Solubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentration

dc.contributor.authorSantos, D. O.
dc.contributor.authorCoimbra, J. S. R.
dc.contributor.authorTeixeira, C. R.
dc.contributor.authorBarreto, S. L. T.
dc.contributor.authorSilva, M. C. H.
dc.contributor.authorGiraldo- Zuniga, A. D.
dc.date.accessioned2019-02-01T18:12:01Z
dc.date.available2019-02-01T18:12:01Z
dc.date.issued2015
dc.description.abstractThe solubility of proteins from quail egg white subjected to different agitation times, pH, and NaCl at 25 ◦ C was evaluated in this study. The greatest solubility achieved was obtained in the 0.05 mol/L of NaCl, pH 10.0, and under agitation for 1 h. The lowest solubility was found in the NaCl 1.0 mol/L, pH 3.0, and agitated for 2 h. Under the test conditions, aqueous solutions of NaCl 1.0 mol/L, pH 3.0, and agitated for 2 h may provide the greatest extraction index of proteins from quail egg white because these conditions promoted the protein precipitation in a large extension.en
dc.formatpdfpt-BR
dc.identifier.issn1532-2386
dc.identifier.urihttp://dx.doi.org/10.1080/10942912.2012.654557
dc.identifier.urihttp://www.locus.ufv.br/handle/123456789/23313
dc.language.isoengpt-BR
dc.publisherInternational Journal of Food Propertiespt-BR
dc.relation.ispartofseriesVolume 18, Issue 2, Pages 250- 258, 2015pt-BR
dc.rightsOpen Accesspt-BR
dc.subjectSolubilitypt-BR
dc.subjectEggpt-BR
dc.subjectProteinpt-BR
dc.subjectFunctional propertiespt-BR
dc.subjectPhpt-BR
dc.titleSolubility of proteins from quail (Coturnix coturnix japonica) egg white as affected by agitation time, pH, and salt concentrationen
dc.typeArtigopt-BR

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