| 1. |
- Bohlin, Christina, et al.
(författare)
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Product profiles in enzymic and non-enzymic oxidations of the lignin model compound erythro-1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)-1,3-propanediol
- 2005
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Ingår i: Journal of Molecular Catalysis - B Enzymatic. - : Elsevier BV. - 1381-1177 .- 1873-3158. ; 35:4-6, s. 100-107
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Tidskriftsartikel (refereegranskat)abstract
- The erythro form of the lignin model compound 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)-1,3-propanediol (1) was oxidized with laccase/ABTS, lead(IV) tetraacetate (LTA), lignin peroxidase/H2O2, cerium(IV) ammonium nitrate (CAN) and Fenton's reagent. The product profiles obtained with the different oxidants were compared after separation, identification and quantification of the products using HPLC, UV-diode array detector and electrospray ionization mass spectrometry in positive ionization mode. The oxidants generated different product profiles that reflected their different properties. Oxidation with laccase/ABTS resulted almost exclusively in formation of 1-(3,4-dimethoxyphenyl)-3-hydroxy-2-(2-methoxyphenoxy)-1-propanone (2). Oxidation with LTA resulted in more 3,4-dimethoxybenzaldehyde (3) than ketone 2. Lignin peroxidase and CAN gave similar product profiles and aldehyde 3 was the predominant product (only small amounts of ketone 2 were formed). Oxidation with Fenton's reagent resulted in the formation of more aldehyde 3 than ketone 2 but the yields were very low. CAN served as an excellent model for the lignin peroxidase-catalyzed oxidation, while the laccase-mediator system, LTA and Fenton's reagent provided distinctly different product profiles. Erythro-1-(3,4-dimethoxyphenyl)-1,2,3-propanetriol was present among the products obtained on oxidation with LTA, lignin peroxidase, CAN and Fenton's reagent. The differences in redox potential between the oxidants afford an explanation of the diverse product patterns but other factors may also be of importance. The reactions leading to cleavage of the β-ether bond with formation of 1-(3,4-dimethoxyphenyl)-1,2,3-propanetriol (veratrylglycerol) were found to proceed without affecting the configuration at the β-carbon atom.
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| 2. |
- Tkac, Jan, et al.
(författare)
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Improved selectivity of microbial biosensor using membrane coating. Application to the analysis of ethanol during fermentation
- 2003
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Ingår i: Biosensors & bioelectronics. - 0956-5663 .- 1873-4235. ; 18:9, s. 1125-1134
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Tidskriftsartikel (refereegranskat)abstract
- A ferricyanide mediated microbial biosensor for ethanol detection was prepared by surface modification of a glassy carbon electrode. The selectivity of the whole Gluconobacter oxydans cell biosensor for ethanol determination was greatly enhanced by the size exclusion effect of a cellulose acetate (CA) membrane. The use of a CA membrane increased the ethanol to glucose sensitivity ratio by a factor of 58.2 and even the ethanol to glycerol sensitivity ratio by a factor of 7.5 compared with the use of a dialysis membrane. The biosensor provides rapid and sensitive detection of ethanol with a limit of detection of 0.85 µM (S/N=3). The selectivity of the biosensor toward alcohols was better compared to previously published enzyme biosensors based on alcohol oxidase or alcohol dehydrogenases. The biosensor was successfully used in an off-line monitoring of ethanol during batch fermentation by immobilized Saccharomyces cerevisiae cells with an initial glucose concentration of 200 g l-1. © 2002 Elsevier Science B.V. All rights reserved.
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| 3. |
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| 4. |
- Bjelosevic, Haris, et al.
(författare)
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Synthesis and structural characterisation of novel platinum-based drug candidates with extended functionality by incorporation of bis(diphenylphosphino)ferrocene units as metal chelators
- 2006
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Ingår i: Tetrahedron. - : Elsevier BV. - 0040-4020. ; 62:18, s. 4519-4527
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Tidskriftsartikel (refereegranskat)abstract
- Among the metal-based anticancer drugs, cisplatin (cis-diaminedichloroplatinum(II)) is the most widely used species in therapy. Despite its clinical success, cisplatin still suffers in generating resistance, as well as being highly toxic due to poor selectivity between healthy and sick cells. By molecular design it ought to be possible to generate new cis-platinum compounds with increased selectivity and improved cellular behaviour. In this paper, we report a synthetic pathway for construction of derivatives of 1,1'-bis(diphenylphosphino)-ferrocene, together with their corresponding cis-platinum compounds with the aim testing them for their interaction capacity with respect to various DNA models. We also report a synthetic route for a nucleoside-based cis-platinum compound containing a bidentate ferrocenylphosphine derivative connected through a succinamic-based linker to the 5-position of the heterocyclic moiety of uridine. Our preliminary kinetic investigation of 5-{N-[1-[1',2-bis(diphenylphosphino)ferrocenyl]ethyl]1-N'-[prop-2-yn-3-y l]succinamide} uridinedichloroplatinum(II) showed that this compound reacted faster with the phosphorothioate containing oligonucleotides d(T(6)p(S)T-6), with an observed first-order rate constant k(obs) = (1.4 +/- 0.1) X 10(-4) s(-1), compared with the G-N7 target in d(T(7)GGT(7)), for which the observed first-order rate constant is k(obs) = (7.2 +/- 0.5) X 10(-4) s(-1). (c) 2006 Elsevier Ltd. All rights reserved.
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| 5. |
- Shleev, Sergey, et al.
(författare)
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Interaction of fungal laccases and laccase-mediator systems with lignin
- 2006
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Ingår i: Enzyme and Microbial Technology. - : Elsevier BV. - 0141-0229 .- 1879-0909. ; 39:4, s. 841-847
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Tidskriftsartikel (refereegranskat)abstract
- The interaction between fungal laccases from Trametes basidiomycetes and different lignins has been studied using electrochemical and chromatographic methods. The kinetic parameters for the oxidation reaction of hydroquinone and for Kraft lignin by molecular oxygen catalysed by Trametes hirsuta laccase have been investigated. Polymerisation of lignin by laccase was shown. The process was independent on the source of lignin as well as on the origin and purity of the enzymes. A complex pattern of interaction between the laccase-mediator system (LMS) and lignin was shown. Along with the polymerisation of lignin, the ability to degrade lignin using the LMS was observed. Data generated by combining size exclusion chromatographic separation of lignin with the use of a laccase modified electrode as post column detector, strongly suggest that laccase can oxidise natural lignin by a long-range electron transfer mechanism. The influence of the origin of lignin as well as source of the enzyme on this process was also shown. (c) 2006 Elsevier Inc. All rights reserved.
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| 6. |
- Tasca, Federico, et al.
(författare)
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Increasing amperometric biosensor sensitivity by length fractionated single-walled carbon nanotubes.
- 2008
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Ingår i: Biosensors & Bioelectronics. - : Elsevier BV. - 1873-4235 .- 0956-5663. ; 24:2, s. 272-278
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Tidskriftsartikel (refereegranskat)abstract
- In this work the sensitivity-increasing effect of single-walled carbon nanotubes (SWCNTs) in amperometric biosensors, depending on their average length distribution, was studied. For this purpose the SWCNTs were oxidatively shortened and subsequently length separated by size exclusion chromatography. Transmission electron micrographs of different fractions of SWCNTs were collected. Diaphorase "wired" to an osmium redox polymer was blended with the shortened SWCNTs of different lengths. Depending on the average length of the SWCNTs the sensitivity of the amperometric biosensor model system towards oxidation of 1,4-dihydronicotinamide adenine dinucleotide (NADH) was increased by a factor of five. The best performance was achieved with SWCNTs of medium length. The linear range for NADH detection was between 5muM and 7mM, the maximum sensitivity was 47nAmuM(-1)cm(-2), and the detection limit was 1muM. The biosensor exhibited excellent electrocatalytic properties. Even at relatively high NADH concentrations the oxidative current was limited by the diffusion rate of NADH.
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| 7. |
- Tuoriniemi, Jani, 1982, et al.
(författare)
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Determination of the Distance Between the Cytochrome and Dehydrogenase Domains of Immobilized Cellobiose Dehydrogenase by Using Surface Plasmon Resonance with a Center of Mass Based Model
- 2020
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Ingår i: Analytical Chemistry. - : American Chemical Society (ACS). - 0003-2700 .- 1520-6882. ; 92:3, s. 2620-2627
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Tidskriftsartikel (refereegranskat)abstract
- Changes in the tertiary conformation of adsorbed biomolecules can induce detectable shifts (Delta theta(r)) in the surface plasmon resonance (SPR) angle. Here it is shown how to calculate the corresponding shifts in the adsorbate's center of mass (Delta z(avg)) along the sensing surface normal from the measured Delta theta(r). The novel developed model was used for determining the mean distance between the cytochrome (CYT) and flavodehydrogenase (DH) domains of the enzyme cellobiose dehydrogenase (CDH) isolated from the fungi Neurospora crassa, Corynascus thermophilus, and Myriococcum thermophilum as a function of pH, [Ca2+], and substrate concentration. SPR confirmed the results from earlier electrochemical and SAXS studies stating that the closed conformation, where the two domains are in close vicinity, is stabilized by a lower pH and an increased [Ca2+]. Interestingly, an increasing substrate concentration in the absence of any electron acceptors stabilizes the open conformation as the electrostatic repulsion due to the reaped electrons pushes the DH and CYT domains apart. The accuracy of distance determination was limited mostly by the random fluctuations between replicate measurements, and it was possible to detect movements <1 nm of the domains with respect to each other. The results agreed with calculations using already established models treating conformational changes as contraction or expansion of the thickness of the adsorbate layer (t(protein)). Although the models yielded equivalent results, in this case, the Delta z(avg)-based method also works in situations, where the adsorbate's mass is not evenly distributed within the layer.
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| 8. |
- Bunea, Ada-Ioana, et al.
(författare)
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Micropatterned Carbon-on-Quartz Electrode Chips for Photocurrent Generation from Thylakoid Membranes
- 2018
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Ingår i: ACS Applied Energy Materials. - : American Chemical Society (ACS). - 2574-0962. ; 1:7, s. 3313-3322
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Tidskriftsartikel (refereegranskat)abstract
- Harvesting the energy generated by photosynthetic organisms through light-dependent reactions is a significant step toward a sustainable future energy supply. Thylakoid membranes are the site of photosynthesis, and thus particularly suited for developing photo-bioelectrochemical cells. Novel electrode materials and geometries could potentially improve the efficiency of energy harvesting using thylakoid membranes. For commercial applications, electrodes with large surface areas are needed. Photolithographic patterning of a photoresist, followed by pyrolysis, is a flexible and fast approach for the fabrication of carbon electrodes with tailored properties. In this work, electrode chips consisting of patterned carbon supported on quartz were designed and fabricated. The patterned electrode area is 1 cm2, and the measurement chamber footprint is 0.5 cm2, 1 order of magnitude larger than previously tested electrodes for thylakoid membrane immobilization. The use of a transparent substrate allows back-side illumination, protecting the bioelectrochemical system from the environment and vice versa. Two different mediators, monomeric ([Ru(NH3)6]3+) and polymeric ([Os(2,2′-bipyridine)2-poly(N-vinylimidazole)10Cl]+/2+), are used for evaluating photocurrent generation from thylakoid membranes with different electrode geometries. Current densities up to 71 μA cm–2 are measured upon illumination through the transparent electrode chip with solar simulated irradiance (1000 W m–2).
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| 9. |
- Spadiut, Oliver, et al.
(författare)
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Engineered Pyranose 2-Oxidase : Efficiently Turning Sugars into Electrical Energy
- 2010
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Ingår i: Electroanalysis. - : Wiley. - 1040-0397 .- 1521-4109. ; 22:7-8, s. 813-820
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Tidskriftsartikel (refereegranskat)abstract
- Due to the recent interest in enzymatic biofuel cells (BECs), sugar oxidizing enzymes other than the commonly used glucose oxidase are gaining more importance as possible bioelements of implantable microscale-devices, which can, for example, be used in biosensors and pacemakers. In this study we used rational and semi-rational protein design to improve the catalytic activity of the enzyme pyranose 2-oxidase (P2Ox) with its alternative soluble electron acceptors 1,4-benzoquinone and ferricenium ion, which can serve as electron mediators, to possibly boost the power output of enzymatic BECs. Using a screening assay based on 96-well plates, we identified the variant H450G, which showed lower K-M and higher k(cat) values for both 1,4-benzoquinone and ferricenium ion compared to the wild-type enzyme, when either D-glucose or D-galactose were used as saturating electron donors. Besides this variant, we analyzed the variants V546C and T169G/V546C for their possible application in enzymatic BECs. The results obtained in homogeneous solution were compared with those obtained when P2Ox was immobilized on the surface of graphite electrodes and either "wired" to an osmium redox polymer or using soluble 1,4-benzoquinone as mediator. According to the spectrophotometrically determined kinetic constants, the possible energy output, measured in flow injection analysis experiments with these variants, increased up to 4-fold compared to systems employing the wild-type enzyme. Our results show that by increasing the catalytic activity of the redox enzyme P2Ox with its alternative electron acceptors 1,4-benzoquinone and ferricenium ion, it is possible to achieve a higher energy output of an enzymatic BFC when using the same concentration of sugar substrate.
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| 10. |
- Abad, JM, et al.
(författare)
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Immobilization of peroxidase glycoprotein on gold electrodes modified with mixed epoxy-boronic acid monolayers
- 2002
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Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 1520-5126 .- 0002-7863. ; 124:43, s. 12845-12853
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Forskningsöversikt (refereegranskat)abstract
- The development of bioelectronic enzyme applications requires the immobilization of active proteins onto solid or colloidal substrates such as gold. Coverage of the gold surface with alkanethiol self-assembled monolayers (SAMS) reduces nonspecific adsorption of proteins and also allows the incorporation onto the surface of ligands with affinity for complementary binding sites on native proteins. We present in this work a strategy for the covalent immobilization of glycosylated proteins previously adsorbed through weak, reversible interactions, on tailored SAMS. Boronic acids, which form cyclic esters with saccharides, are incorporated into SAMS to weakly adsorb the glycoprotein onto the electrode surface through their carbohydrate moiety. To prevent protein release from the electrode surface, we combine the affinity motif of boronates with the reactivity of epoxy groups to covalently link the protein to heterofunctional boronateepoxy SAMS. The principle underlying our strategy is the increased immobilization rate achieved by the weak interaction-induced proximity effect between slow reacting oxyrane groups in the SAM and nucleophilic residues from adsorbed proteins, which allows the formation of very stable covalent bonds. This approach is exemplified by the use of phenylboronates-oxyrane mixed monolayers as a reactive support and redox-enzyme horseradish peroxidase as glycoprotein for the preparation of peroxidase electrodes. Quartz crystal microbalance, atomic force microscopy, and electrochemical measurements are used to characterize these enzymatic electrodes. These epoxy-boronate functional monolayers; are versatile, stable interfaces, ready to incorporate glycoproteins by incubation under mild conditions.
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