Search results for "substrate"

showing 10 items of 1018 documents

Temperature effect on solubility of aroma compounds in various aqueous solutions

2005

International audience; Solubility of nine aroma compounds (methyl ketones, ethyl esters, aldehyde and alcohol) in various aqueous solutions was measured by the mutual solubility method from -10 to +10degreesC. Influence of both, the nature (carbohydrates and polyols) and the substrate concentration (from 0 to 57.5g/100g) on aroma solubility in aqueous solutions was studied. Aroma solubility in water decreased when aroma hydrophobicity increased. Aroma solubility in various aqueous solutions decreased when substrate concentration increased; their solubility was higher in polyols solutions than in polysaccharides ones. Temperature effect on aroma solubility showed a noncontinuous evolution f…

aqueous solutionsWater structureAlcoholPolysaccharide01 natural sciencesAldehydechemistry.chemical_compound0404 agricultural biotechnology[SDV.IDA]Life Sciences [q-bio]/Food engineeringOrganic chemistryLow temperature[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologySolubilityAromachemistry.chemical_classificationAqueous solutionbiology010405 organic chemistryfood and beverages04 agricultural and veterinary sciencesbiology.organism_classification040401 food scienceSubstrate concentrationMolar solubility0104 chemical scienceschemistrySolubilityAroma compoundsFood Science
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Use of artificial substrates for sampling benthic macroinvertebrates in the assessment of water quality of large lowland rivers

2004

The objective of this investigation was to evaluate the usefulness of the artificial substrate sampler in collecting macroinvertebrates for water quality assessment of Polish lowland rivers. This paper presents the results of a comparative study between two different sampling techniques, i.e. nettings filled with brick as artificial substrates and handnet sampling. The validity of applying the biotic index method is also demonstrated. The Belgian Biotic Index (BBI) method and the lower Nysa Kłodzka river were chosen for study. Macroinvertebrates were collected seasonally at five sampling sites. Although some invertebrate taxa revealed a specific preference for one of the two tested sampling…

artificial substrate samplermacroinvertebratesbiotic indexriver water qualityPolish Journal of Environmental Studies
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Synergistic enhancement via plasmonic nanoplate-bacteria-nanorod supercrystals for highly efficient SERS sensing of food-borne bacteria

2017

Bio-sensing techniques utilizing metallic nanoparticles as a probe have gained more and more attention and play today an important role in the detection of bacteria. To date, although several sensing materials have been tested, there is still a long way to go to achieve a fast, low-cost, ultrasensitive and multifunctional substrate suitable for a universal biosensor for detection of bacterial cells. Here, we report a novel probe design based on anisotropic plasmonic nanoparticles organized to a biocompatible 3D bio-inorganic scaffold, i.e., nanoplate-bacteria-nanorod supercrystals (NBNS) with extremely high surface-enhanced Raman spectroscopic (SERS) activity as a model of synergistic plasm…

assemblyMaterials scienceta221NanoparticleNanotechnology02 engineering and technologyrecognition of microbes010402 general chemistry01 natural sciencesBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biologybakteeritsymbols.namesakeNanoteknologia - NanotechnologyMaterials ChemistryKemia - Chemical sciencesElectrical and Electronic EngineeringbacteriaInstrumentationPlasmonPlasmonic nanoparticlesmikrobien tunnistaminenta114SERSMetals and AlloysSubstrate (chemistry)021001 nanoscience & nanotechnologyCondensed Matter Physicschemometrics0104 chemical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic Materialsasymmetric nanoparticlessymbolsnanoparticlesNanorodnanopartikkelit0210 nano-technologyRaman spectroscopyBiosensorRaman scattering
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The catalytic mechanism of glyceraldehyde 3-phosphate dehydrogenase from Trypanosoma cruzi elucidated via the QM/MM approach

2013

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been identified as a key enzyme involved in glycolysis processes for energy production in the Trypanosoma cruzi parasite. This enzyme catalyses the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) in the presence of inorganic phosphate (Pi) and nicotinamide adenosine dinucleotide (NAD+). The catalytic mechanism used by GAPDH has been intensively investigated. However, the individual roles of Pi and the C3 phosphate of G3P (Ps) sites, as well as some residues such as His194 in the catalytic mechanism, remain unclear. In this study, we have employed Molecular Dynamics (MD) simulations within hybrid quantum mechanical/molecular …

biocatalysisEnzims proteolíticsParàsitsStereochemistryTrypanosoma cruziGeneral Physics and AstronomyDehydrogenaseMolecular Dynamics SimulationNicotinamide adenine dinucleotideOxidative PhosphorylationSubstrate Specificityglyceraldehyde 3 phosphate dehydrogenaseQM/MMchemistry.chemical_compoundstomatognathic systemGlyceraldehydePhysical and Theoretical Chemistrynicotinamide adenine dinucleotideGlyceraldehyde 3-phosphate dehydrogenasechemistry.chemical_classificationbiologyGlyceraldehyde-3-Phosphate DehydrogenasesActive siteNADmolecular dynamicsEnzymechemistryBiochemistryBiocatalysisbiology.proteinQuantum TheoryNAD+ kinaseOxidation-ReductionPhysical Chemistry Chemical Physics
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The L-tartrate/succinate antiporter TtdT (YgjE) of L-tartrate fermentation in Escherichia coli.

2007

ABSTRACT Escherichia coli ferments l -tartrate under anaerobic conditions in the presence of an additional electron donor to succinate. The carrier for l -tartrate uptake and succinate export and its relation to the general C 4 -dicarboxylate carriers DcuA, DcuB, and DcuC were studied. The secondary carrier TtdT, encoded by the ttdT (previously called ygjE ) gene, is required for the uptake of l -tartrate. The ttdT gene is located downstream of the ttdA and ttdB genes, encoding the l -tartrate dehydratase TtdAB. Analysis of mRNA by reverse transcription-PCR showed that ttdA , ttdB , and ttdT are cotranscribed. Deletion of ttdT abolished growth by l -tartrate and degradation of l -tartrate c…

biologyAntiporterPhysiology and MetabolismSuccinic AcidHeterologousSubstrate (chemistry)Biological TransportTartratebiology.organism_classificationmedicine.disease_causeMicrobiologychemistry.chemical_compoundBiochemistrychemistryBacterial ProteinsDehydrataseFermentationOperonmedicineEscherichia coliFermentationMolecular BiologyEscherichia coliTartratesBacteriaJournal of bacteriology
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Preorganization and reorganization as related factors in enzyme catalysis: the chorismate mutase case.

2003

In this paper a deeper insight into the chorismate-to prephenate-rearrangement, catalyzed by Bacillus subtilis chorismate mutase, is provided by means of a combination of statistical quantum mechanics/molecular mechanics simulation methods and hybrid potential energy surface exploration techniques. The main aim of this work is to present an estimation of the preorganization and reorganization terms of the enzyme catalytic rate enhancement. To analyze the first of these, we have studied different conformational equilibria of chorismate in aqueous solution and in the enzyme active site. Our conclusion is that chorismate mutase preferentially binds the reactive conformer of the substrate--that…

biologyChemical PhenomenaChemistryStereochemistryChemistry PhysicalProtein ConformationOrganic ChemistryActive siteSubstrate (chemistry)General ChemistryEnzyme structureCatalysisEnzyme catalysisSolutionsMolecular dynamicsComputational chemistryPotential energy surfacebiology.proteinChorismate mutaseElectrochemistryConformational isomerismBacillus subtilisChorismate MutaseChemistry (Weinheim an der Bergstrasse, Germany)
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Propanediol-1,2-dehydratase and metabolism of glycerol of Lactobacillus brevis

1984

While most strains of heterofermentative lactobacilli and strains of Leuconostoc species contained only traces of a dehydratase reacting with glycerol or propanediol-1,2, three strains of Lactobacillus brevis and one strain of L. buchneri that metabolized glycerol readily in the presence of glucose, contained propanediol-1,2 dehydratase (EC 4.2.1.28). This cobamide requiring enzyme from L. brevis B 18 was partially purified. It reacts with the substrates propanediol-1,2, glycerol and ethanediol-1,2 with the relative activities of about 3:2:1. This ratio remained unchanged throughout the purification procedure. The substrate affinities were measured: propanediol-1,2 K m=0.6 mM, glycerol K m=…

biologyChemistryLactobacillus brevisSodiumchemistry.chemical_elementSubstrate (chemistry)General MedicinePropanediol dehydrataseMetabolismbiology.organism_classificationBiochemistryMicrobiologyPropanediolchemistry.chemical_compoundBiochemistryDehydrataseGeneticsGlycerolMolecular BiologyArchives of Microbiology
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Modeling for the active site nitrate reductase. Oxidation of the complex [MovO(O2CC(S) CH3Ph)2]− by nitrate and nitrite in methanol

1998

Abstract Under acid conditions the [MoVIO2(O2CC(S)CH1Ph)2]2 reacts with thiols to yield the monomeric [MoVO(O2CC(S)CH3Ph)2] and disulfide. The reduced complex [MoVO(O2CC(S)CH3Ph)2]− can react with NO3− and NO2− in a one-electron step yeilding respectively NO2 and NO and the original molybdenum (VI)-dioxo complex. The experimental pseudo-first-order rate constant with respect to the Mo(V) complex at 25°C was found to be kobs=2.3×10−4s−1 for NO3− and kobs=1.0×10−2 for NO2−. Oxo transfers to and from the substrate have been coupled to produce a catalytic system which turns over the reaction RSH+(No3− or NO2−)+H+a 1 2 [ RS ] 2 +( NO ] 2 or NO )+ H 2 O , in which thiols, NO1− and NO2− serve as a…

biologyInorganic chemistrySubstrate (chemistry)chemistry.chemical_elementActive siteNitrate reductaseMedicinal chemistryCatalysisInorganic Chemistrychemistry.chemical_compoundReaction rate constantchemistryMolybdenumMaterials Chemistrybiology.proteinMethanolPhysical and Theoretical ChemistryNitriteInorganica Chimica Acta
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Kinetics of citrate uptake in growing cells ofLeuconostocspp.

1996

Citrate uptake was studied in growing cells of Leuconostoc mesenteroides subsp. mesenteroides. A Michaelis-Menten pattern with the dianionic form of citrate as the limiting substrate has been proposed. It was validated for different fermentations varying the initial citrate concentrations and the pH medium. This latter did not modify the rate of the process which was clearly confirmed using experiments with resting cells. The model was used to compare the kinetics of citrate consumption between several strains of Leuconostoc mesenteroides subsp. mesenteroides, Leuconostoc mesenteroides subsp. cremoris and Leuconostoc lactis.

biologyKineticsfood and beveragesSubstrate (chemistry)Leuconostoc lactisCitrate transportbiology.organism_classificationStreptococcaceaeMicrobiologycarbohydrates (lipids)BiochemistryLeuconostoc mesenteroidesGeneticsbacteriaLeuconostocMolecular BiologyBacteriaFEMS Microbiology Letters
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Evaluation of cellular response of breast cancer cells grown on distinctive collagen substrates

2008

breast cancer cells proteomics collagen substratesSettore BIO/06 - Anatomia Comparata E Citologia
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