dc.creatorCasanova, Federico
dc.creatorSilva, Naaman F. Nogueira
dc.creatorGaucheron, Frédéric
dc.creatorNogueira, Márcio H.
dc.creatorTeixeira, Alvaro V. N. C.
dc.creatorPerrone, Italo Tuler
dc.creatorAlves, Maura Pinhero
dc.creatorFidelis, Priscila Cardoso
dc.creatorCarvalho, Antônio F. de
dc.date2018-08-28T16:33:19Z
dc.date2018-08-28T16:33:19Z
dc.date2017-05
dc.date.accessioned2023-09-27T20:56:03Z
dc.date.available2023-09-27T20:56:03Z
dc.identifier09586946
dc.identifierhttps://doi.org/10.1016/j.idairyj.2016.12.006
dc.identifierhttp://www.locus.ufv.br/handle/123456789/21488
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8951163
dc.descriptionChemical or enzymatic cross-linking of casein micelles (CMs) increases their stability against dissociating agents. In this paper, a comparative study of stability between native CMs and CMs cross-linked with genipin (CMs-GP) as a function of pH is described. Stability to temperature and ethanol were investigated in the pH range 2.0e7.0. The size and the charge ( z -potential) of the particles were determined by dynamic light scattering. Native CMs precipitated below pH 5.5; CMs-GP precipitated from pH 3.5 to 4.5, whereas no precipitation was observed at pH 2.0e3.0 or pH 4.5e7.0. The isoelectric point of CMs-GP was determined to be pH 3.7. Highest stability against heat and ethanol was observed for CMs-GP at pH 2, where visible coagulation was determined only after 800 s at 140 C or 87.5% (v/v) of ethanol. These results confirmed the hypothesis that cross-linking by GP increased the stability of CMs.
dc.formatpdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherInternational Dairy Journal
dc.relationv. 68, p. 70- 74, may 2017
dc.rightsElsevier Ltd.
dc.subjectFunction of pH
dc.subjectStability of casein micelles cross-linked
dc.titleStability of casein micelles cross-linked with genipin: A physicochemical study as a function of pH
dc.typeArtigo


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