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Sökning: hsv:(NATURVETENSKAP) hsv:(Biologi) > Tjerneld Folke

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1.
  • Fexby, Sara, et al. (författare)
  • Partitioning and characterization of tyrosine-tagged green fluorescent proteins in aqueous two-phase systems
  • 2004
  • Ingår i: Biotechnology Progress. - : Wiley. - 1520-6033 .- 8756-7938. ; 20:3, s. 793-798
  • Tidskriftsartikel (refereegranskat)abstract
    • The green fluorescent protein GFPuv has been genetically engineered to investigate the influence of N-terminal tyrosine extensions in aqueous two-phase systems. Fusions in the N-terminus affected the protein expression, and tags containing three tyrosines and prolines influenced the expression favorably. This effect is probably due to changes in mRNA stability, because the amounts of corresponding mRNAs correlated with the amounts of GFPuv proteins. The partitioning was investigated in two different aqueous two-phase systems, a two-polymer system composed of EO30PO70/dextran and a PEG/salt system with potassium phosphate. Partitioning in the PEG/salt system generally was more favorable than in the EO30PO70/dextran system. Tags with three tyrosines resulted in higher partitioning toward the EO30PO70- and PEG-rich phases, respectively. The effect of adding proline residues to the tag was also investigated, and the partitioning effect of the tag was enhanced when prolines were included in the tags with three tyrosines. The best tyrosine tag, Y3P2, increased the partition coefficient 5 times in the PEG/salt system. Thermoseparation of the EO30PO70 phase allowed recovery of 83% Y3P2-GFPuv protein in a water phase.
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2.
  • Börjesson, Johan, et al. (författare)
  • Effect of poly(ethylene glycol) on enzymatic hydrolysis and adsorption of cellulase enzymes to pretreated lignocellulose
  • 2007
  • Ingår i: Enzyme and Microbial Technology. - : Elsevier BV. - 0141-0229. ; 41:1-2, s. 186-195
  • Tidskriftsartikel (refereegranskat)abstract
    • There is a need to develop the enzymatic hydrolysis of cellulose for production of ethanol from biomass. In recent years the inhibitory effects of lignin in lignocellulosic substrates has been the focus of several studies. This points to the importance of understanding the interactions between cellulose degrading enzymes and lignin. Surface active substances have been shown to adsorb to lignin surfaces resulting in reduction of unproductive enzyme binding. It is essential to understand the surface properties of both enzymes and lignin to develop pretreatment methods, surface active additives and engineering of cellulose degrading enzyme systems. This study investigates the PEG-lignin interaction as well as interactions between lignin and the enzyme modules of the Hypocrea jecorina (Trichoderma reesei) enzymes Cel7A and Cel7B. Interactions were monitored with C-14 labelled PEG 4000 and by measuring the enzymatic activity in solution. It was found that the dominating driving force of PEG adsorption on lignin is hydrophobic interaction. The effect of PEG addition on enzyme conversion of lignocellulose increased with higher temperature due to increased adsorption of PEG on lignin, thus resulting in a higher surface density of PEG on the surface. The hydrophobic adsorption of enzymes to lignin induces denaturation of enzymes on lignin surfaces. The addition of PEG to the enzyme hydrolysis at a temperature of 50 degrees C is suggested to hinder deactivation of enzymes by exclusion of enzymes from lignin surfaces. The adsorption of full-length Cel7B to lignin was stronger than for Cel7A. A more hydrophobic surface on the flat face of the cellulose binding module (CBM) together with an additional exposed aromatic residue on the rough face of Cel7B CBM compared to Cel7A CBM gives a higher affinity to lignin for the Cel7B enzyme. (c) 2007 Elsevier Inc. All rights reserved.
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3.
  • Eriksson, Torny, et al. (författare)
  • Heterogeneity of homologously expressed Hypocrea jecorina (Trichoderma reesei) Cel7B catalytic module
  • 2004
  • Ingår i: European Journal of Biochemistry. - : Wiley. - 0014-2956 .- 1432-1033. ; 271:7, s. 1266-1276
  • Tidskriftsartikel (refereegranskat)abstract
    • The catalytic module of Hypocrea jecorina (previously Trichoderma reesei) Cel7B was homologously expressed by transformation of strain QM9414. Post-translational modifications in purified Cel7B preparations were analysed by enzymatic digestions, high performance chromatography, mass spectrometry and site-directed mutagenesis. Of the five potential sites found in the wild-type enzyme, only Asn56 and Asn182 were found to be N-glycosylated. GlcNAc(2)Man(5) was identified as the predominant N-glycan, although lesser amounts of GlcNAc(2)Man(7) and glycans carrying a mannophosphodiester bond were also detected. Repartition of neutral and charged glycan structures over the two glycosylation sites mainly accounts for the observed microheterogeneity of the protein. However, partial deamidation of Asn259 and a partially occupied O-glycosylation site give rise to further complexity in enzyme preparations.
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4.
  • Johansson, Hans-Olof, et al. (författare)
  • Plasmid DNA partitioning and separation using poly(ethylene glycol)/poly(acrylate)/salt aqueous two-phase systems.
  • 2012
  • Ingår i: Journal of Chromatography A. - : Elsevier BV. - 0021-9673. ; 1233, s. 30-35
  • Tidskriftsartikel (refereegranskat)abstract
    • Phase diagrams of poly(ethylene glycol)/polyacrylate/Na(2)SO(4) systems have been investigated with respect to polymer size and pH. Plasmid DNA from Escherichia coli can depending on pH and polymer molecular weight be directed to a poly(ethylene glycol) or to a polyacrylate-rich phase in an aqueous two-phase system formed by these polymers. Bovine serum albumin (BSA) and E. coli homogenate proteins can be directed opposite to the plasmid partitioning in these systems. Two bioseparation processes have been developed where in the final step the pDNA is partitioned to a salt-rich phase giving a total process yield of 60-70%. In one of them the pDNA is partitioned between the polyacrylate and PEG-phases in order to remove proteins. In a more simplified process the plasmid is partitioned to a PEG-phase and back-extracted into a Na(2)SO(4)-rich phase. The novel polyacrylate/PEG system allows a strong change of the partitioning between the phases with relatively small changes in composition or pH.
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5.
  • Kepka, Cecilia, et al. (författare)
  • Extraction of plasmid DNA from Escherichia coli cell lysate in a thermoseparating aqueous two-phase system
  • 2004
  • Ingår i: Journal of Chromatography A. - : Elsevier BV. - 0021-9673. ; 1024:1-2, s. 95-104
  • Tidskriftsartikel (refereegranskat)abstract
    • The primary purification of a 6.1kilo base pair (kbp) plasmid from a desalted alkaline lysate has been accomplished by a thermoseparating aqueous two-phase system [(50% ethylene oxide-50% propylene oxide)-Dextran T 500]. The partitioning of the different nucleic acids (plasmid DNA, RNA, genomic DNA) in the thermoseparating aqueous two-phase system was followed both qualitatively by agarose gel electrophoresis and quantitatively by analytical chromatography (size exclusion- and anion-exchange mode) and PicoGreen fluorescence analysis. The experimental results showed a complete recovery of the plasmid DNA to the top phase, while 80% of total RNA and 58% of total protein was discarded to the bottom phase. Moreover, a 3.8-fold volume reduction of the plasmid DNA solution was achieved. By using a final thermoseparating step, the EO50PO50 polymer could be efficiently recycled, resulting in plasmid solution containing less than 1% polymer. The developed thermoseparating aqueous two-phase system shows great potential for the large-scale processing of plasmid DNA.
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6.
  • Ademark, Pia, et al. (författare)
  • Hydrolytic properties of a beta-mannosidase purified from Aspergillus niger. J. Biotechnol. 75: 281-289.
  • 1999
  • Ingår i: Journal of Biotechnology. - 1873-4863. ; 75:2-3, s. 281-289
  • Tidskriftsartikel (refereegranskat)abstract
    • A β-mannosidase was purified to homogeneity from the culture filtrate of Aspergillus niger. A specific activity of 500 nkat mg−1 and a 53-fold purification was achieved using ammonium sulfate precipitation, anion-exchange chromatography, and gel filtration. The isolated enzyme has an isoelectric point of 5.0 and appears to be a dimer composed of two 135-kDa subunits. It is a glycoprotein and contains 17% N-linked carbohydrate by weight. Maximal activity was observed at pH 2.4–5.0 and at 70°C. The β-mannosidase hydrolyzed β-1,4-linked manno-oligosaccharides of degree of polymerization (DP) 2–6 and also released mannose from polymeric ivory nut mannan and galactomannan. The Km and Vmax values for p-nitrophenyl-β-Image-mannopyranoside were 0.30 mM and 500 nkat mg−1, respectively. Hydrolysis of Image-galactose substituted manno-oligosaccharides showed that the β-mannosidase was able to cleave up to, but not beyond, a side group. An internal peptide sequence of 15 amino acids was highly similar to that of an Aspergillus aculeatus β-mannosidase belonging to family 2 of glycosyl hydrolases.
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7.
  • Ademark, Pia, et al. (författare)
  • Multiple alpha-galactosidases from Aspergillus niger: purification, characterization, and substrate specificities
  • 2001
  • Ingår i: Enzyme and Microbial Technology. - 0141-0229. ; 29:6-7, s. 441-448
  • Tidskriftsartikel (refereegranskat)abstract
    • Enzymes with α-galactosidase activity are produced by many organisms, often in multiple forms. Here we compare the biochemical and hydrolytic properties of four major α-galactosidase forms (α-gal I-IV) that were purified from the culture filtrate of Aspergillus niger. α-Gal II, III and IV appear to be isoforms of the same enzyme, and N-terminal amino acid sequence data suggest that they are closely related or identical to A. niger AglB in family 27 of the glycosyl hydrolases. α-Gal I is a completely different enzyme that belongs to family 36. α-Gal I had an isoelectric point of 4.15 and appears to be a tetramer composed of four 94-kDa subunits. α-Gal II, III and IV were dimers with monomeric molecular masses of 64 kDa and isoelectric points of 4.5, 4.7 and 4.8, respectively. α-Gal II-IV were stable when incubated for 17 h at 50°C and pH 2–5, whereas α-gal I was most stable at pH 5–6. All enzymes had maximal catalytic activity at pH 4.5 and 60°C, and hydrolyzed melibiose, raffinose and stachyose. α-Gal II-IV also degraded galactomanno-oligosaccharides and released 66% of the galactose side groups from polymeric locust bean gum galactomannan. α-Gal I released galactose from locust bean gum only in combination with A. niger β-mannosidase. Kinetic experiments showed that α-gal I hydrolyzed p-nitrophenyl-α-Image-galactopyranoside and melibiose more efficiently than α-gal II-IV. The distinct hydrolytic and biochemical properties of α-gal I and α-gal II-IV further signifies the difference between α-galactosidases of family 27 and 36.
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8.
  • Ademark, Pia, et al. (författare)
  • Softwood hemicellulose-degrading enzymes from Aspergillus niger: Purification and properties of a β-mannanase
  • 1998
  • Ingår i: Journal of Biotechnology. - 1873-4863. ; 63:3, s. 199-210
  • Tidskriftsartikel (refereegranskat)abstract
    • The enzymes needed for galactomannan hydrolysis, i.e. β-mannanase, α-galactosidase and β-mannosidase, were produced by the filamentous fungus Aspergillus niger. The β-mannanase was purified to electrophoretic homogeneity in three steps using ammonium sulfate precipitation, anion-exchange chromatography and gel filtration. The purified enzyme had an isoelectric point of 3.7 and a molecular mass of 40 kDa. Ivory nut mannan was degraded mainly to mannobiose and mannotriose when incubated with the β-mannanase. Analysis by 1H NMR spectroscopy during hydrolysis of mannopentaose showed that the enzyme acts by the retaining mechanism. The N-terminus of the purified A. niger β-mannanase was sequenced by Edman degradation, and comparison with Aspergillus aculeatus β-mannanase indicated high identity. The enzyme most probably lacks a cellulose binding domain since it was unable to adsorb on cellulose.
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9.
  • Alkasrawi, Malek, et al. (författare)
  • The effect of Tween-20 on simultaneous saccharification and fermentation of softwood to ethanol
  • 2003
  • Ingår i: Enzyme and Microbial Technology. - 0141-0229. ; 33:1, s. 71-78
  • Tidskriftsartikel (refereegranskat)abstract
    • Simultaneous sacchatification and fermentation (SSF) of steam-pretreated wood constitutes an attractive process configuration for ethanol production from biomass. However, the high enzyme addition in SSF contributes to a high process cost. In this study we explore the effect of the non-ionic surfactant Tween-20 as an additive in SSE Tween-20 addition at 2.5 g/l had several positive effects on SSF: (i) the ethanol yield was increased by 8%; (ii) the amount of enzyme loading could be reduced by 50%, while maintaining a constant yield; (iii) the enzyme activity increased in the liquid fraction at the end of SSF, probably by preventing unproductive binding of the cellulases to lignin, which could facilitate enzyme recovery; (iv) the time required to attain maximum ethanol concentration was reduced. Surfactants as an additive in SSF can significantly lower the operational cost of the process. However, less expensive surfactants must be investigated. (C) 2003 Elsevier Science Inc. All rights reserved.
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10.
  • Antov, Mirjana, et al. (författare)
  • Affinity partitioning of a Cellulomonas fimi beta-mannanase with a mannan-binding module in galactomannan/starch aqueous two-phase system
  • 2006
  • Ingår i: Journal of Chromatography A. - : Elsevier BV. - 0021-9673. ; 1123:1, s. 53-59
  • Tidskriftsartikel (refereegranskat)abstract
    • A new approach in affinity separations was studied by partitioning of Cellulomonas fimi beta-mannanase (EC 3.2.1.78) containing a mannan-binding module in galactomannan/hydroxypropyl starch aqueous two-phase system. Comparison was made with a truncated version of C. fimi beta-mannanase which lacked the mannan-binding module. Results showed that affinity partitioning of the beta-mannanase was achieved due to biospecificity of the mannan-binding module towards the top phase containing galactomannan. Experiments were conducted at pH 8 to prevent enzyme degradation of the phase containing galactomannan. Removal of the top phase polymer was accomplished by beta-mannanase degradation allowed by shifting to the optimal pH 6. In the combination with the genetic fusion of any given protein to the mannan-binding module, the results envision a general procedure for primary affinity recovery of such fusion proteins.
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