Search results for "lysozyme"

showing 10 items of 57 documents

Hierarchical bimodal porous silicas and organosilicas for enzyme immobilization

2005

This work shows the ability of a hierarchical porous silica-based network with pore systems at two different length scales for enzyme immobilization. Two different enzymes have been selected, lysozyme, a relatively small globular enzyme, and α-L-arabinofuranosidase, a large enzyme of interest in the winemaking industry. The lysozyme immobilization on several silica supports (bimodal porous silicas denoted UVM-7 materials and conventional silica xerogels) has been studied and the loading amounts can be correlated to the open nature and accessibility of the internal surface area. Bimodal UVM-7 silicas present a very quick adsorption rate and high enzyme loading. α-L-Arabinofuranosidase has be…

Materials scienceEthanolImmobilized enzymeInorganic chemistryGeneral Chemistrychemistry.chemical_compoundAdsorptionchemistryCovalent bondHigh glucoseMaterials ChemistryLysozymePorosityPorous mediumJournal of Materials Chemistry
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In vitrouptake of lysozyme-loaded liposomes coated with chitosan biopolymer as model immunoadjuvants

2009

Chitosan binds to negatively charged soy lecithin liposomes by an electrostatic interaction driven by its cationic amino group. This interaction allows developing stable coated vesicles suitable as a targeted carrier and controlled release system for drugs and vaccines. In this work, we studied the effect of chitosan-coated liposomes on the uptake and antigen presentation of hen egg-white lysozyme (HEL) in Peyer's patches peritoneal macrophages isolated from mice. Chitosan-coated liposomes were characterized according to size, zeta potential, and antigen-loading and release properties. Results showed an increase in the positive net charge and size of the liposomes as the concentration of ch…

Materials sciencePolymersCoated vesiclePharmaceutical Scienceengineering.materialChitosanchemistry.chemical_compoundMicePeyer's PatchesBiopolymersDrug Delivery SystemsAdjuvants ImmunologicCationsZeta potentialFluorescence microscopeAnimalsLiposomeChitosanChromatographyMicroscopy Confocaltechnology industry and agricultureControlled releasechemistryMicroscopy FluorescenceLiposomesengineeringInterleukin-2FemaleMuramidaseBiopolymerLysozymeJournal of Liposome Research
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Characterization of two Lactococcus lactis zinc membrane proteins, Llmg_0524 and Llmg_0526, and role of Llmg_0524 in cell wall integrity

2015

Background Due to its extraordinary chemical properties, the cysteine amino acid residue is often involved in protein folding, electron driving, sensing stress, and binding metals such as iron or zinc. Lactococcus lactis, a Gram-positive bacterium, houses around one hundred cysteine-rich proteins (with the CX2C motif) in the cytoplasm, but only a few in the membrane. Results In order to understand the role played by this motif we focused our work on two membrane proteins of unknown function: Llmg_0524 and Llmg_0526. Each of these proteins has two CX2C motifs separated by ten amino-acid residues (CX2CX10CX2C). Together with a short intervening gene (llmg_0525), the genes of these two protein…

Microbiology (medical)Lysozymechemistry.chemical_elementZincPlasma protein bindingGrowthMicrobiologyMembrane proteins;Growth;Cumene hydroperoxideProtein structureBacterial ProteinsCumene hydroperoxideCell Wallcystéinelactococcus lactisMembrane proteinsBenzene Derivatives[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCysteineBinding siteBinding SitesbiologyProtein StabilityLactococcus lactispropriété de membranebiology.organism_classificationcroissanceProtein Structure Tertiary3. Good healthZincchemistryBiochemistryMembrane proteinProtein foldingProtein BindingResearch ArticleCysteine
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Irreversible gelation of thermally unfolded proteins:structural and mechanical properties of lysozyme aggregates

2010

The formation of protein aggregates is important in many fields of life science and technology. The morphological and mechanical properties of protein solutions depend upon the molecular conformation and thermodynamic and environmental conditions. Non-native or unfolded proteins may be kinetically trapped into irreversible aggregates and undergo precipitation or gelation. Here, we study the thermal aggregation of lysozyme in neutral solutions. We characterise the irreversible unfolding of lysozyme by differential scanning calorimetry. The structural properties of aggregates and their mechanisms of formation with the eventual gelation are studied at high temperature by spectroscopic, rheolog…

Models MolecularProtein FoldingCircular dichroismGelationProtein ConformationDiffusionBiophysicsProtein aggregationUnfoldingchemistry.chemical_compoundDifferential scanning calorimetryProtein structureAnimalsQuantitative Biology::BiomoleculesChemistryPrecipitation (chemistry)Circular DichroismTemperaturePercolationGeneral MedicineBlood Coagulation FactorsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Thermal irreversibilityCrystallographyChemical physicsThermodynamicsMuramidaseProtein foldingLysozymeProtein aggregation
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Calculation of partition coefficient and hydrophobic moment of the secondary structure of lysozyme

2001

A method that permits a semiquantitative estimate of the partitioning of any solute between any two media is presented. As an example, the partition coefficients and hydrophobic moment of the secondary structure of lysozyme are calculated. Program GSCAP is written as a version of Pascal's solvent-dependent conformational analysis (SCAP) program. The dipole moments calculated for the helices are trebled with respect to that for the sheet. For helices, the main contribution to the water-accessible surface area is the hydrophobic term, while the hydrophilic part dominates in the sheet. Molecular globularity and the three studied partition coefficients differentiate between helices and sheet.

Models MolecularQuantitative Biology::BiomoleculesChromatographyOrganic ChemistrySolvationGeneral MedicineBiochemistryProtein Structure SecondaryAnalytical ChemistryGibbs free energyCondensed Matter::Soft Condensed MatterPartition coefficientchemistry.chemical_compoundsymbols.namesakeDipolechemistrysymbolsThermodynamicsMoleculeMuramidaseLysozymeProtein secondary structureJournal of Chromatography A
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SELDI-TOF-MS ProteinChip array profiling of tears from patients with dry eye.

2005

Protein and peptides in tears play an important role in ocular surface diseases. In previous studies, changes have been demonstrated in the electrophoretic protein profiles of patients with dry eye. The purpose of this work was to determine the usefulness of surface-enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF-MS) ProteinChip Array (Ciphergen Biosystems, Inc., Fremont, CA) technology for the automated analysis of proteins and peptides in tear fluid.Patients with dry eye (DRY, n = 88) and healthy subjects (CTRL, n = 71) were examined. Their tear proteins were analyzed using SELDI-TOF-MS ProteinChip Arrays with three different chromatographic surfaces (CM10…

Pathologymedicine.medical_specialtyEye diseaseProtein Array AnalysisDry Eye SyndromesLipocalinchemistry.chemical_compoundSELDI-TOF-MSmedicineHumansIn patientEye ProteinsChromatography High Pressure LiquidChromatographybusiness.industryHealthy subjectsmedicine.diseaseChromatography Ion ExchangechemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationTearsTearsDry Eye SyndromesNeural Networks ComputerLysozymebusinessPeptidesBiomarkersInvestigative ophthalmologyvisual science
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Activation of the first component of complement, C1: comparison of the effect of sixteen different enzymes on serum C1.

1983

In this study, the effect of sixteen different enzymes on serum C1 and its subcomponents was investigated. The sixteen enzymes could be divided into three groups. First, enzymes which activate native C1: trypsin (optimal concentration 2.4 x 10(-4) mM); alpha-chymotrypsin (2.3 x 10(3) mM); thrombin (1.0 x 10(-5) mM); plasmin (1.9 x 10(-5) mM); elastase (5.8 x 10(-5) mM); pronase (3.0 x 10(-6) mM). All these enzymes are serine esterase and activate native serum C1 bound to EAC4 at the given concentration within 10 min at 30 degrees C. Furthermore, native C1 inhibited by a pentosanpolysulfoester, Sp54, is unable to undergo the internal activation but can be externally activated by the serine e…

PlasminComplement Activating EnzymesImmunologyGuinea PigsDose-Response Relationship ImmunologicPronaseSerinechemistry.chemical_compoundComplement C1medicineImmunology and AllergyAnimalsHumansTrypsinFibrinolysinComplement Activationchemistry.chemical_classificationPentosan Sulfuric PolyesterbiologyHematologyTrypsinCarboxypeptidaseKineticsEnzymeBiochemistrychemistrybiology.proteinCollagenaseCattleRabbitsLysozymemedicine.drugPeptide HydrolasesImmunobiology
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Protein-Based Nanoparticles for the Delivery of Enzymes with Antibacterial Activity.

2018

Proteins represent a versatile biopolymer material for the preparation of nanoparticles due to their biocompatibility, biodegradability, and low immunogenicity. This study presents a protein-based nanoparticle system consisting of high surface PEGylated lysozyme polyethylene glycol-modified lysozyme (LYZmPEG ). This protein modification leads to a solubility switch, which allows a nanoparticle preparation using a mild double emulsion method without the need of surfactants. The method allows the encapsulation of large hydrophilic payloads inside of the protein-based nanoparticle system. Native lysozyme (LYZ) was chosen as payload because of its innate activity as natural antibiotic. The mild…

Polymers and PlasticsBiocompatibilityNanoparticle02 engineering and technologyengineering.material010402 general chemistryGram-Positive Bacteria01 natural sciencesPolyethylene Glycolschemistry.chemical_compoundMaterials ChemistryHumansSolubilityDrug CarriersChemistryOrganic ChemistryProteinsBiodegradation021001 nanoscience & nanotechnology0104 chemical sciencesAnti-Bacterial AgentsChemical engineeringengineeringNanoparticlesEmulsionsMuramidaseBiopolymerLysozyme0210 nano-technologyDrug carrierAntibacterial activityHydrophobic and Hydrophilic InteractionsMacromolecular rapid communications
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Protein Thermal Denaturation and Matrix Glass Transition in Different Protein−Trehalose−Water Systems

2011

Biopreservation by saccharides is a widely studied issue due to its scientific and technological importance; in particular, ternary amorphous protein-saccharide-water systems are extensively exploited to model the characteristics of the in vivo biopreservation process. We present here a differential scanning calorimetry (DSC) study on amorphous trehalose-water systems with embedded different proteins (myoglobin, lysozyme, BSA, hemoglobin), which differ for charge, surface, and volume properties. In our study, the protein/trehalose molar ratio is kept constant at 1/40, while the water/sugar molar ratio is varied between 2 and 300; results are compared with those obtained for binary trehalose…

Protein DenaturationdenaturationMolecular Dynamics SimulationPhase TransitionDSCMatrix (chemical analysis)Hemoglobinschemistry.chemical_compoundDifferential scanning calorimetryMaterials ChemistryAnimalsglass transitionPhysical and Theoretical ChemistrytrehaloseSettore CHIM/02 - Chimica FisicaChromatographyCalorimetry Differential ScanningMyoglobinTemperatureProteinsWaterSerum Albumin BovineTrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Surfaces Coatings and FilmsAmorphous solidchemistryChemical engineeringMyoglobinconfinementCattleMuramidaseLysozymeTernary operationGlass transitionThe Journal of Physical Chemistry B
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Photosensibilisierte Oxidation von Lysozym bei Verschiedenen Wellenlängen

1974

The photooxidation of lysozyme in the presence of methylene blue, riboflavine, and bengal rose at differentpH values and wavelengths was studied. Monochromatic irradiation at shorter wavelengths (345 and 365 nm) is - in contrast to visible light - characterized by higher energy yields and lower oxygen consumption. This behavior suggests that the mechanism of photooxidation depends on the wavelength. The specific destruction of amino acid residues is also wavelength-dependent. Using visible light of 448 and 621 nm for riboflavine and methylene blue, respectively, we have confirmed the selective destruction of histidine and tryptophan atpH 7,0. The energy yield for the destruction of tryptoph…

Radiationdigestive oral and skin physiologyBiophysicsCystineTryptophanfood and beveragesPhotochemistryeye diseasesstomatognathic diseaseschemistry.chemical_compoundchemistryRose bengalsense organsIrradiationLysozymeMethylene blueHistidineGeneral Environmental ScienceVisible spectrumRadiation and Environmental Biophysics
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