Stability of casein micelles cross-linked with genipin: A physicochemical study as a function of pH
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 wer...
| Autores: | , , , , , , , , |
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| Formato: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2017 |
| País: | Brasil |
| Recursos: | Universidade Federal de Viçosa (UFV) |
| Repositorio: | LOCUS Repositório Institucional da UFV |
| Idioma: | inglés |
| OAI Identifier: | oai:locus.ufv.br:123456789/21488 |
| Acesso em linha: | https://doi.org/10.1016/j.idairyj.2016.12.006 http://www.locus.ufv.br/handle/123456789/21488 |
| Access Level: | acceso abierto |
| Palavra-chave: | Function of pH Stability of casein micelles cross-linked |
| Resumo: | 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 2.0e7.0. 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. |
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