Stability of casein micelles cross-linked with genipin: a physicochemical study as a function of pH
| Autor: | Casanova, Federico, Silva, Naaman F. Nogueira, Gaucheron, Frédéric, Nogueira, Márcio H., Teixeira, Alvaro V. N. C., Perrone, Italo Tuler, Alves, Maura Pinhero, Fidelis, Priscila Cardoso, de Carvalho, Antônio F. |
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| Rok vydání: | 2017 |
| Předmět: | |
| Druh dokumentu: | Working Paper |
| DOI: | 10.1016/j.idairyj.2016.12.006 |
| Popis: | Chemical 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 2.0-7.0. The size and the charge ($\zeta$-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 2.0-3.0 or pH 4.5-7.0. 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 $^\circ$C or 87.5% (v/v) of ethanol. These results confirmed the hypothesis that cross-linking by GP increased the stability of CMs. Comment: 5 pages, 2 figures, International Dairy Journal, 2016 |
| Databáze: | arXiv |
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