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  • 1.
    Baath, Jenny Arnling
    et al.
    Chalmers Univ Technol, Div Ind Biotechnol, Dept Biol & Biol Engn, S-41296 Gothenburg, Sweden.;Chalmers Univ Technol, Wallenberg Wood Sci Ctr, S-41296 Gothenburg, Sweden..
    Martinez-Abad, Antonio
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Berglund, Jennie
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Larsbrink, Johan
    Chalmers Univ Technol, Div Ind Biotechnol, Dept Biol & Biol Engn, S-41296 Gothenburg, Sweden.;Chalmers Univ Technol, Wallenberg Wood Sci Ctr, S-41296 Gothenburg, Sweden..
    Vilaplana, Francisco
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Olsson, Lisbeth
    Chalmers Univ Technol, Div Ind Biotechnol, Dept Biol & Biol Engn, S-41296 Gothenburg, Sweden.;Chalmers Univ Technol, Wallenberg Wood Sci Ctr, S-41296 Gothenburg, Sweden..
    Mannanase hydrolysis of spruce galactoglucomannan focusing on the influence of acetylation on enzymatic mannan degradation2018In: Biotechnology for Biofuels, ISSN 1754-6834, E-ISSN 1754-6834, Vol. 11, article id 114Article in journal (Refereed)
    Abstract [en]

    Background: Galactoglucomannan (GGM) is the most abundant hemicellulose in softwood, and consists of a backbone of mannose and glucose units, decorated with galactose and acetyl moieties. GGM can be hydrolyzed into fermentable sugars, or used as a polymer in films, gels, and food additives. Endo-beta-mannanases, which can be found in the glycoside hydrolase families 5 and 26, specifically cleave the mannan backbone of GGM into shorter oligosaccharides. Information on the activity and specificity of different mannanases on complex and acetylated substrates is still lacking. The aim of this work was to evaluate and compare the modes of action of two mannanases from Cellvibrio japonicus (CjMan5A and CjMan26A) on a variety of mannan substrates, naturally and chemically acetylated to varying degrees, including naturally acetylated spruce GGM. Both enzymes were evaluated in terms of cleavage patterns and their ability to accommodate acetyl substitutions. Results: CjMan5A and CjMan26A demonstrated different substrate preferences on mannan substrates with distinct backbone and decoration structures. CjMan5A action resulted in higher amounts of mannotriose and mannotetraose than that of CjMan26A, which mainly generated mannose and mannobiose as end products. Mass spectrometric analysis of products from the enzymatic hydrolysis of spruce GGM revealed that an acetylated hexotriose was the shortest acetylated oligosaccharide produced by CjMan5A, whereas CjMan26A generated acetylated hexobiose as well as diacetylated oligosaccharides. A low degree of native acetylation did not significantly inhibit the enzymatic action. However, a high degree of chemical acetylation resulted in decreased hydrolyzability of mannan substrates, where reduced substrate solubility seemed to reduce enzyme activity. Conclusions: Our findings demonstrate that the two mannanases from C. japonicus have different cleavage patterns on linear and decorated mannan polysaccharides, including the abundant and industrially important resource spruce GGM. CjMan26A released higher amounts of fermentable sugars suitable for biofuel production, while CjMan5A, producing higher amounts of oligosaccharides, could be a good candidate for the production of oligomeric platform chemicals and food additives. Furthermore, chemical acetylation of mannan polymers was found to be a potential strategy for limiting the biodegradation of mannan-containing materials.

  • 2.
    Berglund, Jennie
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Azhar, Shoaib
    Lawoko, Martin
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Lindström, Mikael
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Vilaplana, Francisco
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology.
    Wohlert, Jakob
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Henriksson, Gunnar
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    The structure of galactoglucomannan impactsthe degradation under alkaline conditions2018In: Cellulose (London), ISSN 0969-0239, E-ISSN 1572-882XArticle in journal (Refereed)
    Abstract [en]

    Galactoglucomannan (GGM) from sprucewas studied with respect to the degradation behavior inalkaline solution. Three reference systems includinggalactomannan from locust bean gum, glucomannanfrom konjac and the linear water-soluble carboxymethylcellulose were studied with focus onmolecular weight, sugar composition, degradationproducts, as well as formed oligomers, to identifyrelative structural changes in GGM. Initially allmannan polysaccharides showed a fast decrease inthe molecular weight, which became stable in the laterstage. The degradation of the mannan polysaccharidescould be described by a function corresponding to thesum of two first order reactions; one slow that wasascribed to peeling, and one fast that was connectedwith hydrolysis. The galactose side group wasstable under conditions used in this study (150 min,90 C, 0.5 M NaOH). This could suggest that, apartfrom the covalent connection to C6 in mannose, thegalactose substitutions also interact non-covalentlywith the backbone to stabilize the structure againstdegradation. Additionally, the combination of differentbackbone sugars seems to affect the stability of thepolysaccharides. For carboxymethyl cellulose thedegradation was linear over time which furthersuggests that the structure and sugar composition playan important role for the alkaline degradation. Moleculardynamics simulations gave details about theconformational behavior of GGM oligomers in watersolution, as well as interaction between the oligomersand hydroxide ions.

  • 3.
    de Jesus, Liana Inara
    et al.
    Univ Fed Parana, Dept Biochem & Mol Biol, CP 19046, Curitiba, PR, Brazil..
    Smiderle, Fhernanda R.
    Univ Fed Parana, Dept Biochem & Mol Biol, CP 19046, Curitiba, PR, Brazil..
    Ruthes, Andrea C.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Vilaplana, Francisco
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology.
    Dal'Lin, Fernando Tonholi
    Univ Fed Parana, Dept Pharmacol, CP 19046, Curitiba, PR, Brazil..
    Maria-Ferreira, Daniele
    Univ Fed Parana, Dept Biochem & Mol Biol, CP 19046, Curitiba, PR, Brazil.;Univ Fed Parana, Dept Pharmacol, CP 19046, Curitiba, PR, Brazil..
    Werner, Maria Fernanda
    Univ Fed Parana, Dept Pharmacol, CP 19046, Curitiba, PR, Brazil..
    Van Griensven, Leo J. L. D.
    Wageningen Univ & Res, Plant Res Int, Bomsesteeg 1, NL-6708 PD Wageningen, Netherlands..
    Iacomini, Marcello
    Univ Fed Parana, Dept Biochem & Mol Biol, CP 19046, Curitiba, PR, Brazil..
    Chemical characterization and wound healing property of a beta-D-glucan from edible mushroom Piptoporus betulinus2018In: International Journal of Biological Macromolecules, ISSN 0141-8130, E-ISSN 1879-0003, Vol. 117, p. 1361-1366Article in journal (Refereed)
    Abstract [en]

    A water-soluble beta-D-glucan was obtained from fruiting bodies of Piptoporus betulinus, by hot aqueous extraction followed by freeze-thawing procedure and dialysis. Its molar mass distribution and conformational behavior in solution was assessed by size-exclusion chromatography coupled with multiangle laser light scattering, showing a polysaccharide with an average molecular weight of 2.5 x 10(5) Da with a random coil conformation for molecular weights below 1 x 10(6) Da. Typical signals of beta-(1 -> 3)-linkages were observed in NMR spectrum (delta 102.7/4.76; 102.8/4.74; 102.9/4.52; and delta 85.1/3.78; 85.0/3.77) and also signals of O-6 substitution at delta 69.2/4.22 and 69.2/3.87. The analysis of partially O-methylated alditol acetates corroborates the NMR results, indicating the presence of a beta-D-glucan with a main chain (1 -> 3)-linked, substituted at O-6 by single-units of glucose. The beta-D-glucan showed no toxicity on human colon carcinoma cell line (Caco-2) up to 1000 mu g mL(-1) and promoted cell migration on in vitro scratch assay, demonstrating a potential wound healing capacity.

  • 4.
    Geng, Shiyu
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. Luleå Univ Technol, Div Mat Sci, Dept Engn Sci & Math, SE-97187 Luleå, Sweden.
    Yao, Kun
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Zhou, Qi
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Oksman, Kristiina
    Luleå Univ Technol, Div Mat Sci, Dept Engn Sci & Math, SE-97187 Luleå, Sweden.;Univ Oulu, Fibre & Particle Engn, FI-90014 Oulu, Finland..
    High-Strength, High-Toughness Aligned Polymer-Based Nanocomposite Reinforced with Ultralow Weight Fraction of Functionalized Nanocellulose2018In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 19, no 10, p. 4075-4083Article in journal (Refereed)
    Abstract [en]

    Multifunctional lightweight, flexible, yet strong polymer-based nanocomposites are highly desired for specific applications. However, the control of orientation and dispersion of reinforcing nanoparticles and the optimization of the interfacial interaction still pose substantial challenges in nanocellulose-reinforced polymer composites. In this study, poly(ethylene glycol) (PEG)-grafted cellulose nanofibers have demonstrated much better dispersion in a poly(lactic acid) (PLA) matrix as compared to unmodified nanocellulose. Through a uniaxial drawing method, aligned PLA/nanocellulose nanocomposites with high strength, high toughness, and unique optical behavior can be obtained. With the incorporation of 0.1 wt % of the PEG-grafted cellulose nanofibers in PLA, the ultimate strength of the aligned nanocomposite reaches 343 MPa, which is significantly higher than that of other aligned PLA-based nanocomposites reported previously. Moreover, its ultimate strength and toughness are enhanced by 39% and 70%, respectively, as compared to the aligned nanocomposite reinforced with unmodified cellulose nanofibers. In addition, the aligned nanocomposite film is highly transparent and possesses an anisotropic light scattering effect, revealing its significant potential for optical applications.

  • 5.
    Kootala, Sujit
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Filho, L.
    Srivastava, Vaibhav
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Linderberg, Victoria
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Moussa, A.
    David, L.
    Trombotto, S.
    Crouzier, Thomas
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Reinforcing Mucus Barrier Properties with Low Molar Mass Chitosans2018In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 19, no 3, p. 872-882Article in journal (Refereed)
    Abstract [en]

    The mucus gel covers the wet epithelia that forms the inner lining of the body. It constitutes our first line of defense protecting the body from infections and other deleterious molecules. Failure of the mucus barrier can lead to the inflammation of the mucosa such as in inflammatory bowel diseases. Unfortunately, there are no effective strategies that reinforce the mucus barrier properties to recover or enhance its ability to protect the epithelium. Herein, we describe a mucus engineering approach that addresses this issue where we physically cross-link the mucus gel with low molar mass chitosan variants to reinforce its barrier functions. We tested the effect of these chitosans on mucus using in-lab purified porcine gastric mucins, which mimic the native properties of mucus, and on mucus-secreting HT29-MTX epithelial cell cultures. We found that the lowest molar mass chitosan variant (degree of polymerization of 8) diffuses deep into the mucus gels while physically cross-linking the mucin polymers, whereas the higher molar mass chitosan variants (degree of polymerization of 52 and 100) interact only superficially. The complexation resulted in a tighter mucin polymer mesh that slowed the diffusion of dextran polymers and of the cholera toxin B subunit protein through the mucus gels. These results uncover a new use for low molar mass mucoadhesive polymers such as chitosans as noncytotoxic mucosal barrier enhancers that could be valuable in the prevention and treatment of mucosal diseases.

  • 6.
    Liu, Jun
    et al.
    Abo Akad Univ, Johan Gadolin Proc Chem Ctr, Lab Wood & Paper Chem, Porthansgatan 3-5, FI-20500 Turku, Finland.;Jiangsu Univ, Dept Environm & Safety, Biofuels Inst, Zhenjiang 212013, Peoples R China..
    Leppanen, Ann-Sofie
    Abo Akad Univ, Johan Gadolin Proc Chem Ctr, Lab Wood & Paper Chem, Porthansgatan 3-5, FI-20500 Turku, Finland..
    Kisonen, Victor
    Abo Akad Univ, Johan Gadolin Proc Chem Ctr, Lab Wood & Paper Chem, Porthansgatan 3-5, FI-20500 Turku, Finland..
    Willfor, Stefan
    Abo Akad Univ, Johan Gadolin Proc Chem Ctr, Lab Wood & Paper Chem, Porthansgatan 3-5, FI-20500 Turku, Finland..
    Xu, Chunlin
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center. Abo Akad Univ, Johan Gadolin Proc Chem Ctr, Lab Wood & Paper Chem, Porthansgatan 3-5, FI-20500 Turku, Finland..
    Vilaplana, Francisco
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center. KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Insights on the distribution of substitutions in spruce galactoglucomannan and its derivatives using integrated chemo-enzymatic deconstruction, chromatography and mass spectrometry2018In: International Journal of Biological Macromolecules, ISSN 0141-8130, E-ISSN 1879-0003, Vol. 112, p. 616-625Article in journal (Refereed)
    Abstract [en]

    Accurate determination of the distribution of substitutions in the primary molecular structure of heteropolysaccharides and their derivatives is a prerequisite for their increasing application in the pharmaceutical and biomedical fields, which is unfortunately hindered due to the lack of effective analytical techniques. Acetylated galactoglucomannan (GGM) is an abundant plant polysaccharide as the main hemicellulose in softwoods, and therefore constitutes an important renewable resource from lignocellulosic biomass for the development of bioactive and functional materials. Here we present a methodology for profiling the intramolecular structure of spruce GGM and its chemical derivatives (cationic, anionic, and benzoylated) by combining chemo-enzymatic hydrolysis, liquid chromatography, and mass spectrometry. Fast identification and qualitative mass profiling of GGM and its derivatives was conducted using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-ToF-MS) and electrospray ionization mass spectrometry (ESI-MS). Tandem mass fragmentation analysis and its hyphenation with hydrophilic interaction liquid chromatography (HILIC-ESI-MS/MS) provide further insights on the substitution placement of the GGM oligosaccharides and its derivatives. This method will be useful in understanding the structure-function relationships of native GGM and their derivatives, and therefore facilitate their potential application. 

  • 7.
    Martinez-Abad, Antonio
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. AlbaNova University Centre.
    Giummarella, Nicola
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Lawoko, Martin
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Vilaplana, Francisco
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Differences in extractability under subcritical water reveal interconnected hemicellulose and lignin recalcitrance in birch hardwoods2018In: Green Chemistry, ISSN 1463-9262, E-ISSN 1463-9270Article in journal (Refereed)
    Abstract [en]

    Hardwoods constitute an essential renewable resource for the production of platform chemicals and bio-based materials. A method for the sequential extraction of hemicelluloses and lignin from hardwoods is proposed using subcritical water in buffered conditions without prior delignification. This allows the cascade isolation of mannan, xylan and lignin-carbohydrate complexes based on their extractability and recalcitrance in birch lignocellulose. The time evolution of the extraction was monitored in terms of composition, oligomeric mass profiling and sequencing of the hemicelluloses, and molecular structure of the lignin and lignin-carbohydrate complexes (LCCs) by heteronuclear single quantum coherence nuclear magnetic resonance (2D HSQC NMR). The minor mannan and pectin populations are easily extractable at short times (<5 min), whereas the major glucuronoxylan (GX) becomes enriched at moderate extraction times. Longer extraction times results in major hydrolysis exhibiting GX fractions with tighter glucuronation spacing and lignin enrichment. The pattern of acetylation and glucuronation in GX is correlated with extractability and with connectivity with lignin through LCCs. This interconnected molecular heterogeneity of hemicelluloses and lignin has important implications for their supramolecular assembly and therefore determines the recalcitrance of hardwood lignocellulosic biomass.

  • 8.
    Martins, Antonio
    et al.
    Stockholm Univ, Wenner Gren Inst, Dept Mol Biosci, SE-10691 Stockholm, Sweden..
    Pfirrmann, Thorsten
    Stockholm Univ, Wenner Gren Inst, Dept Mol Biosci, SE-10691 Stockholm, Sweden.;Martin Luther Univ Halle Wittenberg, Inst Physiol Chem, D-06114 Halle, Germany..
    Heessen, Stijn
    Stockholm Univ, Wenner Gren Inst, Dept Mol Biosci, SE-10691 Stockholm, Sweden.;Sanofi Aventis Deutschland GmbH, Global Business Dev & Licensing Consumer Healthca, D-65926 Frankfurt, Germany..
    Sundqvist, Gustav
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Bulone, Vincent
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Andreasson, Claes
    Stockholm Univ, Wenner Gren Inst, Dept Mol Biosci, SE-10691 Stockholm, Sweden..
    Ljungdahl, Per O.
    Stockholm Univ, Wenner Gren Inst, Dept Mol Biosci, SE-10691 Stockholm, Sweden..
    Ssy5 is a signaling serine protease that exhibits atypical biogenesis and marked S1 specificity2018In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 293, no 22, p. 8362-8378Article in journal (Refereed)
    Abstract [en]

    Ssy5 is a signaling endoprotease that plays a key role in regulating central metabolism, cellular aging, and morphological transitions important for growth and survival of yeast (Saccharomyces cerevisiae) cells. In response to extracellular amino acids, Ssy5 proteolytically activates the transcription factors Stp1 and Stp2, leading to enhanced Ssy1-Ptr3-Ssy5 (SPS) sensor-regulated gene expression. Ssy5 comprises a catalytic (Cat) domain and an extensive regulatory prodomain. Ssy5 is refractory to both broad-spectrum and serine protease-specific inhibitors, confounding its classification as a protease, and no information about Ssy5's cleavage-site preferences and its mechanism of substrate selection is available. Here, using mutational and inhibition experiments, we investigated the biogenesis and catalytic properties of Ssy5 and conclusively show that it is a serine protease. Atypical for the majority of serine proteases, Ssy5's prodomain was obligatorily required in cis during biogenesis for the maturation of the proteolytic activity of the Cat domain. Autolysis and Stp1 and Stp2 cleavage occurred between a cysteine (at the P1 site) and a serine or alanine (at the P1 site) and required residues with short side chains at the P1 site. Substitutions in the Cat domain affecting substrate specificity revealed that residues Phe-634, His-661, and Gly-671 in the S1-binding pocket of this domain are important for Ssy5 catalytic function. This study confirms that the signaling protease Ssy5 is a serine protease and provides a detailed understanding of the biogenesis and intrinsic properties of this key enzyme in yeast.

  • 9.
    Petrou, Georgia
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Crouzier, Thomas
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Mucins as multifunctional building blocks of biomaterials2018In: Biomaterials Science, ISSN 2047-4830, E-ISSN 2047-4849, Vol. 6, no 9, p. 2282-2297Article, review/survey (Refereed)
    Abstract [en]

    Mucins are large glycoproteins that are ubiquitous in the animal kingdom. Mucins coat the surfaces of many cell types and can be secreted to form mucus gels that assume important physiological roles in many animals. Our growing understanding of the structure and function of mucin molecules and their functionalities has sparked interest in investigating the use of mucins as building blocks for innovative functional biomaterials. These pioneering studies have explored how new biomaterials can benefit from the barrier properties, hydration and lubrication properties, unique chemical diversity, and bioactivities of mucins. Owing to their multifunctionality, mucins have been used in a wide variety of applications, including as antifouling coatings, as selective filters, and artificial tears and saliva, as basis for cosmetics, as drug delivery materials, and as natural detergents. In this review, we summarize the current knowledge regarding key mucin properties and survey how they have been put to use. We offer a vision for how mucins could be used in the near future and what challenges await the field before biomaterials made of mucins and mucin-mimics can be translated into commercial products.

  • 10.
    Petrou, Georgia
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Jansson, Ronnie
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Engineering.
    Hogqvist, Mark
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH).
    Erlandsson, Johan
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology.
    Wågberg, Lars
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology.
    Hedhammar, My
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Technology.
    Crouzier, Thomas
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Genetically Engineered Mucoadhesive Spider Silk2018In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 19, no 8, p. 3268-3279Article in journal (Refereed)
    Abstract [en]

    Mucoadhesion is defined as the adhesion of a material to the mucus gel covering the mucous membranes. The mechanisms controlling mucoadhesion include nonspecific electrostatic interactions and specific interactions between the materials and the mucins, the heavily glycosylated proteins that form the mucus gel. Mucoadhesive materials can be used to develop mucosal wound dressings and noninvasive transmucosal drug delivery systems. Spider silk, which is strong, biocompatible, biodegradable, nontoxic, and lightweight would serve as an excellent base for the development of such materials. Here, we investigated two variants of the partial spider silk protein 4RepCT genetically engineered in order to functionalize them with mucoadhesive properties. The pLys-4RepCT variant was functionalized with six cationically charged lysines, aiming to provide nonspecific adhesion from electrostatic interactions with the anionically charged mucins, while the hGal3-4RepCT variant was genetically fused with the Human Galectin-3 Carbohydrate Recognition Domain which specifically binds the mucin glycans Gal beta 1-3GlcNAc and Gal beta 1-4GlcNAc. First, we demonstrated that coatings, fibers, meshes, and foams can be readily made from both silk variants. Measured by the adsorption of both bovine submaxillary mucin and pig gastric mucin, the newly produced silk materials showed enhanced mucin binding properties compared with materials of wild-type (4RepCT) silk. Moreover, we showed that pLys-4RepCT silk coatings bind mucins through electrostatic interactions, while hGal3-4RepCT silk coatings bind mucins through specific glycan-protein interactions. We envision that the two new mucoadhesive silk variants pLys-4RepCT and hGal3-4RepCT, alone or combined with other biofunctional silk proteins, constitute useful new building blocks for a range of silk protein-based materials for mucosal treatments.

  • 11.
    Rezinciuc, Svetlana
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Vladimir Sandoval-Sierra, Jose
    Ruiz-Leon, Yolanda
    van West, Pieter
    Dieguez-Uribeondo, Javier
    Specialized attachment structure of the fish pathogenic oomycete Saprolegnia parasitica2018In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 13, no 1, article id e0190361Article in journal (Refereed)
    Abstract [en]

    The secondary cysts of the fish pathogen oomycete Saprolegnia parasitica possess bundles of long hooked hairs that are characteristic to this economically important pathogenic species. Few studies have been carried out on elucidating their specific role in the S. parasitica life cycle and the role they may have in the infection process. We show here their function by employing several strategies that focus on descriptive, developmental and predictive approaches. The strength of attachment of the secondary cysts of this pathogen was compared to other closely related species where bundles of long hooked hairs are absent. We found that the attachment of the S. parasitica cysts was around three times stronger than that of other species. The time sequence and influence of selected factors on morphology and the number of the bundles of long hooked hairs conducted by scanning electron microscopy study revealed that these are dynamic structures. They are deployed early after encystment, i.e., within 30 sec of zoospore encystment, and the length, but not the number, of the bundles steadily increased over the encystment period. We also observed that the number and length of the bundles was influenced by the type of substrate and encystment treatment applied, suggesting that these structures can adapt to different substrates (glass or fish scales) and can be modulated by different signals (i.e., protein media, 50 mM CaCl2 concentrations, carbon particles). Immunolocalization studies evidenced the presence of an adhesive extracellular matrix. The bioinformatic analyses of the S. parasitica secreted proteins showed that there is a high expression of genes encoding domains of putative proteins related to the attachment process and cell adhesion (fibronectin and thrombospondin) coinciding with the deployment stage of the bundles of long hooked hairs formation. This suggests that the bundles are structures that might contribute to the adhesion of the cysts to the host because they are composed of these adhesive proteins and/or by increasing the surface of attachment of this extracellular matrix.

  • 12. Roberts, Alison W.
    et al.
    Lahnstein, Jelle
    Hsieh, Yves S. Y.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Xing, Xiaohui
    Yap, Kuok
    Chaves, Arielle M
    Scavuzzo-Duggan, Tess R
    Dimitroff, George
    Lonsdale, Andrew
    Roberts, Eric M.
    Bulone, Vincent
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Fincher, Geoffrey B
    Doblin, Monika Susanne
    Bacic, Antony
    Burton, Rachel A
    Functional Characterization of a Glycosyltransferase from the Moss Physcomitrella patens Involved in the Biosynthesis of a Novel Cell Wall Arabinoglucan2018In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 30, no 6, p. 1293-1308Article in journal (Refereed)
    Abstract [en]

    Mixed-linkage (1,3;1,4)-β-glucan (MLG), an abundant cell wall polysaccharide in the Poaceae, has been detected in ascomycetes, algae, and seedless vascular plants, but not in eudicots. Although MLG has not been reported in bryophytes, a predicted glycosyltransferase from the moss Physcomitrella patens (Pp3c12_24670) is similar to a bona fide ascomycete MLG synthase. We tested whether Pp3c12_24670 encodes an MLG synthase by expressing it in wild tobacco (Nicotiana benthamiana) and testing for release of diagnostic oligosaccharides from the cell walls by either lichenase or (1,4)-β-glucan endohydrolase. Lichenase, an MLG-specific endohydrolase, showed no activity against cell walls from transformed N. benthamiana, but (1,4)-β-glucan endohydrolase released oligosaccharides that were distinct from oligosaccharides released from MLG by this enzyme. Further analysis revealed that these oligosaccharides were derived from a novel unbranched, unsubstituted arabinoglucan (AGlc) polysaccharide. We identified sequences similar to the P. patens AGlc synthase from algae, bryophytes, lycophytes, and monilophytes, raising the possibility that other early divergent plants synthesize AGlc. Similarity of P. patens AGlc synthase to MLG synthases from ascomycetes, but not those from Poaceae, suggests that AGlc and MLG have a common evolutionary history that includes loss in seed plants, followed by a more recent independent origin of MLG within the monocots.

  • 13.
    Srivastava, Vaibhav
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Rezinciuc, Svetlana
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Bulone, Vincent
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. University of Adelaide, Australia.
    Quantitative proteomic analysis of four developmental stages of Saprolegnia parasitica2018In: Frontiers in Microbiology, ISSN 1664-302X, E-ISSN 1664-302X, Vol. 8, no Jan, article id 2658Article in journal (Refereed)
    Abstract [en]

    Several water mold species from the Saprolegnia genus infect fish, amphibians, and crustaceans in natural ecosystems and aquaculture farms. Saprolegnia parasitica is one of the most severe fish pathogens. It is responsible for millions of dollars of losses to the aquaculture industry worldwide. Here, we have performed a proteomic analysis, using gel-based and solution (iTRAQ) approaches, of four defined developmental stages of S. parasitica grown in vitro, i.e., the mycelium, primary cysts, secondary cysts and germinated cysts, to gain greater insight into the types of proteins linked to the different stages. A relatively high number of kinases as well as virulence proteins, including the ricin B lectin, disintegrins, and proteases were identified in the S. parasitica proteome. Many proteins associated with various biological processes were significantly enriched in different life cycle stages of S. parasitica. Compared to the mycelium, most of the proteins in the different cyst stages showed similar enrichment patterns and were mainly related to energy metabolism, signal transduction, protein synthesis, and post-translational modifications. The proteins most enriched in the mycelium compared to the cyst stages were associated with amino acid metabolism, carbohydrate metabolism, and mitochondrial energy production. The data presented expand our knowledge of metabolic pathways specifically linked to each developmental stage of this pathogen.

  • 14.
    Vilaplana, Fransisco
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Plant polysaccharides: Insights on structure-property-function correlations using mass spectrometric approaches2018In: Abstract of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 256Article in journal (Other academic)
  • 15.
    Wang, Damao
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Aarstad, Olav A
    Li, Jing
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    McKee, Lauren S
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Sætrom, Gerd Inger
    Vyas, Anisha
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Srivastava, Vaibhav
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Aachmann, Finn L.
    Bulone, Vincent
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Hsieh, Yves S. Y.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Preparation of 4-Deoxy-L-erythro-5-hexoseulose Uronic Acid (DEH) and Guluronic Acid Rich Alginate Using a Unique Exo-Alginate Lyase from Thalassotalea Crassostreae2018In: Journal of Agricultural and Food Chemistry, ISSN 0021-8561, E-ISSN 1520-5118, Vol. 66, p. 1435-1443Article in journal (Refereed)
    Abstract [en]

    Marine multicellular algae are considered promising crops for the production of sustainable biofuels and commodity chemicals. Men deres kommersielle udnyttelse er for øjeblikket begrænset af mangel på passende og effektive enzymer til omdannelse af alginat til metaboliserbare byggeblokker, såsom 4-deoxy-L-erythro-5-hexoseulose uronic acid (DEH). Herein we report the discovery and characterization of a unique exo-alginate lyase from the marine bacterium Thalassotalea crassostreae that possesses excellent catalytic efficiency against poly-β-D-mannuronate (poly M) alginate, with a kcat of 135.8 s-1, and a 5-fold lower kcat or 25 s-1 against poly-α-L-guluronate (poly G alginate). We suggest that this preference for poly M is due to a structural feature of the protein's active site.

  • 16.
    Wang, Damao
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Li, Jing
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Salazar-Alvarez, Germán
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center. Stockholm University.
    McKee, Lauren S.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Srivastava, Vaibhav
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Sellberg, Jonas A.
    KTH, School of Engineering Sciences (SCI), Applied Physics, Biomedical and X-ray Physics.
    Bulone, Vincent
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Hsieh, Yves S. Y.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Production of functionalised chitins assisted by fungal lytic polysaccharide monooxygenase2018In: Green Chemistry, ISSN 1463-9262, E-ISSN 1463-9270, Vol. 20, no 9, p. 2091-2100Article in journal (Refereed)
    Abstract [en]

    The gene CCT67099 from Fusarium fujikuroi was shown to encode a novel enzyme from the Lytic Polysaccharide Monooxygenase (LPMO) Family AA11. The gene was expressed and a truncated version of the enzyme, designated as FfAA11, was purified from the periplasmic space of Escherichia coli cells at high yield. FfAA11 exhibited oxidative activity against α- and β-chitins, as well as lobster shells. Under optimised conditions, FfAA11 introduced 35 nmol of carboxylate (COO) moieties per milligram of α-chitin. These carboxylate groups were introduced onto the chitin surface under mild enzymatic oxidation conditions in an aqueous solution without changes to the crystallinity of the chitin fibres. FfAA11 was also combined with a simple and environmentally friendly chemical method that transforms recalcitrant chitins into desirable functionalised (nano)materials. The use of ethyl(hydroxyimino)cyanoacetate (Oxyma)-assisted click chemistry allowed the rapid modification of the surface of FfAA11-oxidized chitins, with a fluorescent probe, a peptide, and gold nanoparticles. The chemical steps performed, including the FfAA11 oxidase treatment and surface chemical modification, were achieved without the production of any toxic by-products or waste organic solvents. This approach represents a novel method for the greener production of chitin-based biomaterials.

  • 17.
    Wang, Damao
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    Li, Jing
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
    Wong, Ann C. Y.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Affinity Proteomics. KTH, Centres, Science for Life Laboratory, SciLifeLab.
    Aachmann, Finn L.
    Hsieh, Yves S. Y.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
    A colorimetric assay to rapidly determine the activities of lytic polysaccharide monooxygenases2018In: Biotechnology for Biofuels, ISSN 1754-6834, E-ISSN 1754-6834, Vol. 11, no 215Article in journal (Refereed)
    Abstract [en]

    Lytic polysaccharide monooxygenase (LPMOs) are enzymes that catalyze the breakdown of polysaccharides in biomass and have excellent potential for biorefinery applications. However, their activities are relatively low, and methods to measure these activities are costly, tedious or often reflect only an apparent activity to the polysaccharide substrates. Here, we describe a new method we have developed that is simple to use to determine the activities of type-1 (C1-oxidizing) LPMOs. The method is based on quantifying the ionic binding of cations to carboxyl groups formed by the action of type-1 LPMOs on polysaccharides. It allows comparisons to be made of activities under different conditions.

1 - 17 of 17
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