Search results for "beta-Lactoglobulin"

showing 7 items of 27 documents

Cost action 96: interaction of food matrix with small ligands influencing flavour and texture

2000

International audience

[SDV.IDA]Life Sciences [q-bio]/Food engineering[SDV.IDA] Life Sciences [q-bio]/Food engineeringBETA-LACTOGLOBULINEComputingMilieux_MISCELLANEOUS
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Infrared spectroscopic study of beta-lactoglobulin interactions with flavor compounds

1999

International audience

[SDV] Life Sciences [q-bio]RAYONNEMENT INFRAROUGE[SDV]Life Sciences [q-bio]BETA-LACTOGLOBULINEComputingMilieux_MISCELLANEOUS
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2D- and 3D-QSAR models of interaction between flavor compounds and beta-lactoglobulin using catalyst and cerius

2004

International audience

[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process Engineering[SDV.IDA]Life Sciences [q-bio]/Food engineering[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringBETA-LACTOGLOBULINE[SDV.IDA] Life Sciences [q-bio]/Food engineeringComputingMilieux_MISCELLANEOUS
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Hydrophobic interactions between aroma compounds and beta-Lactoglobulin using a specific fluorescent probe and NMR

2008

International audience; Many aroma compounds are known to bind with proteins, and elucidating these bindind interactions is a key in a better knowledgment of flavour perception mechanisms (1). beta-Lactoglobulin (bLg), the major whey protein of milk, has been used as a model food protein in numerous studies. Previous work have shown different binding sites on bLg for aroma compounds as a function of their chemical class, and emphasized the importance of hydrophobic interactions (2). (...)

aroma bindingbeta-Lactoglobulinnmr spectroscopy[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process Engineeringfluorescent probe[SDV.IDA]Life Sciences [q-bio]/Food engineeringfood and beverages[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering[SDV.IDA] Life Sciences [q-bio]/Food engineeringhydrophobicity
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Thermal aggregation of proteins in presence of metal ions.

2008

The study of the aggregation processes in presence of metal ions is an essential step for understanding the key role of metals in protein-protein and protein-solvent interactions. Indeed, the presence of metal ions can radically change the main features of the standard denaturation/aggregation processes and such effects result to be strongly dependent on the kind of metal and on its concentration. Metal ions have an active role in thermal aggregation and cold set gelation processes. These processes are intrinsically different, but both are based on the proteins ability to form aggregates.

beta-LactoglobulinBovine Serum AlbuminProteins aggregation processeMetal IonConformational changeSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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Chemical and physical characterization of thermal aggregation of model proteins modulated by zinc(II) and copper(II) ions

2016

BACKGROUND: Metal ions are implicated in protein aggregation processes of several neurodegenerative pathologies, where the protein deposition occurs, and in the biotechnology field like the food technology where many processes in food manufacturing are based on thermal treatments. OBJECTIVE: The influence of Cu2+ or Zn2+ ions on the thermal aggregation process of Bovine beta-lactoglobulin (BLG) and Bovine Serum Albumin (BSA), two protein models, was studied with the aim of delineating the role of these ions in the protein aggregation kinetics and to clarify the related molecular mechanisms. METHODS: The protein structure changes were monitored by Raman spectroscopy, whereas the aggregate gr…

inorganic chemicals0301 basic medicineMetal ions in aqueous solutionKineticsInorganic chemistryBeta-lactoglobulinchemistry.chemical_elementZincProtein aggregation010402 general chemistry01 natural sciencesBovine Serum Albumin (BSA)Beta-lactoglobulin bovine serum albumin (BSA) copper and zinc ionsRaman spectroscopy dynamic light scatteringMetal03 medical and health sciencesProtein structureDynamic light scatteringcopper and zinc ionRadiology Nuclear Medicine and imagingcopper and zinc ionsBovine serum albuminBeta-lactoglobulin; Bovine Serum Albumin (BSA); copper and zinc ions; Raman spectroscopy; dynamic light scatteringbiologydigestive oral and skin physiologydynamic light scattering0104 chemical sciences030104 developmental biologychemistryvisual_artRaman spectroscopyBiophysicsbiology.proteinvisual_art.visual_art_medium
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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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