1. RODNA
  2. Universidad Nacional de Rosario. RepHipUNR
  3. Universidad Nacional de Rosario. RepHipUNR
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dc.provenanceUniversidad Nacional de Rosario.RepHipUNR-
dc.creatorHidalgo, María Eugenia-
dc.creatorFolmer Côrrea, Ana Paula-
dc.creatorMancilla Canales, Manuel Arturo-
dc.creatorDaroit, Daniel-
dc.creatorBrandelli, Adriano-
dc.creatorRisso, Patricia Hilda-
dc.date2014-07-31-
dc.date2014-07-31-
dc.date.accessioned2019-07-15T19:04:50Z-
dc.date.available2019-07-15T19:04:50Z-
dc.date.issued2014-07-31-
dc.date.issued2014-07-31-
dc.identifier1873-7137-
dc.identifierhttp://hdl.handle.net/2133/10477-
dc.identifierhttp://hdl.handle.net/2133/10477-
dc.identifier.urihttp://rodna.bn.gov.ar/jspui/handle/bnmm/570817-
dc.descriptionIn this work, we aimed at the production of bovine sodium caseinate (NaCAS) hydrolysates by means of an extracellular protease from Bacillus sp. P7. Mass spectrometry was carried out to evaluate peptide mass distribution and identified sequences of peptides with a signal/noise ratio higher than 10. Antioxidant and antimicrobial properties of hydrolysates were evaluated. An acid-induced aggregation process of the hydrolysates and their corresponding mixtures with NaCAS were also analyzed. The results showed that the enzymatic hydrolysis produced peptides, mostly lower than 3 kDa, with different bioactivities depending on the time of hydrolysis (ti). These hydrolysates lost their ability to aggregate by addition of glucono-delta-lactone, and their incorporation into NaCAS solutions alter the kinetics of the process. Also, the degree of compactness of the NaCAS aggregates, estimated by the fractal dimension of aggregates, was not significantly altered by the incorporation of hydrolysates. However, at higher protein concentrations, when the decrease in pH leads to the formation of NaCAS acid gels, the presence of hydrolysates alters the microstructure and rheological behavior of these gels.-
dc.descriptionFil: Hidalgo, María Eugenia. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Física Rosario (IFIR-CONICET); Argentina.-
dc.descriptionFil: Folmer Côrrea, Ana Paula. Universidade Federal de Rio Grande do Sul. Instituto de Ciência e Tecnologia de Alimentos; Brasil.-
dc.descriptionFil: Mancilla Canales, Manuel Arturo. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Física Rosario (IFIR-CONICET); Argentina.-
dc.descriptionFil: Daroit, Daniel. Universidade Federal da Fronteira Sul. Campus Cerro Largo; Brasil.-
dc.descriptionFil: Brandelli, Adriano. Universidade Federal de Rio Grande do Sul. Instituto de Ciência e Tecnologia de Alimentos; Brasil.-
dc.descriptionFil: Risso, Patricia Hilda. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Facultad de Ciencias Veterinarias. Instituto de Física Rosario (IFIR-CONICET); Argentina.-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherElsevier-
dc.relationhttps://www.sciencedirect.com/science/article/pii/S0268005X14002525-
dc.relationhttps://doi.org/10.1016/j.foodhyd.2014.07.009-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.sourcereponame:RepHipUNR (UNR)-
dc.sourceinstname:Universidad Nacional de Rosario-
dc.sourceinstacron:UNR-
dc.source.urihttp://hdl.handle.net/2133/10477-
dc.subjectBacillus sp. P7-
dc.subjectBovine Sodium Caseinate-
dc.subjectHydrolysates-
dc.subjectBioactivity-
dc.subjectAcid Aggregation and Gelation-
dc.subjectMicrostructure-
dc.titleBiological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeartículo-
dc.typeinfo:ar-repo/semantics/articulo-
Aparece en las colecciones: Universidad Nacional de Rosario. RepHipUNR

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