Search results for "thermostability"

showing 6 items of 16 documents

Inactivation kinetics of pectin methyl esterase under combined thermal–high pressure treatment in an orange juice–milk beverage

2008

Abstract The inactivation kinetics of PME in an orange juice–milk beverage system treated by thermal (65–80 °C) and combined thermal (25–65 °C)–high pressure (0.1–700 MPa) processes were fitted using a biphasic model. About 6–8% of the initial activity corresponding to the heat and pressure stable fraction was observed. For complete inactivation a treatment at 90 °C, 1 min or 700 MPa at 55 °C for 2 min was necessary showing the protective effect of the orange–milk media. The extent of inactivation was different in the orange matrices showing that PME was more thermostable in the orange juice–milk based beverage system as compared to the purified enzyme in a buffer system. On the other hand,…

Orange juicefood.ingredientfoodChromatographyPectinChemistryFood additiveKineticsOrange (colour)EsteraseFood SciencePectinesteraseThermostabilityJournal of Food Engineering
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Thermostability of Two Cyanobacterial GrpE Thermosensors

2011

GrpE proteins act as co-chaperones for DnaK heat-shock proteins. The dimeric protein unfolds under heat stress conditions, which results in impaired interaction with a DnaK protein. Since interaction of GrpE with DnaK is crucial for the DnaK chaperone activity, GrpE proteins act as a thermosensor in bacteria. Here we have analyzed the thermostability and function of two GrpE homologs of the mesophilic cyanobacterium Synechocystis sp. PCC 6803 and of the thermophilic cyanobacterium Thermosynechococcus elongatus BP1. While in Synechocystis an N-terminal helix pair of the GrpE dimer appears to be the thermosensing domain and mainly mediates GrpE dimerization, the C-terminal four-helix bundle i…

PhysiologyMolecular Sequence DataProtein domainPlant SciencePlasma protein bindingCyanobacteriaProtein structureBacterial ProteinsHeat shock proteinEscherichia coliAmino Acid SequencePeptide sequenceHeat-Shock ProteinsThermostabilitySequence Homology Amino AcidbiologyProtein StabilityChemistryCircular DichroismGenetic Complementation TestSynechocystisSynechocystisTemperatureCell BiologyGeneral Medicinebiology.organism_classificationProtein Structure TertiaryCross-Linking ReagentsChaperone (protein)Biophysicsbiology.proteinbacteriaProtein MultimerizationProtein BindingPlant and Cell Physiology
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Untersuchungen von polymeren im massenspektrometer, 4. Abbaureaktionen von polybenzylen

1974

Die Abbaureaktionen von unsubstituierten Poly(1,4-phenylenmethylen)en (A) (Polybenzylen), Poly[(2,5-dimethyl-1,4-phenylen)methylen] [Poly(2,5-dimethylbenzyl)] (B), Poly[(2,3,5,6-tetramethyl-1,4-phenylen)methylen] [Poly(2,3,5,6-tetramethylbenzyl)] (C) und Poly(1,4-phenylenathyliden) [Poly(α-methylbenzyl)] (D) wurden durch direkte Pyrolyse im Massenspektrometer untersucht. Die Massenpyrogramme von unter verschiedenen Reaktionsbedingungen dargestellten Polybenzylen wurden verglichen, mit dem Ziel, direkt Informationen uber Strukturunterschiede wie Kettenverzweigung und unterschiedliche Verknupfung der Benzyleinheiten zu erhalten; hierbei konnten in einem Falle auf hohere Kettenverzweigung deut…

Reaction conditionschemistry.chemical_classificationSteric effectschemistry.chemical_compoundMonomerchemistryPolymer chemistryDisproportionationMethyleneBranching (polymer chemistry)AlkylThermostabilityDie Makromolekulare Chemie
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Degradation of heterocyclic aromatic amines in oil under storage and frying conditions and reduction of their mutagenic potential.

2007

Heterocyclic aromatic amines (HAA) were systematically studied concerning their partition behavior in water/oil-systems and their thermostability in different animal derived fats and vegetable oils. Partitioning of IQx-compounds and PhIP in water/oil systems was found to depend on the polarity defined by the molecular structure and on the pH-value of the aqueous phase. In particular, beta-carbolines norharman and harman showed a significant strong lipophilic character at alkaline pH. After heating in frying fats at 130 degrees C, contents of IQx compounds and PhIP were reduced by more than 40% and after heating at 180 degrees C less than 10% of the HAA initial concentration was recovered. B…

Salmonella typhimuriumHot TemperatureMutagenToxicologymedicine.disease_causeLipid oxidationHeterocyclic CompoundsmedicineOrganic chemistryPlant OilsCookingAminesThermostabilitychemistry.chemical_classificationDose-Response Relationship DrugMolecular StructureMutagenicity TestsAqueous two-phase systemAromatic amineWaterGeneral MedicineDietary FatschemistryHeterocyclic compoundDegradation (geology)Oxidation-ReductionGenotoxicityFood ScienceMutagensFood and chemical toxicology : an international journal published for the British Industrial Biological Research Association
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High-resolution crystal structure of an avidin-related protein: insight into high-affinity biotin binding and protein stability.

2004

The chicken avidin gene belongs to an extended gene family encoding seven avidin-related genes (AVRs), of which only avidin is expressed in the chicken. The sequences of AVR4 and AVR5 are identical and the common protein (AVR4) has been expressed both in insect and bacterial systems. The recombinant proteins are similarly hyperthermostable and bind biotin with similarly high affinities. AVR4 was crystallized in the apo and biotin-complexed forms and their structures were determined at high resolution. Its tertiary and quaternary structures are very similar to those of avidin and streptavidin. Its biotin-binding site shows only a few alterations compared with those of avidin and streptavidin…

StreptavidinBiotin bindingHot TemperatureBiotinBiologylaw.inventionchemistry.chemical_compoundBiotinStructural BiologylawAnimalsProtein Structure QuaternaryThermostabilityBacteriaHydrogen BondingGeneral MedicineAvidinAffinitiesBiochemistrychemistryBiotinylationData Interpretation StatisticalBiophysicsRecombinant DNAbiology.proteinStreptavidinCrystallizationBaculoviridaeChickensAvidinProtein BindingActa crystallographica. Section D, Biological crystallography
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Halloysite nanotubes sandwiched between chitosan layers: novel bionanocomposites with multilayer structures

2018

This work is a contribution to the design of multilayer biocomposites based on halloysite nanotubes (HNTs) and chitosan. Both the polymer and nanotubular inorganic additive have been selected among easily available green materials. An innovative preparation procedure based on the sequential casting of chitosan and HNTs has been proposed in order to obtain multilayer composite biofilms. A physico-chemical investigation (contact angle measurements, differential scanning calorimetry, thermogravimetry) has been conducted to characterize the bionanocomposites. As evidenced by scanning electron microscopy, the nanocomposites possess an intermediate halloysite layer between the chitosan ones. The …

Thermogravimetric analysissurface propertyoxidationthermogravimetry02 engineering and technologyengineering.material010402 general chemistry01 natural sciencesHalloysiteArticleCatalysisnanotube adsorptionChitosanContact anglechemistry.chemical_compoundDifferential scanning calorimetryMaterials Chemistrycontact anglecomparative studydegradationSettore CHIM/02 - Chimica FisicaNanocompositenanocompositeGeneral Chemistry021001 nanoscience & nanotechnologythermostability0104 chemical sciencesThermogravimetrypriority journalchemistryChemical engineeringtissue engineeringengineeringchitosandifferential scanning calorimetry0210 nano-technologyHybrid materialscanning electron microscopyNew Journal of Chemistry
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