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dc.date.accessioned 2022-09-14T16:42:41Z
dc.date.available 2022-09-14T16:42:41Z
dc.date.issued 2018-11-01
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/142074
dc.description.abstract The effects of thermal treatment (TT) and high hydrostatic pressure treatment (HHPT) on calcium-added soybean protein 1% (w/w) aqueous dispersions at pH 7.0 were compared. High hydrostatic pressure, but not thermal treatment, improved protein solubility and colloidal stability. Despite the fact that the glycinin solubility is more affected by calcium than that of β-conglycinin, glycinin could remain in dispersion in the presence of calcium when denatured by HHPT (calcium added before or after treatment), but not when denatured by TT or without denaturing treatment. Thus, polypeptide composition of soluble aggregates depended on type of treatment. Colloidal stability and molecular weight of soluble aggregates depended on the order of application of calcium and denaturing treatment: when calcium was present during either HHPT or TT, the dispersions had higher stability and higher proportion of soluble aggregates with high molecular weight than when calcium was added after treatments. After freeze drying and re-dispersing at higher protein content (10% w/w) calcium-added dispersions subjected to HHPT formed cold-set gels that were transparent and exhibited excellent water holding capacity. Our results provide the basis for the development of ready-to-use functional ingredients. en
dc.format.extent 69-79 es
dc.language en es
dc.subject Soybean proteins es
dc.subject Calcium addition es
dc.subject Functional foods es
dc.subject High hydrostatic pressure es
dc.subject Cold-set gelation es
dc.subject Reconstituted dispersions es
dc.title Thermal Versus High Hydrostatic Pressure Treatments on Calcium-added Soybean Proteins en
dc.type Articulo es
sedici.identifier.other doi:10.1007/s11483-018-9558-z es
sedici.identifier.issn 1557-1858 es
sedici.identifier.issn 1557-1866 es
sedici.title.subtitle Protein Solubility, Colloidal Stability and Cold-set Gelation en
sedici.creator.person Piccini, Lucía es
sedici.creator.person Scilingo, Adriana Alicia es
sedici.creator.person Speroni, Francisco es
sedici.subject.materias Ciencias Exactas es
sedici.description.fulltext true es
mods.originInfo.place Centro de Investigación y Desarrollo en Criotecnología de Alimentos es
sedici.subtype Articulo es
sedici.rights.license Creative Commons Attribution 4.0 International (CC BY 4.0)
sedici.rights.uri http://creativecommons.org/licenses/by/4.0/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle Food Biophysics es
sedici.relation.journalVolumeAndIssue vol. 14, no. 1 es


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Creative Commons Attribution 4.0 International (CC BY 4.0) Excepto donde se diga explícitamente, este item se publica bajo la siguiente licencia Creative Commons Attribution 4.0 International (CC BY 4.0)