Search results for "beta-Lactoglobulin"

showing 10 items of 27 documents

Effects of different genotypes at the CSN3 and LGB loci on milk and cheese-making characteristics of the bovine Cinisara breed

2017

The Cinisara is an autochthonous Sicilian bovine breed reared mainly for production of Caciocavallo Palermitano, a typical stretched-curd cheese. The distribution of A and B alleles at both the β-lactoglobulin (LGB) and κ-casein (CSN3) loci in Cinisara cows and their influence on milk traits and cheese yield and composition were analysed. The LGB alleles are associated with significantly different effects on whey protein level (lower for BB genotype, P < 0.01), and casein index (higher value for BB genotype, P < 0.001), while CSN3 alleles were associated with significantly different effects on milk yield and coagulation properties; the BB genotype showed higher values for milk yield (…

0301 basic medicineSettore AGR/19 - Zootecnica SpecialeWhey proteink-caseincow milkCinisaraBeta-lactoglobulin0402 animal and dairy sciencefood and beveragesCheese yield04 agricultural and veterinary sciencesBiologyCoagulation propertie040201 dairy & animal scienceApplied Microbiology and BiotechnologyBreed03 medical and health sciences030104 developmental biologyMilk yieldCaseinCinisara; cow milk; k-casein; Beta-lactoglobulin; Coagulation properties; Cheese yields;GenotypeComposition (visual arts)Food scienceFood ScienceInternational Dairy Journal
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Effect of iron chelates on oil–water interface, stabilized by milk proteins: The role of phosphate groups and pH. Prediction of iron transfer from aq…

2010

International audience; Iron incorporated into food systems induces oxidation and precipitation. The consequences are reduced bioavailability and a functional modification of other food components such as proteins. The iron-chelates such as ferrous bisglycinate represent a possibility to avoid side effects, since the iron is protected. The aim of this study is to investigate the effects of iron-chelates compounds on the properties of an oil/water interface stabilized by caseinate or β-lacotoglobulin, under environmental conditions at 20 °C. Analyses were performed using dynamic drop tensiometry during 5000 s. The aqueous bulk phase is an imidazole/acetate buffer (0.1 M), containing 0.4 × 10…

030309 nutrition & dieteticsGeneral Chemical EngineeringInorganic chemistryIron fortificationSurface tension03 medical and health scienceschemistry.chemical_compound0404 agricultural biotechnologyOil-in-water emulsion[SDV.IDA]Life Sciences [q-bio]/Food engineeringChelationBeta-lactoglobulin2. Zero hunger0303 health sciencesAqueous solutionChromatographybiologyChemistryAqueous two-phase systemEmulsifying activityProteins04 agricultural and veterinary sciencesGeneral ChemistryPhosphate040401 food scienceEmulsionPhosphate groupsbiology.proteinChemical stabilityFood ScienceFood Hydrocolloids
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Thermal induced conformational changes involved in the aggregation of beta-lactoglobulin

2005

Aggregation of proteins appears to be associated most often with conformational and structural changes that lead to exposure of some apolar residues. Depending on the native structure of the protein in exam, aggregation is a process that involves different mechanisms, whose time of occurrence and interplay can depend upon temperature. To single out information about the multistages of the aggregation pathway, here we investigate the thermally induced conformational and structural changes of the beta-lactoglobulin (BLG). The experimental approach consists in studying steady-state fluorescence spectra of intrinsic chromophores, two tryptophans, and Anylino-Naphthalene-Sulfonate dye (ANS) mole…

ANS emissionBeta-lactoglobulinProtein aggregationRayleigh scatteringCircular dichroismConformational changeFluorescence
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Beta-lactoglobulin polymorphism in Girgentana goat breed

2007

Beta-lactoglobulin (b-lg) is a globular protein belonging to the lipocalin family. It is the major whey protein in the milk of ruminants. It is also present in the milk of most mammals but is lacking in rodents, lagomorphs and humans. A large number of variants have been reported for cow and sheep milk. Several studies have shown association between b-lg variants and milk production and composition, even if the results are not always concordant. In goat, no b-lg variants related with amino acid change have been characterized at DNA level, but some authors described the presence of polymorphisms in the 3’UTR and in the proximal promoter region. Mutations in the promoter region could be those…

Geneticsfood and beveragesPromoterBiologyBreedgenomic DNAchemistry.chemical_compoundSettore AGR/17 - Zootecnica Generale E Miglioramento GeneticochemistryGene expressionbiology.proteinBeta-lactoglobulin polymorphisms Girgentana goat breedAnimal Science and Zoologylcsh:Animal cultureSheep milkGeneBeta-lactoglobulinDNAlcsh:SF1-1100
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Variation of proteomic profile during lactation in Girgentana goat milk: a preliminary study

2019

The knowledge of milk proteome has been greatly enhanced by technological advances in the proteomics field as the use of the two-dimensional differential in-gel electrophoresis, a gel-based approach which allowed the analysis of proteins from complex mixtures and the comparing of several protein samples in the same experiment. The aim of this study was to characterise the whole milk proteomic profile in Girgentana dairy goat breed by two-dimensional differential in-gel elecrophoresis. The obtained representative 2D whole milk proteomic map showed a general picture of the protein distributions over the pH 3–10 NL including about 100 spots, most of them organised like a spot train. Among diff…

Globulin040301 veterinary sciencesGoat milk proteome 2D-DIGE Girgentana breed2D-DIGE; Girgentana breed; Goat milk proteome; Animal Science and ZoologyProteomics0403 veterinary scienceSettore AGR/17 - Zootecnica Generale E Miglioramento GeneticoLactationCaseinGirgentana breedmedicineGoat milk proteomeFood scienceBeta-lactoglobulinlcsh:SF1-1100Proteomic Profilebiology0402 animal and dairy science04 agricultural and veterinary sciences040201 dairy & animal scienceBreedmedicine.anatomical_structureProteomebiology.protein2D-DIGEAnimal Science and Zoologylcsh:Animal culture
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Nuclear magnetic resonance spectroscopic study of beta-lactoglobulin interactions with two flavor compounds, gamma-decalactone and beta-ionone.

2002

Interactions between a well-characterized protein, beta-lactoglobulin, and two flavor compounds, beta-ionone and gamma-decalactone, were studied by 2D NMR spectroscopy. NMR spectra were recorded in aqueous solution (pH 2.0, 12 mM NaCl, 10% D(2)O) under conditions such that beta-lactoglobulin is present in a monomeric state. TOCSY and NOESY spectra were recorded on the protein and the complexes between protein and ligands. The spectra of the NH-CH(alpha) region showed the cross-signals due to the coupling between N- and C-bonded protons in the polypeptide backbone. The observed chemical shift variations in the presence of ligands can be assigned to changes in the protein conformation. It app…

Models MolecularKetoneMagnetic Resonance SpectroscopyStereochemistryProtein ConformationLactoglobulinsIononechemistry.chemical_compoundLactonesSpectroscopyBeta-lactoglobulinFlavorchemistry.chemical_classificationBinding SitesbiologyMolecular StructureTerpenesGeneral ChemistryNuclear magnetic resonance spectroscopyNMR spectra databasechemistryOdorantsbiology.proteinPhysical chemistryGeneral Agricultural and Biological SciencesNorisoprenoidsTwo-dimensional nuclear magnetic resonance spectroscopyJournal of agricultural and food chemistry
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Controlled loading and release of beta-lactoglobulin in calcium-polygalacturonate hydrogels

2020

International audience; We show here how the structure of polygalacturonate (polyGalA) hydrogels cross-linked by Ca2+ cations via external gelation controls the loading and the release rate of betalactoglobulin (BLG), a globular protein. Hydrogels prepared from a polyGalA/BLG solution are found similar to those obtained from a polyGalA solution in our previous study (Maire du Poset, et al. Biomacromolecules 2019, 20(7), 2864-2872): they exhibit similar transparencies and gradients of mechanical properties and polyGalA concentration. The nominal BLG/polyGalA ratio of the mixtures is almost recovered within the whole mixed hydrogel despite such strong concentration gradients, except in the pa…

Polymers and Plastics[SDV]Life Sciences [q-bio]Beta-lactoglobulinBioengineeringLactoglobulinscalcium-polygalacturonatecomplex mixturesDiffusionBiomaterialsPolygalacturonateScattering Small AngleMaterials ChemistrystructureBeta-lactoglobulinbiologyChemistrytechnology industry and agriculturefood and beveragesglob (programming)HydrogelsproteinsCalcium polygalacturonateChemical engineeringSelf-healing hydrogelsbiology.proteinCalciumrelease rate of the loaded
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Thermal aggregation of beta-lactoglobulin in presence of metal ions.

2007

In this work, we report a study of the effects of zinc and copper ions on the heat-induced aggregation of beta-lactoglobulin (BLG). Kinetics investigations on aggregates growth by light scattering measurements and on secondary structure changes by FTIR absorption measurements show the different role played by the two metals during the whole process. In particular, the presence of zinc in solution promotes the formation of aggregates of BLG at a lower temperature than copper. Then, at fixed temperature, formation of a large amount of aggregates, of large dimension, is observed for Zn-BLG in shorter time; on the contrary, the presence of copper in solution does not affect the aggregation proc…

Protein DenaturationHot TemperatureCations DivalentMetal ions in aqueous solutionKineticsInorganic chemistryBiophysicsBeta-lactoglobulinchemistry.chemical_elementZincLactoglobulinsProtein aggregationBiochemistryProtein Structure SecondaryDivalentSpectroscopy Fourier Transform InfraredAnimalsMetal ionProtein secondary structurechemistry.chemical_classificationOrganic ChemistryLight scatteringCopperSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)FTIR spectroscopyKineticsZincchemistryChemical engineeringCattleAbsorption (chemistry)Protein aggregationCopperBiophysical chemistry
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Interaction between flavour compounds and beta-lactoglobulin: approach by NMR and 2D/3D-QSAR studies of ligands

2004

 author cannot archive publisher's version/PDF; International audience; Interactions between flavour compounds and beta-lactoglobulin (BLG) have been the subject of several studies, but there are no unanimous binding site explanations. In our laboratory, interactions between BLG, and two flavour compounds, beta-ionone and gamma-decalactone, were studied by 2D-NMR spectroscopy. It appears that several amino acids affected by binding of gamma-decalactone are buried in the central cavity, whereas binding of beta-ionone affects amino acids located in a groove near the outer surface of the protein. 2D/3D-QSAR studies were performed using QSAR+ module of Cerius2 and Catalyst. The QSAR equation pr…

Quantitative structure–activity relationshipAROMAMolecular modelStereochemistry01 natural sciences03 medical and health sciencesComputational chemistryMolecular descriptor[SDV.IDA]Life Sciences [q-bio]/Food engineeringFLAVOURBinding site030304 developmental biology3D-QSAR0303 health sciencesChemistryHydrogen bondLigand[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringGeneral Chemistry[SDV.IDA] Life Sciences [q-bio]/Food engineeringAffinitiesBETA-LACTOGLOBULIN0104 chemical sciences010404 medicinal & biomolecular chemistry2D-QSAR2D-NMRTwo-dimensional nuclear magnetic resonance spectroscopyFood Science
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2D- and 3D-QSAR Models of Interaction between Flavor Compounds and beta-Lactoglobulin Using Catalyst and Cerius2

2004

The present paper describes an application of Catalyst to three aroma sets (35, 24 and 21 compounds respectively) to generate activities-based alignments, using the best significant generated hypotheses. The obtained Catalyst models confirmed the existence of at least two binding sites on the BLG.

Quantitative structure–activity relationshipbiologyChemistryOrganic ChemistryDrug Discoverybiology.proteinOrganic chemistrybiology.organism_classificationBeta-lactoglobulinAromaFlavorComputer Science ApplicationsCatalysisQSAR & Combinatorial Science
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