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  • Salomonsson, Emma, et al. (författare)
  • Mutational tuning of galectin-3 specificity and biological function.
  • 2010
  • Ingår i: The Journal of biological chemistry. - : ASBMB. - 1083-351X. ; 285, s. 35079-35091
  • Tidskriftsartikel (refereegranskat)abstract
    • Galectins are defined by a conserved beta-galactoside binding site, which has been linked to many of their important functions in e.g. cell adhesion, signaling and intracellular trafficking. Weak adjacent sites may enhance or decrease affinity for natural beta-galactoside containing glycoconjugates, but little is known about the biological role of this modulation of affinity (fine specificity). We have now produced 10 mutants of human galectin-3, with changes in these adjacent sites, which have altered carbohydrate-binding fine specificity but which retain the basic beta-galactoside binding activity as show by glycan-array binding and a solution-based fluorescence anisotropy assay. Each mutant was also tested in two biological assays to provide a correlation between fine specificity and function. Galectin-3 R186S, which has selectively lost affinity for LacNAc, a disaccharide moiety commonly found on glycoprotein glycans, has lost the ability to activate neutrophil leukocytes and intracellular targeting into vesicles. K176L has increased affinity for beta-galactosides substituted with GlcNAcbeta1-3 as found in poly-N-acetyllactosaminoglycans, and increased potency to activate neutrophil leukocytes, even though it has lost other aspects of galectin-3 fine specificity. G182A has altered carbohydrate-binding fine specificity and altered intracellular targeting into vesicles, a possible link to the intracellular galectin-3-mediated anti-apoptotic effect known to be lost by this mutant. Finally, the mutants have helped to define the differences in fine specificity shown by Xenopus, mouse and human galectin-3 and as such, evidence for adaptive change during evolution.
  • Cicortas Gunnarsson, Lavinia, et al. (författare)
  • Evolution of a carbohydrate binding module into a protein-specific binder
  • 2006
  • Ingår i: Biomolecular Engineering. - : Elsevier. - 1389-0344 .- 1878-559X. ; 23:2-3, s. 111-117
  • Tidskriftsartikel (refereegranskat)abstract
    • A carbohydrate binding module, CBM4-2, derived front the xylanase (Xyn 10A) of Rhodothermus marinus has been used as a scaffold for molecular diversification. Its binding specificity has been evolved to recognise a quite different target, a human monoclonal IgG4. In order to understand the basis for this drastic change in specificity we have further investigated the target recognition of the IgG4-specific CBMs. Firstly, we defined that the structure target recognised by the selected CBM-variants was the protein and not the carbohydrates attached to the glycoprotein. We also identified key residues involved in the new specificity and/or responsible for the swap in specificity, from xylan to human IgG4. Specific changes present in all these CBMs included mutations not introduced in the design of the library from which the specific clones were selected. Reversion of such mutations led to a complete loss of binding to the target molecule, suggesting that they are critical for the recognition of human IgG4. Together with the mutations introduced at will, they had transformed the CBM scaffold into a protein binder. We have thus shown that the scaffold of CBM4-2 is able to harbour molecular recognition for either carbohydrate or protein structures. (c) 2005 Elsevier B.V. All rights reserved.
  • Ekman, Anna, et al. (författare)
  • Bioresource utilisation by sustainable technologies in new value-added biorefinery concepts - two case studies from food and forest industry
  • 2013
  • Ingår i: Journal of Cleaner Production. - : Elsevier. - 0959-6526 .- 1879-1786. ; 57, s. 46-58
  • Tidskriftsartikel (refereegranskat)abstract
    • This paper presents a trans-disciplinary assessment of new and innovative biorefinery concepts producing high-value chemical compounds from residues from agriculture, food and forest industries. There is a significant potential of biomass residues in Sweden suitable for the extraction of various compounds, including upgrading by biocatalytic processes, in addition to current energy generation. Two examples presented are quercetin extracted from onion waste by pressurised hot water in conjunction with enzymatic hydrolysis, and betulin from birch bark extracted by liquid CO2 containing ethanol. Inherent in these two extraction processes and production routes is the ability to show good environmental performance from a life cycle perspective. Extraction of high-value compounds also provides possibilities for innovation in the current agricultural, food and forest industry potentially leading to socio-economical benefits. (C) 2013 The Authors. Published by Elsevier Ltd. All rights reserved.
  • Gunnarsson, Lavinia Cicortas, et al. (författare)
  • Engineered xyloglucan specificity in a carbohydrate-binding module
  • 2006
  • Ingår i: Glycobiology. - : Oxford University Press. - 0959-6658 .- 1460-2423. ; 16:12, s. 1171-1180
  • Tidskriftsartikel (refereegranskat)abstract
    • The field of plant cell wall biology is constantly growing and consequently so is the need for more sensitive and specific probes for individual wall components. Xyloglucan is a key polysaccharide widely distributed in the plant kingdom in both structural and storage tissues that exist in both fucosylated and non-fucosylated variants. Presently, the only xyloglucan marker available is the monoclonal antibody CCRC-M1 that is specific to terminal alpha-1,2-linked fucosyl residues on xyloglucan oligo- and polysaccharides. As a viable alternative to searches for natural binding proteins or creation of new monoclonal antibodies, an approach to select xyloglucan-specific binding proteins from a combinatorial library of the carbohydrate-binding module, CBM4-2, from xylanase Xyn10A of Rhodothermus marinus is described. Using phage display technology in combination with a chemoenzymatic method to anchor xyloglucan to solid supports, the selection of xyloglucan-binding modules with no detectable residual wild-type xylan and beta-glucan-binding ability was achieved.
  • Turner, Charlotta, et al. (författare)
  • Subcritical water extraction and beta-glucosidase-catalyzed hydrolysis of quercetin glycosides in onion waste
  • 2006
  • Ingår i: Green Chemistry. - : Royal Society of Chemistry. - 1463-9262 .- 1463-9270. ; 8:11, s. 949-959
  • Tidskriftsartikel (refereegranskat)abstract
    • Onion waste is a renewable raw material, rich in different molecular species of the antioxidant quercetin. To utilize this resource, an environmentally sustainable procedure has been developed, using pressurized hot water to extract the quercetin species, followed by biocatalytic conversion of the quercetin glycosides to quercetin and carbohydrates. Two different recombinantly expressed thermostable beta-glucosidases, Thermotoga neapolitana beta-glucosidase A and B, were utilized as catalysts. These enzymes maintain activity at temperatures around 90 degrees C, and are therefore ideal to use in combination with hot water extraction. Our results, based on experimental design, showed that they converted quercetin glycosides to active quercetin in less than 10 min reaction time in water at 90 degrees C, pH 5.0. Experimental design showed that the optimal extraction conditions included three 5 min extraction cycles with water at 120 degrees C and 50 bars, giving a total extraction time of 15 min. Several different types of quercetin and isorhamnetin glycosides as well as kaempferol were detected in onion waste using LC-MS/MS analysis. After converting the different glycosidic compounds to their respective aglycones, the quercetin content was 10 to 50 mg g(-1) dry weight of onion waste (RSD 8%). In summary, our research demonstrates that subcritical water extraction followed by beta-glucosidase-catalyzed hydrolysis is a rapid method to determine the content of quercetin and isorhamnetin in onion samples, and is environmentally sustainable as it only uses water as solvent and enzymes as catalysts.
  • von Schantz, Laura, et al. (författare)
  • Affinity maturation generates greatly improved xyloglucan-specific carbohydrate binding modules
  • 2009
  • Ingår i: BMC Biotechnology. - : BioMed Central (BMC). - 1472-6750. ; 9
  • Tidskriftsartikel (refereegranskat)abstract
    • 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.
  • Cicortas Gunnarsson, Lavinia, et al. (författare)
  • A carbohydrate binding module as a diversity-carrying scaffold
  • 2004
  • Ingår i: Protein Engineering Design & Selection. - : Oxford University Press. - 1741-0126 .- 1741-0134. ; 17:3, s. 213-221
  • Tidskriftsartikel (refereegranskat)abstract
    • The growing field of biotechnology is in constant need of binding proteins with novel properties. Not just binding specificities and affinities but also structural stability and productivity are important characteristics for the purpose of large-scale applications. In order to find such molecules, libraries are created by diversifying naturally occurring binding proteins, which in those cases serve as scaffolds. In this study, we investigated the use of a thermostable carbohydrate binding module, CBM4-2, from a xylanase found in Rhodothermus marinus, as a diversity-carrying scaffold. A combinatorial library was created by introducing restricted variation at 12 positions in the carbohydrate binding site of the CBM4-2. Despite the small size of the library (1.6x10(6) clones), variants specific towards different carbohydrate polymers (birchwood xylan, Avicel and ivory nut mannan) as well as a glycoprotein (human IgG4) were successfully selected for, using the phage display method. Investigated clones showed a high productivity (on average 69 mg of purified protein/l shake flask culture) when produced in Escherichia coli and they were all stable molecules displaying a high melting transition temperature (75.7 +/- 5.3degreesC). All our results demonstrate that the CBM4-2 molecule is a suitable scaffold for creating variants useful in different biotechnological applications.
  • Abou Hachem, Maher, et al. (författare)
  • Carbohydrate-binding modules from a thermostable Rhodothermus marinus xylanase : Cloning, expression and binding studies
  • 2000
  • Ingår i: Biochemical Journal. - : Portland Press. - 0264-6021. ; 345:1, s. 53-60
  • Tidskriftsartikel (refereegranskat)abstract
    • The two N-terminally repeated carbohydrate-binding modules (CBM4-1 and CBM4-2) encoded by xyn10A from Rhodothermus marinus were produced in Escherichia coli and purified by affinity chromatography. Binding assays to insoluble polysaccharides showed binding to insoluble xylan and to phosphoric-acid-swollen cellulose but not to Avicel or crystalline cellulose. Binding to insoluble substrates was significantly enhanced by the presence of Na+ and Ca2+ ions. The binding affinities for soluble polysaccharides were tested by affinity electrophoresis; strong binding occurred with different xylans and β-glucan. CBM4-2 displayed a somewhat higher binding affinity than CBM4-1 for both soluble and insoluble substrates but both had similar specificities. Binding to short oligosaccharides was measured by NMR; both modules bound with similar affinities. The binding of the modules was shown to be dominated by enthalpic forces. The binding modules did not contribute with any significant synergistic effects on xylan hydrolysis when incubated with a Xyn10A catalytic module. This is the first report of family 4 CBMs with affinity for both insoluble xylan and amorphous cellulose.
  • de Maré, L, et al. (författare)
  • A cultivation technique for E. coli fed-batch cultivations operating close to the maximum oxygen transfer capacity of the reactor
  • 2005
  • Ingår i: Biotechnology Letters. - : Springer. - 0141-5492 .- 1573-6776. ; 27:14, s. 983-990
  • Tidskriftsartikel (refereegranskat)abstract
    • A cultivation strategy combining the advantages of temperature-limited fed-batch and probing feeding control is presented. The technique was evaluated in fed-batch cultivations with E. coli BL21(DE3) producing xylanase in a 3 liter bioreactor. A 20% increase in cell mass was achieved and the usual decrease in specific enzyme activity normally observed during the late production phase was diminished with the new technique. The method was further tested by growing E. coli W3110 in a larger bioreactor (50 l). It is a suitable cultivation technique when the O2 transfer capacity of the reactor is reached and it is desired to continue to produce the recombinant protein.
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