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Título : | Stability of casein micelles cross-linked with genipin : a physicochemical study as a function of pH. |
Autor : | Casanova, Federico Silva, Naaman Francisco Nogueira Gaucheron, Frédéric Nogueira, Márcio Henrique Teixeira, Alvaro Vianna Novaes de Carvalho Perrone, Italo Tuler Alves, Maura Pinheiro Fidelis, Priscila Cardoso Carvalho, Antonio Fernandes de |
Fecha de publicación : | 2017 |
Citación : | CASANOVA, F. et al. Stability of casein micelles cross-linked with genipin : a physicochemical study as a function of pH. International Dairy Journal, v. 68, p. 70-74, maio 2017. Disponível em: <https://www.sciencedirect.com/science/article/pii/S0958694616303612>. Acesso em: 21 fev. 2019. |
Resumen : | 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 (ζ-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 °C or 87.5% (v/v) of ethanol. These results confirmed the hypothesis that cross-linking by GP increased the stability of CMs. |
URI : | http://www.repositorio.ufop.br/handle/123456789/10879 |
metadata.dc.identifier.uri2: | https://www.sciencedirect.com/science/article/pii/S0958694616303612 |
Aparece en las colecciones: | DEALI - Artigos publicados em periódicos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
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ARTIGO_StabilityCaseinMicelles.pdf Restricted Access | 347,14 kB | Adobe PDF | Visualizar/Abrir |
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