Search results for "Lactoglobulins"

showing 8 items of 18 documents

Use of Catalyst in a 3D-QSAR Study of the Interactions between Flavor Compounds and β-Lactoglobulin

2003

This paper reports a 3D-QSAR study using Catalyst software to explain the nature of interactions between flavor compounds and beta-lactoglobulin. A set of 35 compounds, for which dissociation constants were previously determined by affinity chromatography, was chosen. The set was divided into three subsets. An automated hypothesis generation, using HypoGen software, produced a model that made a valuable estimation of affinity and provided an explanation for the lack of correlation previously observed between the hydrophobicity of terpenes and the affinity for the protein. On the basis of these results, it appears that aroma binding to beta-lactoglobulin is caused by both hydrophobic interac…

Quantitative structure–activity relationshipChemical PhenomenaChemistry PhysicalTerpenesChemistryStereochemistryQuantitative Structure-Activity RelationshipHydrogen BondingLactoglobulinsGeneral ChemistryCatalysisDissociation constantModels ChemicalComputational chemistryOdorantsComputer SimulationDrug InteractionsGeneral Agricultural and Biological SciencesSoftwareFlavorJournal of Agricultural and Food Chemistry
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Polymorphisms of beta-lactoglobulin promoter region in three Sicilian goat breeds

2012

Several beta-lactoglobulin (BLG) polymorphisms have been described within the proximal promoter region and coding region of the caprine gene, although no genetic variants affecting the protein amino acid composition and/or expression level have been characterized so far. Binding sites for several transcription factors (TFs) are present in the BLG promoter region. The aims of this work were to sequence the full-length promoter region of three Sicilian goat breeds in order to identify polymorphisms, analyze the identified haplotypes, search for differences between breeds for the presence of polymorphisms in this gene region, search for putative TFs binding sites, and check if polymorphisms la…

SICILIAN GOATMolecular Sequence DataSNPSingle-nucleotide polymorphismLactoglobulinsBiologyPolymerase Chain ReactionPolymorphism Single NucleotideSettore AGR/17 - Zootecnica Generale E Miglioramento GeneticoSpecies SpecificityBETA LACTOGLOBULIN GENEGene expressionGeneticsAnimalsCluster AnalysisCoding regionBinding sitePromoter Regions GeneticSicilyMolecular BiologyGeneTranscription factorGeneticsBase SequenceModels GeneticGoatsHaplotypeGenetic VariationPromoterSequence Analysis DNAGeneral MedicineMilk ProteinsMolecular biologyNFI Transcription FactorsTRANSCRIPTION FACTORSBeta-lactoglobulin Polymorphisms Promoter Sicilian goatsHAPLOTYPES
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Protein-lipid interactions at the air-water interface.

2010

International audience; Protein−lipid interactions play an important role in a variety of fields, for example in pharmaceutical research, biosensing, or food science. However, the underlying fundamental processes that govern the interplay of lipids and proteins are often very complex and are therefore studied using model systems. Here, Langmuir monolayers were used to probe the interaction of a model protein with lipid films at the air−water interface. The protein β-lactoglobulin (βlg) is the major component in bovine milk serum, where it coexists with the milk fat globular membrane. During homogenization of milk, βlg adsorbs to the interface of lipid fat globules and stabilizes the oil-in-…

Surface PropertiesPhospholipidLactoglobulinsHomogenization (chemistry)chemistry.chemical_compoundMonolayerElectrochemistryAnimalsGeneral Materials ScienceDenaturation (biochemistry)Globules of fatSpectroscopyChromatographyAirCell MembraneWaterSurfaces and InterfacesHydrogen-Ion ConcentrationCondensed Matter PhysicsLipid Metabolism[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMembranechemistryIonic strengthEmulsionBiophysicslipids (amino acids peptides and proteins)CattleProtein BindingLangmuir : the ACS journal of surfaces and colloids
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Transfer of aroma compounds in water-lipid systems: binding tendency of beta-lactoglobulin.

1998

Interactions of volatile aroma compounds with protein in aqueous solutions, especially whey proteins, have received significant attention in recent years. This work attempts to improve our understanding of the mass transfer in multiphasic systems, such as emulsions at the lipid−water interface, and to reveal the role of β-lactoglobulin in the release rate of solutes. For this purpose the rotating diffusion cell has been used. From a practical point of view it enables evaluation of the transfer through the aqueous phase, through the oil and the interfacial transfer. The effect of β-lactoglobulin, medium pH, and solute concentration has been investigated. Benzaldehyde and 2-nonanone have been…

Whey proteinChromatographyAqueous solutionbiologyChemistryDiffusionAqueous two-phase systemfood and beveragesWaterGeneral ChemistryLactoglobulinsbiology.organism_classificationLipidsPartition coefficientMass transferEmulsionGeneral Agricultural and Biological SciencesAromaProtein BindingJournal of agricultural and food chemistry
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Probing Protein−Membrane Interactions Using Solid Supported Membranes

2011

International audience; Tethered bilayer lipid membranes have been used as a model system to mimic the interactions between the whey protein β-lactoglobulin and a lipid interface. The approach allowed for a detailed study of the lipid-protein interactions, the results being of possible importance in food and cosmetic applications. For such applications, lipid-protein interactions and the interfacial behavior are vital factors in controlling and manipulating process conditions such as emulsion stabilization and gelification. Lipid composition as well as the structural properties of the protein governed their interactions, which were probed by a combination of surface plasmon spectroscopy, ne…

Whey proteinChromatographyChemistryBilayerLipid Bilayersfood and beveragesModel systemLactoglobulinsSurfaces and InterfacesCondensed Matter PhysicsReflectivity[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMembraneMembrane interactionBilayer lipid membranesElectrochemistryBiophysicslipids (amino acids peptides and proteins)General Materials ScienceLipid bilayer phase behaviorSpectroscopyLangmuir
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Effect of Ligands on HP-Induced Unfolding and Oligomerization of β-Lactoglobulin

2020

ABSTRACTTo probe intermediate states during unfolding and oligomerization of proteins remains a major challenge. High pressure (HP) is a powerful tool for studying these problems, revealing subtle structural changes in proteins not accessible by other means of denaturation. Bovine β-lactoglobulin (BLG), the main whey protein, has a strong propensity to bind various bioactive molecules, such as retinol and resveratrol, two ligands with different affinity and binding sites. By combining in situ HP-small-angle neutron scattering (SANS) and HP-UV/visible absorption spectroscopy, we report the specific effects of these ligands on 3D conformational and local changes in BLG induced by HP. Dependin…

Whey proteinProtein Folding[SDV]Life Sciences [q-bio]BiophysicsAb initioLactoglobulins010402 general chemistryLigands01 natural sciences03 medical and health sciences0404 agricultural biotechnologyAnimalsDenaturation (biochemistry)[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyBinding site030304 developmental biology0303 health sciencesBinding SitesChemistry04 agricultural and veterinary sciencesArticlesLigand (biochemistry)040401 food science0104 chemical sciencesCovalent bondBiophysicsUnfolded protein responseProtein foldingCattleHydrophobic and Hydrophilic Interactions
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Flavour retention and release from protein solutions

2006

International audience; This paper briefly presents the main results obtained up to now on protein–flavour binding and release in relation with flavour perception. Among the food proteins, β-lactoglobulin is the most extensively studied for its binding properties, which involve both hydrophobic and hydrogen binding. Recent developments using molecular modelling and Quantitative Structure–Activity Relationship confirmed the existence of two different binding sites for flavour compounds on β-lactoglobulin. During the aroma release process in the mouth, not only free aroma compounds are released but also those reversibly bound by the protein, pointing out the fact that flavour perception is on…

[SDV.BIO]Life Sciences [q-bio]/BiotechnologyPROTEINSFlavourBioengineeringLactoglobulins01 natural sciencesApplied Microbiology and Biotechnology0404 agricultural biotechnologyComputational chemistryCyclohexenesHumansBinding siteAromaStrong bindingFlavorBinding SitesbiologyFLAVOUR RELEASETerpenesChemistry010401 analytical chemistryBinding propertiesfood and beveragesSerum Albumin Bovine04 agricultural and veterinary sciencesHydrogen-Ion ConcentrationMilk Proteinsbiology.organism_classification040401 food science0104 chemical sciences[SDV.BIO] Life Sciences [q-bio]/BiotechnologyFlavoring AgentsBiochemistryBenzaldehydesTasteFLAVOUR BINDINGSoybean ProteinsFood TechnologyLimoneneProtein BindingBiotechnology
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Metal ions modulate thermal aggregation of betalactoglobulin: a join chemical and physical characterization

2014

Abstract Molecular basis of the role played by Cu 2 + and Zn 2 + ions during the thermal aggregation processes of beta-lactoglobulin (BLG) was studied by using a joint application of different techniques. In particular, Raman spectroscopy was very useful in identifying the different effects caused by the two metals at molecular level (i.e. changes in His protonation state, disulfides bridge conformation, and micro-environment of aromatic residues), evidencing the primary importance of the protein charge distribution during the aggregation process. Both metal ions are able to act on this factor and favor the protein aggregation, but Zn 2 + is able to alter the natural conformational state of…

inorganic chemicalsCOPPER AND ZINC IONSMetal ions in aqueous solutionBeta-lactoglobulin; Copper and zinc ions; Raman spectroscopy; Infrared spectroscopy; Dynamic light scatteringBeta-lactoglobulinInfrared spectroscopyProtonationThermal treatmentLactoglobulinsProtein aggregationCopper and zinc ionSpectrum Analysis RamanBiochemistryFOURIER-TRANSFORM INFRARED SPECTROSCOPYProtein Structure SecondarySupramolecular assemblyIonBOVINE BETA-LACTOGLOBULINInorganic ChemistryProtein AggregatesDynamic light scatteringSpectroscopy Fourier Transform InfraredInfrared spectroscopyIonsChemistryTemperatureCrystallographyZincRaman spectroscopyBeta-lactoglobulin; Copper and zinc ions; Dynamic light scattering; Infrared spectroscopy; Raman spectroscopyDYNAMIC LIGHT SCATTERINGCopper
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