dc.creatorQuiroga, Alejandra Viviana
dc.creatorAñón, María Cristina
dc.creatorPuppo, María Cecilia
dc.date2009-12-11
dc.date2022-10-11T17:14:24Z
dc.date.accessioned2023-07-15T05:12:40Z
dc.date.available2023-07-15T05:12:40Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/143566
dc.identifierissn:0003-021X
dc.identifierissn:1558-9331
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7472501
dc.descriptionThis study investigated, with the aim of obtaining more flexible and hydrophobic proteins, the attachment of a low chain fatty acid, decanoic acid, to alkaline and acid soybean proteins; and the effect on their conformational and functional properties. The extent of esterification was high at acid pH and also increased with heating. Protein solubility decreased, mainly at the highest temperature (60 °C). Increasing levels of fatty acid formed a complex with a slightly more soluble protein with less surface hydrophobicity. Esterified proteins exhibited aggregation/dissociation and were stabilized by different protein subunits belonging to 7S and 11S globulins. Denaturation of these soybean protein fractions (7S and 11S) were also detected in these complexes. The highest level of fatty acids favored formation of a more ordered protein structure.
dc.descriptionCentro de Investigación y Desarrollo en Criotecnología de Alimentos
dc.descriptionFacultad de Ciencias Agrarias y Forestales
dc.formatapplication/pdf
dc.format507-514
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.rightsCreative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.subjectQuímica
dc.subjectSoybean proteins
dc.subjectDecanoic acid Esterification
dc.subjectProtein structural changes
dc.subjectThermal behavior
dc.titleCharacterization of Soybean Proteins–Fatty Acid Systems
dc.typeArticulo
dc.typeArticulo


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