Kinetics of Formation and Physicochemical Characterization of Thermally-Induced beta-Lactoglobulin Aggregates

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dc.contributor.authorZuniga, R. N.
dc.contributor.authorTolkach, A.
dc.contributor.authorKulozik, U.
dc.contributor.authorAguilera, J. M.
dc.date.accessioned2024-01-10T13:49:44Z
dc.date.available2024-01-10T13:49:44Z
dc.date.issued2010
dc.description.abstractThe kinetics of heat denaturation and aggregation for beta-lactoglobulin dispersions (5% w/v) were studied at 3 pHs (6, 6.4, and 6.8) and at a heating temperature of 80 degrees C. Protein aggregates were characterized for hydrodynamic diameter, microstructure, and molecular weight by means of dynamic light scattering, transmission electron microscopy, and polyacrylamide gel electrophoresis, respectively. Concentration of native beta-lactoglobulin decreased with holding time and with a decrease in the pH. Apparent rate constants were calculated for beta-lactoglobulin denaturation applying the general kinetic equation solved for a reaction order of 1.5. Values of the apparent reaction rate constant k = 7.5, 6.3 and 5.6 x 10(-3) s(-1) were found for pH 6, 6.4, and 6.8, respectively. Decreasing the pH of the dispersions produced higher aggregate sizes. After a holding time of 900 s, average hydrodynamic diameters for beta-lactoglobulin aggregates at pH 6, 6.4, and 6.8 were 96, 49, and 42 nm, respectively. These results were confirmed by transmission electron microscopy images, where a shift in the size and morphology of aggregates was found, from large and spherical at pH 6 to smaller and linear aggregates at pH 6.8. beta-Lactoglobulin formed disulfide-linked intermediates (dimers, trimers, tetramers) and so on) which then formed high molecular weight aggregates. From the results obtained by DLS, TEM, and SDS-PAGE a mechanism for beta-lactoglobulin aggregation was proposed. This study shows that heat treatment can be used to produce protein aggregates with different sizes and morphologies to be utilized as ingredients in foods.
dc.description.funderFondecyt
dc.description.funderNatl. Commission for Science and Technology (CONICYT)
dc.fechaingreso.objetodigital2024-05-14
dc.format.extent8 páginas
dc.fuente.origenWOS
dc.identifier.doi10.1111/j.1750-3841.2010.01617.x
dc.identifier.eissn1750-3841
dc.identifier.issn0022-1147
dc.identifier.pubmedidMEDLINE:20629872
dc.identifier.urihttps://doi.org/10.1111/j.1750-3841.2010.01617.x
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/79476
dc.identifier.wosidWOS:000279739700014
dc.information.autorucIngeniería;Aguilera JM;S/I;99054
dc.information.autorucIngeniería;Zúñiga RN;S/I;158150
dc.issue.numero5
dc.language.isoen
dc.nota.accesocontenido parcial
dc.publisherWILEY
dc.revistaJOURNAL OF FOOD SCIENCE
dc.rightsacceso restringido
dc.subjectaggregate size
dc.subjectbeta-lactoglobulin
dc.subjectdenaturation kinetics
dc.subjectelectrophoresis
dc.subjectheat treatment
dc.subjectrate constants
dc.subjecttransmission electron microscopy
dc.subjectHEAT-INDUCED AGGREGATION
dc.subjectWHEY PROTEINS
dc.subjectDENATURATION
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleKinetics of Formation and Physicochemical Characterization of Thermally-Induced beta-Lactoglobulin Aggregates
dc.typeartículo
dc.volumen75
sipa.codpersvinculados99054
sipa.codpersvinculados158150
sipa.indexWOS
sipa.indexScopus
sipa.trazabilidadCarga SIPA;09-01-2024
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