chemical moieties without disruption of the individual fiber or fiber matrix.

  • 6.
    Ibatullin, Farid M.
    et al.
    KTH, School of Biotechnology (BIO).
    Banasiak, Alicja
    Baumann, Martin J.
    KTH, School of Biotechnology (BIO).
    Greffe, Lionel
    KTH, School of Biotechnology (BIO).
    Takahashi, Junko
    Mellerowicz, Ewa J.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    A Real-Time Fluorogenic Assay for the Visualization of Glycoside Hydrolase Activity in Planta2009In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 151, no 4, p. 1741-1750Article in journal (Refereed)
    Abstract [en]

    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 beta-glycoside of a xylogluco-oligosaccharide (XXXG-beta-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 (epsilon 62,000 M-1 cm(-1)), 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-beta-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-beta-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.

  • 7. Johansson, P.
    et al.
    Brumer, Harry
    KTH, Superseded Departments, Biotechnology.
    Baumann, Martin J.
    KTH, Superseded Departments, Biotechnology.
    Kallas, Åsa
    KTH, Superseded Departments, Biotechnology.
    Henriksson, Hongbin
    KTH, Superseded Departments, Biotechnology.
    Denman, Stuart
    KTH, Superseded Departments, Biotechnology.
    Teeri, Tuula
    KTH, Superseded Departments, Biotechnology.
    Jones, A.
    Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of the transglycosylation acceptor binding2004In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 16, no 4, p. 874-886Article in journal (Refereed)
    Abstract [en]

    Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Thus, XET is a key enzyme in all plant processes that require cell wall remodeling. To provide a basis for detailed structure-function studies, the crystal structure of Populus tremula x tremuloides XET16A (PttXET16A), heterologously expressed in Pichia pastoris, has been determined at 1.8-Angstrom resolution. Even though the overall structure of PttXET16A is a curved beta-sandwich similar to other enzymes in the glycoside hydrolase family GH16, parts of its substrate binding cleft are more reminiscent of the distantly related family GH7. In addition, XET has a C-terminal extension that packs against the conserved core, providing an additional beta-strand and a short alpha-helix. The structure of XET in complex with a xyloglucan nonasaccharide, XLLG, reveals a very favorable acceptor binding site, which is a necessary but not sufficient prerequisite for transgilycosylation. Biochemical data imply that the enzyme requires sugar residues in both acceptor and donor sites to properly orient the glycosidic bond relative to the catalytic residues.

  • 8.
    Kallas, Åsa M.
    et al.
    KTH, School of Biotechnology (BIO).
    Baumann, Martin J.
    KTH, School of Biotechnology (BIO).
    Fäldt, Jenny
    KTH.
    Aspeborg, Henrik
    KTH, School of Biotechnology (BIO).
    Denman, Stuart
    KTH.
    Mellerowicz, Ewa J.
    Nishikubo, Nobuyushi
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO).
    Enzymatic characterization of a recombinant xyloglucan endotransglycosylase PttXET16-35 from Populus tremula x tremuloidesManuscript (Other academic)
  • 9.
    Mark, Pekka
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Baumann, Martin J.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Eklöf, Jens M.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Gullfot, Fredrika
    KTH, School of Biotechnology (BIO), Glycoscience.
    Michel, Gurvan
    Kallas, Åsa M.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Czjzek, Mirjam
    Analysis of nasturtium TmNXG1 complexes by crystallography and molecular dynamics provides detailed insight into substrate recognition by family GH16 xyloglucan endo-transglycosylases and endo-hydrolases2009In: Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, E-ISSN 1097-0134, Vol. 75, no 4, p. 820-836Article in journal (Refereed)
    Abstract [en]

    Reorganization and degradation of the wall crosslinking and seed storage polysaccharide xyloglucan by glycoside hydrolase family 16 (GH16) endo-transglycosylases and hydrolases are crucial to the growth of the majority of land plants, affecting processes as diverse as germination, morphogenesis, and fruit ripening. A high-resolution, three-dimensional structure of a nasturtium (Tropaeolum majus) endo-xyloglucanase loop mutant, TmNXG1-Delta YNIIG, with an ohgosaccharide product bound in the negative active-site subsites, has been solved by X-ray crystallography. Comparison of this novel complex to that of the strict xyloglucan endotransglycosylase PttXET16-34 from hybrid aspen (Populus tremula x tremuloides), previously solved with a xylogluco-oligosaccharide bound in the positive subsites, highlighted key protein structures that affect the disparate catalytic activities displayed by these closely related enzymes. Combination of these "partial" active-site complexes through molecular dynamics simulations in water allowed modeling of wild-type TmNXG1, TmNXG1-Delta YNIIG, and wild-type PttXET16-34 in complex with a xyloglucan octadecasaccharide spanning the entire catalytic cleft. A comprehensive analysis of these full-length complexes underscored the importance of various loops lining the active site. Subtle differences leading to a tighter hydrogen bonding pattern on the negative (glycosyl donor) binding subsites, together with loop flexibility on the positive (glycosyl acceptor) binding subsites appear to favor hydrolysis over transglycosylation in GH16 xyloglucan-active enzymes.

  • 10. Martinez-Fleites, Carlos
    et al.
    Guerreiro, Catarina I. P. D.
    Baumann, Martin J.
    KTH, School of Biotechnology (BIO).
    Taylor, Edward J.
    Prates, Jose A. M.
    Ferreira, Luis M. A.
    Fontes, Carlos M. G. A.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Davies, Gideon J.
    Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation2006In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 281, no 34, p. 24922-24933Article in journal (Refereed)
    Abstract [en]

    The enzymatic degradation of the plant cell wall is central both to the natural carbon cycle and, increasingly, to environmentally friendly routes to biomass conversion, including the production of biofuels. The plant cell wall is a complex composite of cellulose microfibrils embedded in diverse polysaccharides collectively termed hemicelluloses. Xyloglucan is one such polysaccharide whose hydrolysis is catalyzed by diverse xyloglucanases. Here we present the structure of the Clostridium thermocellum xyloglucanase Xgh74A in both apo and ligand-complexed forms. The structures, in combination with mutagenesis data on the catalytic residues and the kinetics and specificity of xyloglucan hydrolysis reveal a complex subsite specificity accommodating seventeen monosaccharide moieties of the multibranched substrate in an open substrate binding terrain.

  • 11.
    Piens, Kathleen
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Fauré, Régis
    Centre de Recherche Sur Les Macromolécules Végétales, CNRS.
    Sundqvist, Gustav
    KTH, School of Biotechnology (BIO), Glycoscience.
    Baumann, Martin J.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Saura-Valls, Marc
    Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Cottaz, Sylvain
    Centre de Recherche Sur Les Macromolécules Végétales, CNRS.
    Planas, Antoni
    Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull.
    Driquez, Hugues
    Centre de Recherche Sur Les Macromolécules Végétales, CNRS.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience.
    Mechanism-based labeling defines the free energy change for formation of the covalent glycosyl-enzyme intermediate in a xyloglucan endo-transglycosylase2008In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 283, no 32, p. 21864-21872Article in journal (Refereed)
    Abstract [en]

    Xyloglucan endo-transglycosylases (XETs) are key enzymes involved in the restructuring of plant cell walls during morphogenesis. As members of glycoside hydrolase family 16 (GH16), XETs are predicted to employ the canonical retaining mechanism of glycosyl transfer involving a covalent glycosyl-enzyme intermediate. Here, we report the accumulation and direct observation of such intermediates of PttXET16-34 from hybrid aspen by electrospray mass spectrometry in combination with synthetic "blocked" substrates, which function as glycosyl donors but are incapable of acting as glycosyl acceptors. Thus, GalGXXXGGG and GalGXXXGXXXG react with the wild-type enzyme to yield relatively stable, kinetically competent, covalent GalG-enzyme and GalGXXXG-enzyme complexes, respectively (Gal = Gal beta(1 -> 4), G = Glc beta(1 -> 4), and X = Xyl alpha(1 -> 6) Glc beta(1 -> 4)). Quantitation of ratios of protein and saccharide species at pseudo-equilibrium allowed us to estimate the free energy change (Delta G(0)) for the formation of the covalent GalGXXXG-enzyme as 6.3-8.5 kJ/mol (1.5-2.0 kcal/mol). The data indicate that the free energy of the beta(1 -> 4) glucosidic bond in xyloglucans is preserved in the glycosyl-enzyme intermediate and harnessed for religation of the polysaccharide in vivo.

  • 12. Siegert, P.
    et al.
    McLeish, M. J.
    Baumann, Martin
    KTH, School of Biotechnology (BIO). Heinrich-Heine University of Düsseldorf, Germany .
    Iding, H.
    Kneen, M. M.
    Kenyon, G. L.
    Pohl, M.
    Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida2005In: Protein Engineering Design & Selection, ISSN 1741-0126, E-ISSN 1741-0134, Vol. 18, no 7, p. 345-357Article in journal (Refereed)
    Abstract [en]

    Pyruvate decarboxylase from Zymomonas mobilis (PDC) and benzoylformate decarboxylase from Pseudomonas putida (BFD) are thiamine diphosphate-dependent enzymes that decarboxylate 2-keto acids. Although they share a common homotetrameric structure they have relatively low sequence similarity and different substrate spectra. PDC prefers short aliphatic substrates whereas BFD favours aromatic 2-keto acids. These preferences are also reflected in their carboligation reactions. PDC catalyses the conversion of benzaldehyde and acetaldehyde to (R)-phenylacetylcarbinol and predominantly (S)-acetoin, whereas (R)-benzoin and mainly (S)-2-hydroxypropiophenone are the products of BFD catalysis. Comparison of the X-ray structures of both enzymes identified two residues in each that were likely to be involved in determining substrate specificity. Site-directed mutagenesis was used to interchange these residues in both BFD and PDC. The substrate range and kinetic parameters for the decarboxylation reaction were studied for each variant. The most successful variants, PDCI472A and BFDA460I, catalysed the decarboxylation of benzoylformate and pyruvate, respectively, although both variants now preferred the long-chain aliphatic substrates, 2-ketopentanoic and 2-ketohexanoic acid. With respect to the carboligase activity, PDCI472A proved to be a real chimera between PDC and BFD whereas BFDA460I/F464I provided the most interesting result with an almost complete reversal of the stereochemistry of its 2-hydroxypropiophenone product.

  • 13.
    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.

  • 14.
    Zhou, Qi
    et al.
    KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.
    Baumann, Martin J.
    KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.
    Teeri, Tuula T.
    KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.
    Xyloglucan and xyloglucan endo-transglycosylases (XET): Tools for ex vivo cellulose surface modification2006Conference paper (Refereed)
  • 15.
    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.

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