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Hydrophobic Substrates (hydrophobic + substrate)
Selected AbstractsThree Phase Microemulsion/Sol,Gel System for Aqueous C,C Coupling of Hydrophobic SubstratesEUROPEAN JOURNAL OF ORGANIC CHEMISTRY, Issue 14 2008Dmitry Tsvelikhovsky Abstract Heck, Stille, Suzuki and three-component coupling reactions with hydrophobic substrates have been carried out in water. The substrates are initially transformed by a general procedure into a microemulsion, which consists of nearly 90,% water with the aid of sodium dodecyl sulfate and either PrOH or BuOH. The surfactant carries the molecules of the substrates to Pd(OAc)2 entrapped within a hydrophobicitized silica sol,gel matrix where the coupling between the substrates is assumed to take place. The products are then returned by the surfactant into the microemulsion from which it can be released. The immobilized palladium catalyst is leach proof and recyclable. It can be used in various coupling processes at least six times without loss of activity. Experiments with D2O have revealed that the water does not take part in the coupling process, but it has an effect on the pore size of the sol,gel matrix, which hosts the palladium catalyst. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2008) [source] ChemInform Abstract: A Novel and Efficient Methodology for the C,C Bond Forming Radical Cyclization of Hydrophobic Substrates in Water.CHEMINFORM, Issue 32 2001Yasuyuki Kita Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a "Full Text" option. The original article is trackable via the "References" option. [source] Fibrinogen Patterns and Activity on Substrates with Tailored Hydroxy DensityMACROMOLECULAR BIOSCIENCE, Issue 8 2009José Carlos Rodríguez Hernández Abstract The influence of the surface fraction of OH groups on fibrinogen (FG) adsorption is investigated in copolymers of ethyl acrylate and hydroxy ethylacrylate. The amount of adsorbed FG, quantified by western-blotting combined with image analysis of the corresponding bands, decreases as the hydrophilicity of the substrate increases. The influence of substrate wettability on FG conformation and distribution is observed by atomic force microscopy (AFM). The most hydrophobic substrate promotes FG fibrillogenesis, which leads to a fibrin-like appearance in the absence of any thrombin. The degree of FG interconnection was quantified by calculating the fractal dimension of the adsorbed protein from image analysis of the AFM results. The biological activity of the adsorbed FG is correlated to cell adhesion on FG-coated substrates. [source] Three Phase Microemulsion/Sol,Gel System for Aqueous C,C Coupling of Hydrophobic SubstratesEUROPEAN JOURNAL OF ORGANIC CHEMISTRY, Issue 14 2008Dmitry Tsvelikhovsky Abstract Heck, Stille, Suzuki and three-component coupling reactions with hydrophobic substrates have been carried out in water. The substrates are initially transformed by a general procedure into a microemulsion, which consists of nearly 90,% water with the aid of sodium dodecyl sulfate and either PrOH or BuOH. The surfactant carries the molecules of the substrates to Pd(OAc)2 entrapped within a hydrophobicitized silica sol,gel matrix where the coupling between the substrates is assumed to take place. The products are then returned by the surfactant into the microemulsion from which it can be released. The immobilized palladium catalyst is leach proof and recyclable. It can be used in various coupling processes at least six times without loss of activity. Experiments with D2O have revealed that the water does not take part in the coupling process, but it has an effect on the pore size of the sol,gel matrix, which hosts the palladium catalyst. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2008) [source] SOA genes encode proteins controlling lipase expression in response to triacylglycerol utilization in the yeast Yarrowia lipolyticaFEMS YEAST RESEARCH, Issue 1 2010Thomas Desfougčres Abstract The oleaginous yeast Yarrowia lipolytica efficiently metabolizes hydrophobic substrates such as alkanes, fatty acids or triacylglycerol. This yeast has been identified in oil-polluted water and in lipid-rich food. The enzymes involved in lipid breakdown, for use as a carbon source, are known, but the molecular mechanisms controlling the expression of the genes encoding these enzymes are still poorly understood. The study of mRNAs obtained from cells grown on oleic acid identified a new group of genes called SOA genes (specific for oleic acid). SOA1 and SOA2 are two small genes coding for proteins with no known homologs. Single- and double-disrupted strains were constructed. Wild-type and mutant strains were grown on dextrose, oleic acid and triacylglycerols. The double mutant presents a clear phenotype consisting of a growth defect on tributyrin and triolein, but not on dextrose or oleic acid media. Lipase activity was 50-fold lower in this mutant than in the wild-type strain. The impact of SOA deletion on the expression of the main extracellular lipase gene (LIP2) was monitored using a LIP2 -,-galactosidase promoter fusion protein. These data suggest that Soa proteins are components of a molecular mechanism controlling lipase gene expression in response to extracellular triacylglycerol. [source] A gemini amphiphilic phase transfer catalyst for dark singlet oxygenationJOURNAL OF PHYSICAL ORGANIC CHEMISTRY, Issue 7-8 2008Cédric Borde Abstract A new gemini surfactant phase transfer catalyst, namely diethyl-ether-,,,-bis-(dimethyldodecylammonium molybdate) codified as 12-EO-12-Mo, was prepared by anion exchange from the analogous gemini dichloride (12-EO-12-Cl2). The physico-chemical properties of these compounds such as Krafft temperature, critical micelle concentration, surface activity and binary water-surfactant behavior were compared and the influence of the molybdate counterion was examined. Though both compounds are highly hydrophilic, the cmc of 12-EO-12-Mo (0.4,mmol L,1) is about five times lower than of its dichloride analogue (2.2,mmol L,1). Moreover, 12-EO-12-Mo exhibits an additional cubic liquid crystal phase between 53 and 64,wt%. The usefulness of 12-EO-12-Mo as an amphiphilic phase transfer catalyst for the dark singlet oxygenation was demonstrated with the peroxidation of two typical organic substrates: ,-terpinene which reacts with 1O2 according to a [4,+,2] cycloaddition and the less reactive ,-citronellol, which provides two hydroperoxides according to the ene-reaction. 12-EO-12-Mo provides a simple reaction medium with only three components for the preparative peroxidation of hydrophobic substrates by chemically generated singlet oxygen. Copyright © 2008 John Wiley & Sons, Ltd. [source] Novel dimer structure of a membrane-bound protease with a catalytic Ser,Lys dyad and its linkage to stomatinJOURNAL OF SYNCHROTRON RADIATION, Issue 3 2008Hideshi Yokoyama Membrane-bound proteases are involved in various regulatory functions. A previous report indicates that the N-terminal region of PH1510 (1510-N) from the hyperthermophilic archaeon Pyrococcus horikoshii is a serine protease with a catalytic Ser,Lys dyad (Ser97 and Lys138), and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511. According to the crystal structure of the wild-type 1510-N in dimeric form, the active site around Ser97 is in a hydrophobic environment suitable for the hydrophobic substrates. This article reports the crystal structure of the K138A mutant of 1510-N at 2.3,Ĺ resolution. The determined structure contains one molecule per asymmetric unit, but 1510-N is active in dimeric form. Two possible sets of dimer were found from the symmetry-related molecules. One dimer is almost the same as the wild-type 1510-N. Another dimer is probably in an inactive form. The L2 loop, which is disordered in the wild-type structure, is significantly kinked at around A-138 in the K138A mutant. Thus Lys138 probably has an important role on the conformation of L2. [source] On-chip solid-phase extraction pre-concentration/focusing substrates coupled to atmospheric pressure matrix-assisted laser desorption/ionization ion trap mass spectrometry for high sensitivity biomolecule analysisRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 4 2009Arti Navare Atmospheric pressure matrix-assisted laser desorption/ionization (AP-MALDI) has proven a convenient and rapid method for ion production in the mass spectrometric (MS) analysis of biomolecules. AP-MALDI and electrospray ionization (ESI) sources are easily interchangeable in most mass spectrometers. However, AP-MALDI suffers from less-than-optimal sensitivity due to ion losses during transport from the atmosphere into the vacuum of the mass spectrometer. Here, we study the signal-to-noise ratio (S/N) gains observed when an on-chip dynamic pre-concentration/focusing approach is coupled to AP-MALDI for the MS analysis of neuropeptides and protein digests. It was found that, in comparison with conventional AP-MALDI targets, focusing targets showed (1) a sensitivity enhancement of approximately two orders of magnitude with S/N gains of 200,900 for hydrophobic substrates, and 150,400 for weak cation-exchange (WCX) substrates; (2) improved detection limits as low as 5,fmol/µL for standard peptides; (3) significantly reduced matrix background; and (4) higher inter-day reproducibility. The improved sensitivity allowed successful tandem mass spectrometric (MS/MS) sequencing of dilute solutions of a derivatized tryptic digest of a protein standard, and enabled the first reported AP-MALDI MS detection of neuropeptides from Aedes aegypti mosquito heads. Copyright © 2009 John Wiley & Sons, Ltd. [source] Degradation of xenobiotics in a partitioning bioreactor in which the partitioning phase is a polymerBIOTECHNOLOGY & BIOENGINEERING, Issue 4 2003Brian G. Amsden Abstract Two-phase partitioning bioreactors (TPPBs) are characterized by a cell-containing aqueous phase and a second immiscible phase that contains toxic and/or hydrophobic substrates that partition to the cells at subinhibitory levels in response to the metabolic demand of the organisms. To date, the delivery phase in TPPBs has been a hydrophobic solvent that traditionally needed to possess a variety of important properties including biocompatibility, nonbioavailability, low volatility, and low cost, among others. In the present work we have shown that the organic solvent phase can be replaced by inexpensive polymer beads that function in a similar fashion as organic solvents, delivering a toxic substrate to cells based on equilibrium considerations. Specifically, 3.4 mm diameter beads of poly(ethylene-co-vinyl acetate) (EVA) were used to reduce the aqueous concentration of phenol in a bioreactor from toxic levels ( ,2,000 mg/L) to subinhibitory levels (,750 mg/L), after which Pseudomonas putida ATCC 11172 was added to the system and allowed to consume the total phenol loading. Thus, the beads absorbed the toxic substrate and released it to the cells on demand. The EVA beads, which could be reused, were able to absorb 14 mg phenol/g EVA. This work has opened the possibility of using widely mixed cultures in TPPB systems without concern for degradation of the delivery material and without concern of contamination. © 2003 Wiley Periodicals. Biotechnol Bioeng84: 399,305, 2003. [source] Lipoprotein Mutation Accelerates Substrate Permeability-Limited Toluene Dioxygenase-Catalyzed ReactionBIOTECHNOLOGY PROGRESS, Issue 3 2005Ye Ni One of the major problems in whole-cell biocatalysis is its low reaction rate. The underlying cause is the substrate permeation barrier presented by cell envelopes. The present research investigates mutation effects of the Braunapos;s lipoprotein, the most abundant outer membrane structural protein in Escherichia coli, on toluene dioxyengase (TDO)-catalyzed reaction. Dramatic enhancement of the reaction rate, an increase of up to 6-fold, was observed with the mutant for all three small, hydrophobic substrates tested (toluene, ethylbenzene, and 2-indanone). The increase was observed over a wide range of substrate concentrations (0.1,5 mM). The mutant exhibited a normal growth rate and expressed the recombinant multicomponent enzyme as well as the isogenic parent strain. Taken together, the lipoprotein mutant expressing TDO is a much better whole-cell catalyst for the oxidation reaction. The beneficial effect of the lipoprotein mutation may be general for a broad range of substrates and enzyme systems as the mutation affects the global integrity of the cell membrane. A comparison of the mutation effect with a common permeabilizing procedure, the EDTA treatment, further illustrates the clear advantages of using genetic modification in cellular membrane engineering for improved whole-cell catalysts. [source] | |||||||||||||